Enzyme Nomenclature

EC 2.4.1 (continued)

Hexosyltransferases

Continued from:
EC 2.4.1.1 to EC 2.4.1.50
EC 2.4.1.51 to EC 2.4.1.100
EC 2.4.1.101 to EC 2.4.1.150
EC 2.4.1.151 to EC 2.4.1.200
EC 2.4.1.201 to EC 2.4.1.250
EC 2.4.1.251 to EC 2.4.1.300

Contents

EC 2.4.1.301 2'-deamino-2'-hydroxyneamine 1-α-D-kanosaminyltransferase
EC 2.4.1.302 L-demethylnoviosyl transferase
EC 2.4.1.303 UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol β-1,3-galactosyltransferase
EC 2.4.1.304 UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol β-1,4-galactosyltransferase
EC 2.4.1.305 UDP-Glc:α-D-GlcNAc-glucosaminyl-diphosphoundecaprenol β-1,3-glucosyltransferase
EC 2.4.1.306 UDP-GalNAc:α-D-GalNAc-diphosphoundecaprenol α-1,3-N-acetylgalactosaminyltransferase
EC 2.4.1.307 now included with EC 2.4.1.122
EC 2.4.1.308 GDP-Fuc:β-D-Gal-1,3-α-D-GalNAc-1,3-α-GalNAc-diphosphoundecaprenol α-1,2-fucosyltransferase
EC 2.4.1.309 UDP-Gal:α-L-Fuc-1,2-β-Gal-1,3-α-GalNAc-1,3-α-GalNAc-diphosphoundecaprenol α-1,3-galactosyltransferase
EC 2.4.1.310 vancomycin aglycone glucosyltransferase
EC 2.4.1.311 chloroorienticin B synthase
EC 2.4.1.312 protein O-mannose β-1,4-N-acetylglucosaminyltransferase
EC 2.4.1.313 protein O-mannose β-1,3-N-acetylgalactosaminyltransferase
EC 2.4.1.314 ginsenoside Rd glucosyltransferase
EC 2.4.1.315 diglucosyl diacylglycerol synthase (1,6-linking)
EC 2.4.1.316 tylactone mycaminosyltransferase
EC 2.4.1.317 O-mycaminosyltylonolide 6-deoxyallosyltransferase
EC 2.4.1.318 demethyllactenocin mycarosyltransferase
EC 2.4.1.319 β-1,4-mannooligosaccharide phosphorylase
EC 2.4.1.320 1,4-β-mannosyl-N-acetylglucosamine phosphorylase
EC 2.4.1.321 cellobionic acid phosphorylase
EC 2.4.1.322 desvancosaminyl-vancomycin vancosaminetransferase
EC 2.4.1.323 7-deoxyloganetic acid glucosyltransferase
EC 2.4.1.324 7-deoxyloganetin glucosyltransferase
EC 2.4.1.325 TDP-N-acetylfucosamine:lipid II N-acetylfucosaminyltransferase
EC 2.4.1.326 aklavinone 7-β-L-rhodosaminyltransferase
EC 2.4.1.327 aclacinomycin-T 2-deoxy-L-fucose transferase
EC 2.4.1.328 erythronolide mycarosyltransferase
EC 2.4.1.329 sucrose 6F-phosphate phosphorylase
EC 2.4.1.330 β-D-glucosyl crocetin β-1,6-glucosyltransferase
EC 2.4.1.331 8-demethyltetracenomycin C L-rhamnosyltransferase
EC 2.4.1.332 1,2-α-glucosylglycerol phosphorylase
EC 2.4.1.333 1,2-β-oligoglucan phosphorylase
EC 2.4.1.334 1,3-α-oligoglucan phosphorylase
EC 2.4.1.335 dolichyl N-acetyl-α-D-glucosaminyl phosphate 3-β-D-2,3-diacetamido-2,3-dideoxy-β-D-glucuronosyltransferase
EC 2.4.1.336 monoglucosyldiacylglycerol synthase
EC 2.4.1.337 1,2-diacylglycerol 3-α-glucosyltransferase
EC 2.4.1.338 validoxylamine A glucosyltransferase
EC 2.4.1.339 β-1,2-mannobiose phosphorylase
EC 2.4.1.340 1,2-β-oligomannan phosphorylase
EC 2.4.1.341 α-1,2-colitosyltransferase
EC 2.4.1.342 α-maltose-1-phosphate synthase
EC 2.4.1.343 UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol α-1,3-galactosyltransferase
EC 2.4.1.344 type 2 galactoside α-(1,2)-fucosyltransferase
EC 2.4.1.345 phosphatidyl-myo-inositol α-mannosyltransferase
EC 2.4.1.346 phosphatidyl-myo-inositol dimannoside synthase
EC 2.4.1.347 α,α-trehalose-phosphate synthase (ADP-forming)
EC 2.4.1.348 N-acetyl-α-D-glucosaminyl-diphospho-ditrans, octacis-undecaprenol 3-α-mannosyltransferase
EC 2.4.1.349 mannosyl-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 3-α-mannosyltransferase
EC 2.4.1.350 mogroside IE synthase
EC 2.4.1.351 rhamnogalacturonan I rhamnosyltransferase
EC 2.4.1.352 glucosylglycerate phosphorylase
EC 2.4.1.353 sordaricin 6-deoxyaltrosyltransferase
EC 2.4.1.354 (R)-mandelonitrile β-glucosyltransferase
EC 2.4.1.355 poly(ribitol-phosphate) β-N-acetylglucosaminyltransferase
EC 2.4.1.356 glucosyl-dolichyl phosphate glucuronosyltransferase
EC 2.4.1.357 phlorizin synthase
EC 2.4.1.358 acylphloroglucinol glucosyltransferase
EC 2.4.1.359 glucosylglycerol phosphorylase (configuration-retaining)
EC 2.4.1.360 2-hydroxyflavanone C-glucosyltransferase
EC 2.4.1.361 GDP-mannose:di-myo-inositol-1,3'-phosphate β-1,2-mannosyltransferase
EC 2.4.1.362 α-(1→3) branching sucrase
EC 2.4.1.363 ginsenoside 20-O-glucosyltransferase
EC 2.4.1.364 protopanaxadiol-type ginsenoside 3-O-glucosyltransferase
EC 2.4.1.365 protopanaxadiol-type ginsenoside-3-O-glucoside 2"-O-glucosyltransferase
EC 2.4.1.366 ginsenoside F1 6-O-glucosyltransferase
EC 2.4.1.367 ginsenoside 6-O-glucosyltransferase
EC 2.4.1.368 oleanolate 3-O-glucosyltransferase

Entries

EC 2.4.1.301

Accepted name: 2'-deamino-2'-hydroxyneamine 1-α-D-kanosaminyltransferase

Reaction: (1) UDP-α-D-kanosamine + 2'-deamino-2'-hydroxyneamine = UDP + kanamycin A
(2) UDP-α-D-kanosamine + neamine = UDP + kanamycin B
(3) UDP-α-D-kanosamine + paromamine = UDP + kanamycin C
(4) UDP-α-D-kanosamine + 2'-deamino-2'-hydroxyparomamine = UDP + kanamycin X

For diagram of reaction click here.

Glossary: neamine = (1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl 2,6-diamino-2,6-dideoxy-α-D-glucopyranoside
paromamine = (1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl 2-amino-2-deoxy-α-D-glucopyranoside
UDP-α-D-kanosamine = uridine 5'-[3-(3-amino-3-deoxy-α-D-glucopyranosyl) diphosphate]
kanamycin A = (1S,2R,3R,4S,6R)-4,6-diamino-3-(6-amino-6-deoxy-α-D-glucopyranosyloxy)-2-hydroxycyclohexyl 3-amino-3-deoxy-α-D-glucopyranoside
kanamycin B = (1R,2S,3S,4R,6S)-4,6-diamino-3-(3-amino-3-deoxy-α-D-glucopyranosyloxy)-2-hydroxycyclohexyl 2,6-diamino-2,6-dideoxy-α-D-glucopyranoside
kanamycin C = (1R,2S,3S,4R,6S)-4,6-diamino-3-(3-amino-3-deoxy-α-D-glucopyranosyloxy)-2-hydroxycyclohexyl 2-amino-2-deoxy-α-D-glucopyranoside
kanamycin X = (1S,2R,3R,4S,6R)-4,6-diamino-3-(α-D-glucopyranosyloxy)-2-hydroxycyclohexyl 3-amino-3-deoxy-α-D-glucopyranoside

Other name(s): kanE (gene name); kanM2 (gene name)

Systematic name: UDP-α-D-kanosamine:2'-deamino-2'-hydroxyneamine 1-α-D-kanosaminyltransferase

Comments: Involved in the biosynthetic pathway of kanamycins. The enzyme characterized from the bacterium Streptomyces kanamyceticus can also accept UDP-α-D-glucose with lower efficiency [2].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Kudo, F., Sucipto, H. and Eguchi, T. Enzymatic activity of a glycosyltransferase KanM2 encoded in the kanamycin biosynthetic gene cluster. J. Antibiot. (Tokyo) 62 (2009) 707-710. [PMID: 19911031]

2. Sucipto, H., Kudo, F. and Eguchi, T. The last step of kanamycin biosynthesis: unique deamination reaction catalyzed by the α-ketoglutarate-dependent nonheme iron dioxygenase KanJ and the NADPH-dependent reductase KanK. Angew. Chem. Int. Ed. Engl. 51 (2012) 3428-3431. [PMID: 22374809]

[EC 2.4.1.301 created 2013]

EC 2.4.1.302

Accepted name: L-demethylnoviosyl transferase

Reaction: dTDP-4-O-demethyl-β-L-noviose + novobiocic acid = dTDP + demethyldecarbamoyl novobiocin

For diagram of reaction click here.

Glossary: novobiocic acid = N-(2,7-dihydroxy-8-methyl-4-oxo-4H-chromen-3-yl)-4-hydroxy-3-(3-methylbut-2-en-1-yl)benzamide
dTDP-4-O-demethyl-β-L-noviose = dTDP-6-deoxy-5-methyl-β-L-altropyranose = dTDP-(2S,3R,4R,5R)-6,6-dimethyltetrahydro-2H-pyran-2,3,4,5-tetraol
demethyldecarbamoyl novobiocin = N-{7-[(6-deoxy-5-methyl-β-D-gulopyranosyl)oxy]-4-hydroxy-8-methyl-2-oxo-2H-chromen-3-yl}-4-hydroxy-3-(3-methylbut-2-en-1-yl)benzamide

Other name(s): novM (gene name); dTDP-β-L-noviose:novobiocic acid 7-O-noviosyltransferase; L-noviosyl transferase

Systematic name: dTDP-4-O-demethyl-β-L-noviose:novobiocic acid 7-O-[4-O-demethyl-L-noviosyl]transferase

Comments: The enzyme is involved in the biosynthesis of the aminocoumarin antibiotic, novobiocin.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Freel Meyers, C.L., Oberthur, M., Anderson, J.W., Kahne, D. and Walsh, C.T. Initial characterization of novobiocic acid noviosyl transferase activity of NovM in biosynthesis of the antibiotic novobiocin. Biochemistry 42 (2003) 4179-4189. [PMID: 12680772]

2. Albermann, C., Soriano, A., Jiang, J., Vollmer, H., Biggins, J.B., Barton, W.A., Lesniak, J., Nikolov, D.B. and Thorson, J.S. Substrate specificity of NovM: implications for novobiocin biosynthesis and glycorandomization. Org. Lett. 5 (2003) 933-936. [PMID: 12633109]

[EC 2.4.1.302 created 2013, modified 2016]

EC 2.4.1.303

Accepted name: UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol β-1,3-galactosyltransferase

Reaction: UDP-α-D-galactose + N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + β-D-Gal-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol

Other name(s): WbbD; WbbD β3Gal-transferase; UDP-Gal:GlcNAc-R β1,3-galactosyltransferase; UDP-Gal:GlcNAcα-pyrophosphate-R β1,3-galactosyltransferase; UDP-Gal:GlcNAc-R galactosyltransferase

Systematic name: UDP-α-D-galactose:N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 3-β-galactosyltransferase (configuration-inverting)

Comments: The enzyme is involved in the the biosynthesis of the O-antigen repeating unit of Escherichia coli O7:K1 (VW187). Requires Mn2+. cf. EC 2.4.1.343, UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol α-1,3-galactosyltransferase.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Riley, J.G., Menggad, M., Montoya-Peleaz, P.J., Szarek, W.A., Marolda, C.L., Valvano, M.A., Schutzbach, J.S. and Brockhausen, I. The wbbD gene of E. coli strain VW187 (O7:K1) encodes a UDP-Gal: GlcNAcα-pyrophosphate-R β1,3-galactosyltransferase involved in the biosynthesis of O7-specific lipopolysaccharide. Glycobiology 15 (2005) 605-613. [PMID: 15625181]

2. Brockhausen, I., Riley, J.G., Joynt, M., Yang, X. and Szarek, W.A. Acceptor substrate specificity of UDP-Gal: GlcNAc-R β1,3-galactosyltransferase (WbbD) from Escherichia coli O7:K1. Glycoconj. J. 25 (2008) 663-673. [PMID: 18536883]

[EC 2.4.1.303 created 2013, modified 2017]

EC 2.4.1.304

Accepted name: UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol β-1,4-galactosyltransferase

Reaction: UDP-α-D-galactose + N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + β-D-Gal-(1→4)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol

Other name(s): WfeD; UDP-Gal:GlcNAc-R 1,4-Gal-transferase; UDP-Gal:GlcNAc-pyrophosphate-lipid β-1,4-galactosyltransferase

Systematic name: UDP-α-D-galactose:N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol β-1,4-galactosyltransferase

Comments: The enzyme is involved in the the biosynthesis of the O-polysaccharide repeating unit of the bacterium Shigella boydii B14. The activity is stimulated by Mn2+ or to a lesser extent by Mg2+, Ca2+, Ni2+ or Pb2+.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Xu, C., Liu, B., Hu, B., Han, Y., Feng, L., Allingham, J.S., Szarek, W.A., Wang, L. and Brockhausen, I. Biochemical characterization of UDP-Gal:GlcNAc-pyrophosphate-lipid β-1,4-Galactosyltransferase WfeD, a new enzyme from Shigella boydii type 14 that catalyzes the second step in O-antigen repeating-unit synthesis. J. Bacteriol. 193 (2011) 449-459. [PMID: 21057010]

[EC 2.4.1.304 created 2013]

EC 2.4.1.305

Accepted name: UDP-Glc:α-D-GlcNAc-glucosaminyl-diphosphoundecaprenol β-1,3-glucosyltransferase

Reaction: UDP-α-D-glucose + N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + β-D-Glc-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol

Other name(s): WfaP; WfgD; UDP-Glc:GlcNAc-pyrophosphate-lipid β-1,3-glucosyltransferase; UDP-Glc:GlcNAc-diphosphate-lipid β-1,3-glucosyltransferase

Systematic name: UDP-α-D-glucose:N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol β-1,3-glucosyltransferase

Comments: The enzyme is involved in the the biosynthesis of the O-polysaccharide repeating unit of the bacterium Escherichia coli serotype O56 and serotype O152.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Brockhausen, I., Hu, B., Liu, B., Lau, K., Szarek, W.A., Wang, L. and Feng, L. Characterization of two β-1,3-glucosyltransferases from Escherichia coli serotypes O56 and O152. J. Bacteriol. 190 (2008) 4922-4932. [PMID: 18487334]

[EC 2.4.1.305 created 2013]

EC 2.4.1.306

Accepted name: UDP-GalNAc:α-D-GalNAc-diphosphoundecaprenol α-1,3-N-acetylgalactosaminyltransferase

Reaction: UDP-N-acetyl-α-D-galactosamine + N-acetyl-α-D-galactosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + α-D-GalNAc-(1→3)-α-D-GalNAc-diphospho-ditrans,octacis-undecaprenol

Other name(s): WbnH

Systematic name: UDP-N-acetyl-α-D-galactosamine:N-acetyl-α-D-galactosaminyl-diphospho-ditrans,octacis-undecaprenol α-1,3-N-acetyl-D-galactosyltransferase

Comments: The enzyme is involved in the the biosynthesis of the O-polysaccharide repeating unit of Escherichia coli serotype O86.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Yi, W., Yao, Q., Zhang, Y., Motari, E., Lin, S. and Wang, P.G. The wbnH gene of Escherichia coli O86:H2 encodes an α-1,3-N-acetylgalactosaminyl transferase involved in the O-repeating unit biosynthesis. Biochem. Biophys. Res. Commun. 344 (2006) 631-639. [PMID: 16630548]

[EC 2.4.1.306 created 2013]

[EC 2.4.1.307 Deleted entry: UDP-Gal:α-D-GalNAc-1,3-α-D-GalNAc-diphosphoundecaprenol β-1,3-galactosyltransferase. Now included in EC 2.4.1.122, glycoprotein-N-acetylgalactosamine β-1,3-galactosyltransferase (EC 2.4.1.307 created 2013, deleted 2016)]

EC 2.4.1.308

Accepted name: GDP-Fuc:β-D-Gal-1,3-α-D-GalNAc-1,3-α-GalNAc-diphosphoundecaprenol α-1,2-fucosyltransferase

Reaction: GDP-β-L-fucose + β-D-Gal-(1→3)-α-D-GalNAc-(1→3)-α-D-GalNAc-diphospho-ditrans,octacis-undecaprenol = GDP + α-L-Fuc-(1→2)-β-D-Gal-(1→3)-α-D-GalNAc-(1→3)-α-D-GalNAc-diphospho-ditrans,octacis-undecaprenol

Other name(s): WbnK

Systematic name: GDP-β-L-fucose:β-D-Gal-(1→3)-α-D-GalNAc-(1→3)-α-D-GalNAc-diphospho-ditrans,octacis-undecaprenol α-1,2-fucosyltransferase

Comments: The enzyme is involved in the biosynthesis of the O-polysaccharide repeating unit of the bacterium Escherichia coli serotype O86.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Yi, W., Shao, J., Zhu, L., Li, M., Singh, M., Lu, Y., Lin, S., Li, H., Ryu, K., Shen, J., Guo, H., Yao, Q., Bush, C.A. and Wang, P.G. Escherichia coli O86 O-antigen biosynthetic gene cluster and stepwise enzymatic synthesis of human blood group B antigen tetrasaccharide. J. Am. Chem. Soc. 127 (2005) 2040-2041. [PMID: 15713070]

2. Woodward, R., Yi, W., Li, L., Zhao, G., Eguchi, H., Sridhar, P.R., Guo, H., Song, J.K., Motari, E., Cai, L., Kelleher, P., Liu, X., Han, W., Zhang, W., Ding, Y., Li, M. and Wang, P.G. In vitro bacterial polysaccharide biosynthesis: defining the functions of Wzy and Wzz. Nat. Chem. Biol. 6 (2010) 418-423. [PMID: 20418877]

[EC 2.4.1.308 created 2013]

EC 2.4.1.309

Accepted name: UDP-Gal:α-L-Fuc-1,2-β-Gal-1,3-α-GalNAc-1,3-α-GalNAc-diphosphoundecaprenol α-1,3-galactosyltransferase

Reaction: UDP-α-D-galactose + α-L-Fuc-(1→2)-β-D-Gal-(1→3)-α-D-GalNAc-(1→3)-α-D-GalNAc-diphospho-ditrans,octacis-undecaprenol = UDP + α-D-Gal-(1→3)-(α-L-Fuc-(1→2))-β-D-Gal-(1→3)-α-D-GalNAc-(1→3)-α-D-GalNAc-diphospho-ditrans,octacis-undecaprenol

Other name(s): WbnI

Systematic name: UDP-α-D-galactose:α-L-Fuc-(1→2)-β-D-Gal-(1→3)-α-D-GalNAc-(1→3)-α-D-GalNAc-diphospho-ditrans,octacis-undecaprenol α-1,3-galactosyltransferase

Comments: The enzyme is involved in the the biosynthesis of the O-polysaccharide repeating unit of the bacterium Escherichia coli serotype O86.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Yi, W., Shao, J., Zhu, L., Li, M., Singh, M., Lu, Y., Lin, S., Li, H., Ryu, K., Shen, J., Guo, H., Yao, Q., Bush, C.A. and Wang, P.G. Escherichia coli O86 O-antigen biosynthetic gene cluster and stepwise enzymatic synthesis of human blood group B antigen tetrasaccharide. J. Am. Chem. Soc. 127 (2005) 2040-2041. [PMID: 15713070]

2. Yi, W., Zhu, L., Guo, H., Li, M., Li, J. and Wang, P.G. Formation of a new O-polysaccharide in Escherichia coli O86 via disruption of a glycosyltransferase gene involved in O-unit assembly. Carbohydr. Res. 341 (2006) 2254-2260. [PMID: 16839526]

3. Woodward, R., Yi, W., Li, L., Zhao, G., Eguchi, H., Sridhar, P.R., Guo, H., Song, J.K., Motari, E., Cai, L., Kelleher, P., Liu, X., Han, W., Zhang, W., Ding, Y., Li, M. and Wang, P.G. In vitro bacterial polysaccharide biosynthesis: defining the functions of Wzy and Wzz. Nat. Chem. Biol. 6 (2010) 418-423. [PMID: 20418877]

[EC 2.4.1.309 created 2013]

EC 2.4.1.310

Accepted name: vancomycin aglycone glucosyltransferase

Reaction: UDP-α-D-glucose + vancomycin aglycone = UDP + devancoaminyl-vancomycin

For diagram of reaction, click here

Glossary: desvancoaminyl-vancomycin = vancomycin pseudoaglycone

Other name(s): GtfB (ambiguous)

Systematic name: UDP-α-D-glucose:vancomycin aglycone 48-O-β-glucosyltransferase

Comments: The enzyme from the bacterium Amycolatopsis orientalis is involved in the biosynthesis of the glycopeptide antibiotic chloroeremomycin.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Losey, H.C., Peczuh, M.W., Chen, Z., Eggert, U.S., Dong, S.D., Pelczer, I., Kahne, D. and Walsh, C.T. Tandem action of glycosyltransferases in the maturation of vancomycin and teicoplanin aglycones: novel glycopeptides. Biochemistry 40 (2001) 4745-4755. [PMID: 11294642]

2. Mulichak, A.M., Losey, H.C., Walsh, C.T. and Garavito, R.M. Structure of the UDP-glucosyltransferase GtfB that modifies the heptapeptide aglycone in the biosynthesis of vancomycin group antibiotics. Structure 9 (2001) 547-557. [PMID: 11470430]

[EC 2.4.1.310 created 2013]

EC 2.4.1.311

Accepted name: chloroorienticin B synthase

Reaction: dTDP-β-L-4-epi-vancosamine + desvancosaminyl-vancomycin = dTDP + chloroorienticin B

For diagram of reaction, click here

Glossary: dTDP-β-L-4-epi-vancosamine = dTDP-3-amino-2,3,6-trideoxy-3-methyl-β-L-arabino-hexopyranose
desvancosaminyl-vancomycin = vanomycin pseudoaglycone

Other name(s): GtfA

Systematic name: dTDP-L-4-epi-vancosamine:desvancosaminyl-vancomycin vancosaminyltransferase

Comments: The enzyme from the bacterium Amycolatopsis orientalis is involved in the biosynthesis of the glycopeptide antibiotic chloroeremomycin.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Mulichak, A.M., Losey, H.C., Lu, W., Wawrzak, Z., Walsh, C.T. and Garavito, R.M. Structure of the TDP-epi-vancosaminyltransferase GtfA from the chloroeremomycin biosynthetic pathway. Proc. Natl. Acad. Sci. USA 100 (2003) 9238-9243. [PMID: 12874381]

2. Lu, W., Oberthur, M., Leimkuhler, C., Tao, J., Kahne, D. and Walsh, C.T. Characterization of a regiospecific epivancosaminyl transferase GtfA and enzymatic reconstitution of the antibiotic chloroeremomycin. Proc. Natl. Acad. Sci. USA 101 (2004) 4390-4395. [PMID: 15070728]

[EC 2.4.1.311 created 2013]

EC 2.4.1.312

Accepted name: protein O-mannose β-1,4-N-acetylglucosaminyltransferase

Reaction: UDP-N-acetyl-α-D-glucosamine + 3-O-(α-D-mannosyl)-L-threonyl-[protein] = UDP + 3-O-[N-acetyl-β-D-glucosaminyl-(1→4)-α-D-mannosyl]-L-threonyl-[protein]

For diagram of reaction click here.

Other name(s): GTDC2 (gene name); POMGNT2

Systematic name: UDP-N-acetyl-α-D-glucosamine:α-D-mannosyl-threonyl-[protein] 4-β-N-acetyl-D-glucosaminyltransferase

Comments: The human protein is involved in the formation of a phosphorylated trisaccharide on a threonine residue of α-dystroglycan, an extracellular peripheral glycoprotein that acts as a receptor for extracellular matrix proteins containing laminin-G domains.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Yoshida-Moriguchi, T., Willer, T., Anderson, M.E., Venzke, D., Whyte, T., Muntoni, F., Lee, H., Nelson, S.F., Yu, L. and Campbell, K.P. SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function. Science 341 (2013) 896-899. [PMID: 23929950]

[EC 2.4.1.312 created 2013]

EC 2.4.1.313

Accepted name: protein O-mannose β-1,3-N-acetylgalactosaminyltransferase

Reaction: UDP-N-acetyl-α-D-galactosamine + 3-O-[N-acetyl-β-D-glucosaminyl-(1→4)-α-D-mannosyl]-L-threonyl-[protein] = UDP + 3-O-[N-acetyl-β-D-galactosaminyl-(1→3)-N-acetyl-β-D-glucosaminyl-(1→4)-α-D-mannosyl]-L-threonyl-[protein]

For diagram of reaction click here.

Other name(s): B3GALNT2

Systematic name: UDP-N-acetyl-α-D-galactosamine:N-acetyl-β-D-glucosaminyl-(1→4)-α-D-mannosyl-threonyl-[protein] 3-β-N-acetyl-D-galactosaminyltransferase

Comments: The human protein is specific for UDP-N-acetyl-α-D-galactosamine as donor [1]. The enzyme is involved in the formation of a phosphorylated trisaccharide on a threonine residue of α-dystroglycan, an extracellular peripheral glycoprotein that acts as a receptor for extracellular matrix proteins containing laminin-G domains.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Hiruma, T., Togayachi, A., Okamura, K., Sato, T., Kikuchi, N., Kwon, Y.D., Nakamura, A., Fujimura, K., Gotoh, M., Tachibana, K., Ishizuka, Y., Noce, T., Nakanishi, H. and Narimatsu, H. A novel human β1,3-N-acetylgalactosaminyltransferase that synthesizes a unique carbohydrate structure, GalNAcβ1-3GlcNAc. J. Biol. Chem. 279 (2004) 14087-14095. [PMID: 14724282]

2. Yoshida-Moriguchi, T., Willer, T., Anderson, M.E., Venzke, D., Whyte, T., Muntoni, F., Lee, H., Nelson, S.F., Yu, L. and Campbell, K.P. SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function. Science 341 (2013) 896-899. [PMID: 23929950]

[EC 2.4.1.313 created 2013]

EC 2.4.1.314

Accepted name: ginsenoside Rd glucosyltransferase

Reaction: UDP-α-D-glucose + ginsenoside Rd = UDP + ginsenoside Rb1

Glossary: ginsenoside Rd = 20-(β-D-glucopyranosyl)oxy-3β-[β-D-glucopyranosyl-(1→2)-β-D-glucopyranosyloxy]dammar-24-en-12β-ol
ginsenoside Rb1 = 3β-[β-D-glucopyranosyl-(1→2)-β-D-glucopyranosyloxy]-20-[β-D-glucopyranosyl-(1→6)-β-D-glucopyranosyloxy]dammar-24-en-12β-ol

For diagram of reaction click here.

Other name(s): UDPG:ginsenoside Rd glucosyltransferase; UDP-glucose:ginsenoside Rd glucosyltransferase; UGRdGT

Systematic name: UDP-glucose:ginsenoside-Rd β-1,6-glucosyltransferase

Comments: The glucosyl group forms a 1→6 bond to the glucosyloxy moiety at C-20 of ginsenoside Rd. Isolated from sanchi ginseng (Panax notoginseng).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Yue, C.-J. and Zhong J.-J. Purification and characterization of UDPG:ginsenoside Rd glucosyltransferase from suspended cells of Panax notoginseng. Process Biochem. 40 (2005) 3742-3748.

[EC 2.4.1.314 created 2013]

EC 2.4.1.315

Accepted name: diglucosyl diacylglycerol synthase (1,6-linking)

Reaction: (1) UDP-α-D-glucose + 1,2-diacyl-3-O-(β-D-glucopyranosyl)-sn-glycerol = 1,2-diacyl-3-O-[β-D-glucopyranosyl-(1→6)-O-β-D-glucopyranosyl]-sn-glycerol + UDP
(2) UDP-α-D-glucose + 1,2-diacyl-3-O-[β-D-glucopyranosyl-(1→6)-O-β-D-glucopyranosyl]-sn-glycerol = 1,2-diacyl-3-O-[β-D-glucopyranosyl-(1→6)-β-D-glucopyranosyl-(1→6)-O-β-D-glucopyranosyl]-sn-glycerol + UDP

Other name(s): monoglucosyl diacylglycerol (1→6) glucosyltransferase; MGlcDAG (1→6) glucosyltransferase; DGlcDAG synthase (ambiguous); UGT106B1; ypfP (gene name)

Systematic name: UDP-α-D-glucose:1,2-diacyl-3-O-(β-D-glucopyranosyl)-sn-glycerol 6-glucosyltransferase

Comments: The enzyme is found in several bacterial species. The enzyme from Bacillus subtilis is specific for glucose [1]. The enzyme from Mycoplasma genitalium can incoporate galactose with similar efficiency, but forms mainly 1,2-diacyl-diglucopyranosyl-sn-glycerol in vivo [3]. The enzyme from Staphylococcus aureus can also form glucosyl-glycero-3-phospho-(1′-sn-glycerol) [2].

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Jorasch, P., Wolter, F.P., Zahringer, U. and Heinz, E. A UDP glucosyltransferase from Bacillus subtilis successively transfers up to four glucose residues to 1,2-diacylglycerol: expression of ypfP in Escherichia coli and structural analysis of its reaction products. Mol. Microbiol. 29 (1998) 419-430. [PMID: 9720862]

2. Jorasch, P., Warnecke, D.C., Lindner, B., Zahringer, U. and Heinz, E. Novel processive and nonprocessive glycosyltransferases from Staphylococcus aureus and Arabidopsis thaliana synthesize glycoglycerolipids, glycophospholipids, glycosphingolipids and glycosylsterols. Eur. J. Biochem. 267 (2000) 3770-3783. [PMID: 10848996]

3. Andres, E., Martinez, N. and Planas, A. Expression and characterization of a Mycoplasma genitalium glycosyltransferase in membrane glycolipid biosynthesis: potential target against mycoplasma infections. J. Biol. Chem. 286 (2011) 35367-35379. [PMID: 21835921]

[EC 2.4.1.315 created 2014]

EC 2.4.1.316

Accepted name: tylactone mycaminosyltransferase

Reaction: tylactone + dTDP-α-D-mycaminose = dTDP + 5-O-β-D-mycaminosyltylactone

For diagram of reaction click here.

Glossary: tylactone = (4R,5S,6S,7S,9R,11E,13E,15S,16R)-7,16-diethyl-4,6-dihydroxy-5,9,13,15-tetramethyloxacyclohexadeca-11,13-diene-2,10-dione
dTDP-α-D-mycaminose = dTDP-3,6-dideoxy-3-dimethylamino-α-D-glucopyranose

Other name(s): tylM2 (gene name)

Systematic name: dTDP-α-D-mycaminose:tylactone 5-O-β-D-mycaminosyltransferase

Comments: The enzyme participates in the biosynthetic pathway of the macrolide antibiotic tylosin, which is produced by several species of Streptomyces bacteria. Activity is significantly enhanced by the presence of an accessory protein encoded by the tylM3 gene.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Gandecha, A.R., Large, S.L. and Cundliffe, E. Analysis of four tylosin biosynthetic genes from the tylLM region of the Streptomyces fradiae genome. Gene 184 (1997) 197-203. [PMID: 9031628]

2. Melancon, C.E., 3rd, Takahashi, H. and Liu, H.W. Characterization of tylM3/tylM2 and mydC/mycB pairs required for efficient glycosyltransfer in macrolide antibiotic biosynthesis. J. Am. Chem. Soc. 126 (2004) 16726-16727. [PMID: 15612702]

[EC 2.4.1.316 created 2014]

EC 2.4.1.317

Accepted name: O-mycaminosyltylonolide 6-deoxyallosyltransferase

Reaction: 5-O-β-D-mycaminosyltylonolide + dTDP-6-deoxy-α-D-allose = dTDP + demethyllactenocin

For diagram of reaction click here.

Glossary: mycaminose = 3,6-dideoxy-3-dimethylamino-glucopyranose
tylonolide = 2-[(4R,5S,6S,7R,9R,11E,13E,15R,16R)-16-ethyl-4,6-dihydroxy-15-(hydroxymethyl)-5,9,13-trimethyl-2,10-dioxooxacyclohexadeca-11,13-dien-7-yl]acetaldehyde
demethyllactenocin = [(2R,3R,4E,6E,9R,11R,12S,13S,14R)-12-{[3,6-dideoxy-3-(dimethylamino)-D-glucopyranosyl]oxy}-2-ethyl-14-hydroxy-5,9,13-trimethyl-8,16-dioxo-11-(2-oxoethyl)oxacyclohexadeca-4,6-dien-3-yl]methyl 6-deoxy-β-D-allopyranoside

Other name(s): tylN (gene name)

Systematic name: dTDP-6-deoxy-α-D-allose:5-O-β-D-mycaminosyltylonolide 23-O-6-deoxy-α-D-allosyltransferase

Comments: The enzyme participates in the biosynthetic pathway of the macrolide antibiotic tylosin, which is produced by several species of Streptomyces bacteria.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Wilson, V.T. and Cundliffe, E. Characterization and targeted disruption of a glycosyltransferase gene in the tylosin producer, Streptomyces fradiae. Gene 214 (1998) 95-100. [PMID: 9651492]

[EC 2.4.1.317 created 2014]

EC 2.4.1.318

Accepted name: demethyllactenocin mycarosyltransferase

Reaction: dTDP-β-L-mycarose + demethyllactenocin = dTDP + demethylmacrocin

For diagram of reaction click here.

Glossary: dTDP-β-L-mycarose = dTDP-2,6-dideoxy-3-C-methyl-β-L-ribo-hexose
demethyllactenocin = [(2R,3R,4E,6E,9R,11R,12S,13S,14R)-12-{[3,6-dideoxy-3-(dimethylamino)-D-glucopyranosyl]oxy}-2-ethyl-14-hydroxy-5,9,13-trimethyl-8,16-dioxo-11-(2-oxoethyl)oxacyclohexadeca-4,6-dien-3-yl]methyl 6-deoxy-D-allopyranoside

Other name(s): tylCV (gene name); tylC5 (gene name)

Systematic name: dTDP-β-L-mycarose:demethyllactenocin 4'-O-α-L-mycarosyltransferase

Comments: The enzyme participates in the biosynthetic pathway of the macrolide antibiotic tylosin, which is produced by several species of Streptomyces bacteria.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Bate, N., Butler, A.R., Smith, I.P. and Cundliffe, E. The mycarose-biosynthetic genes of Streptomyces fradiae, producer of tylosin. Microbiology 146 (2000) 139-146. [PMID: 10658660]

[EC 2.4.1.318 created 2014]

EC 2.4.1.319

Accepted name: β-1,4-mannooligosaccharide phosphorylase

Reaction: [(1→4)-β-D-mannosyl]n + phosphate = [(1→4)-β-D-mannosyl]n-1 + α-D-mannose 1-phosphate

Other name(s): RaMP2

Systematic name: 1,4-β-D-mannooligosaccharide::phosphate α-D-mannosyltransferase

Comments: The enzyme, isolated from the ruminal bacterium Ruminococcus albus, catalyses the reversible phosphorolysis of β-1,4-mannooligosaccharide with a minimum size of three monomers.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Kawahara, R., Saburi, W., Odaka, R., Taguchi, H., Ito, S., Mori, H. and Matsui, H. Metabolic mechanism of mannan in a ruminal bacterium, Ruminococcus albus, involving two mannoside phosphorylases and cellobiose 2-epimerase: discovery of a new carbohydrate phosphorylase, β-1,4-mannooligosaccharide phosphorylase. J. Biol. Chem. 287 (2012) 42389-42399. [PMID: 23093406]

[EC 2.4.1.319 created 2014]

EC 2.4.1.320

Accepted name: 1,4-β-mannosyl-N-acetylglucosamine phosphorylase

Reaction: 4-O-β-D-mannopyranosyl-N-acetyl-D-glucosamine + phosphate = N-acetyl-D-glucosamine + α-D-mannose 1-phosphate

Other name(s): BT1033

Systematic name: 4-O-β-D-mannopyranosyl-N-acetyl-D-glucosamine:phosphate α-D-mannosyltransferase

Comments: The enzyme isolated from the anaerobic bacterium Bacteroides thetaiotaomicron is involved in the degradation of host-derived N-glycans.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Nihira, T., Suzuki, E., Kitaoka, M., Nishimoto, M., Ohtsubo, K. and Nakai, H. Discovery of β-1,4-D-mannosyl-N-acetyl-D-glucosamine phosphorylase involved in the metabolism of N-glycans. J. Biol. Chem. 288 (2013) 27366-27374. [PMID: 23943617]

[EC 2.4.1.320 created 2014]

EC 2.4.1.321

Accepted name: cellobionic acid phosphorylase

Reaction: 4-O-β-D-glucopyranosyl-D-gluconate + phosphate = α-D-glucose 1-phosphate + D-gluconate

Glossary: 4-O-β-D-glucopyranosyl-D-gluconate = cellobionate

Systematic name: 4-O-β-D-glucopyranosyl-D-gluconate:phosphate α-D-glucosyltransferase

Comments: The enzyme occurs in cellulolytic bacteria and fungi. It catalyses the reversible phosphorolysis of cellobionic acid. In the synthetic direction it produces 4-O-β-D-glucopyranosyl-D-glucuronate from α-D-glucose 1-phosphate and D-glucuronate with low activity

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Nihira, T., Saito, Y., Nishimoto, M., Kitaoka, M., Igarashi, K., Ohtsubo, K. and Nakai, H. Discovery of cellobionic acid phosphorylase in cellulolytic bacteria and fungi. FEBS Lett 587 (2013) 3556-3561. [PMID: 24055472]

[EC 2.4.1.321 created 2014]

EC 2.4.1.322

Accepted name: devancosaminyl-vancomycin vancosaminetransferase

Reaction: dTDP-β-L-vancosamine + devancosaminyl-vancomycin = dTDP + vancomycin

For diagram of reaction click here.

Glossary: dTDP-β-L-vancosamine = dTDP-3-amino-2,3,6-trideoxy-3-C-methyl-β-L-lyxo-hexopyranose

Other name(s): devancosaminyl-vancomycin TDP-vancosaminyltransferase; GtfD; dTDP-β-L-vancomycin:desvancosaminyl-vancomycin β-L-vancosaminetransferase; desvancosaminyl-vancomycin vancosaminetransferase

Systematic name: dTDP-β-L-vancomycin:devancosaminyl-vancomycin β-L-vancosaminetransferase

Comments: The enzyme, isolated from the bacterium Amycolatopsis orientalis, catalyses the ultimate step in the biosynthesis of the antibiotic vancomycin.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Losey, H.C., Peczuh, M.W., Chen, Z., Eggert, U.S., Dong, S.D., Pelczer, I., Kahne, D. and Walsh, C.T. Tandem action of glycosyltransferases in the maturation of vancomycin and teicoplanin aglycones: novel glycopeptides. Biochemistry 40 (2001) 4745-4755. [PMID: 11294642]

2. Mulichak, A.M., Lu, W., Losey, H.C., Walsh, C.T. and Garavito, R.M. Crystal structure of vancosaminyltransferase GtfD from the vancomycin biosynthetic pathway: interactions with acceptor and nucleotide ligands. Biochemistry 43 (2004) 5170-5180. [PMID: 15122882]

[EC 2.4.1.322 created 2014]

EC 2.4.1.323

Accepted name: 7-deoxyloganetic acid glucosyltransferase

Reaction: UDP-α-D-glucose + 7-deoxyloganetate = UDP + 7-deoxyloganate

For diagram of reaction click here.

Other name(s): UGT8

Systematic name: UDP-α-D-glucose:7-deoxyloganetate O-D-glucosyltransferase

Comments: Isolated from the plant Catharanthus roseus (Madagascar periwinkle). Involved in loganin and secologanin biosynthesis. Does not react with 7-deoxyloganetin. cf. EC 2.4.1.324 7-deoxyloganetin glucosyltransferase.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Asada, K., Salim, V., Masada-Atsumi, S., Edmunds, E., Nagatoshi, M., Terasaka, K., Mizukami, H. and De Luca, V. A 7-deoxyloganetic acid glucosyltransferase contributes a key step in secologanin biosynthesis in madagascar periwinkle. Plant Cell 25 (2013) 4123-4134. [PMID: 24104568]

[EC 2.4.1.323 created 2014]

EC 2.4.1.324

Accepted name: 7-deoxyloganetin glucosyltransferase

Reaction: UDP-α-D-glucose + 7-deoxyloganetin = UDP + 7-deoxyloganin

For diagram of reaction click here.

Other name(s): UDPglucose:iridoid glucosyltransferase; UGT6; UGT85A24

Systematic name: UDP-α-D-glucose:7-deoxyloganetin O-D-glucosyltransferase

Comments: Isolated from the plants Catharanthus roseus (Madagascar periwinkle) and Gardenia jasminoides (cape jasmine). With Gardenia it also acts on genipin. Involved in loganin and secologanin biosynthesis. Does not react with 7-deoxyloganetate. cf. EC 2.4.1.323 7-deoxyloganetic acid glucosyltransferase.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Nagatoshi, M., Terasaka, K., Nagatsu, A. and Mizukami, H. Iridoid-specific glucosyltransferase from Gardenia jasminoides. J. Biol. Chem. 286 (2011) 32866-32874. [PMID: 21799001]

2. Asada, K., Salim, V., Masada-Atsumi, S., Edmunds, E., Nagatoshi, M., Terasaka, K., Mizukami, H. and De Luca, V. A 7-deoxyloganetic acid glucosyltransferase contributes a key step in secologanin biosynthesis in madagascar periwinkle. Plant Cell 25 (2013) 4123-4134. [PMID: 24104568]

[EC 2.4.1.324 created 2014]

EC 2.4.1.325

Accepted name: TDP-N-acetylfucosamine:lipid II N-acetylfucosaminyltransferase

Reaction: dTDP-4-acetamido-4,6-dideoxy-α-D-galactose + N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = dTDP + 4-acetamido-4,6-dideoxy-α-D-galactosyl-(1→4)-N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol

Glossary: dTDP-4-acetamido-4,6-dideoxy-α-D-galactose = dTDP-N-acetyl-α-D-fucosamine
a lipid II = an undecaprenyldiphospho-N-acetyl-(N-acetylglucosaminyl)muramoyl peptide; the peptide element refers to L-alanyl-D-γ-glutamyl-L-lysyl/meso-2,6-diaminopimelyl-D-alanyl-D-alanine or a modified version thereof = an undecaprenyldiphospho-4-O-(N-acetyl-β-D-glucosaminyl)-3-O-peptidyl-α-N-acetylmuramate; the peptide element refers to L-alanyl-D-γ-glutamyl-L-lysyl/meso-2,6-diaminopimelyl-D-alanyl-D-alanine or a modified version thereof
lipid III = N-acetyl-β-D-fucosyl-(1→4)-N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol

Other name(s): TDP-Fuc4NAc:lipid II Fuc4NAc-transferase; TDP-Fuc4NAc:lipid II Fuc4NAc transferase; wecF (gene name)

Systematic name: dTDP-N-acetyl-α-D-fucose:N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol N-acetylfucosaminyltransferase

Comments: Involved in the enterobacterial common antigen (ECA) biosynthesis in the bacterium Escherichia coli. The trisaccharide of the product (lipid III) is the repeat unit of ECA.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Rahman, A., Barr, K. and Rick, P.D. Identification of the structural gene for the TDP-Fuc4NAc:lipid II Fuc4NAc transferase involved in synthesis of enterobacterial common antigen in Escherichia coli K-12. J. Bacteriol. 183 (2001) 6509-6516. [PMID: 11673418]

[EC 2.4.1.325 created 2014]

EC 2.4.1.326

Accepted name: aklavinone 7-L-rhodosaminyltransferase

Reaction: dTDP-β-L-rhodosamine + aklavinone = dTDP + aclacinomycin T

For diagram of reaction click here.

Glossary: dTDP-β-L-rhodosamine = dTDP-2,3,6-trideoxy-3-dimethylamino-β-L-lyxo-hexose
aklavinone = methyl (1R,2R,4S)-2-ethyl-2,4,5,7-tetrahydroxy-6,11-dioxo-1,2,3,4,6,11-hexahydrotetracene-1-carboxylate
aclacinomycin T = 7-O-(α-L-rhodosaminyl)aklavinone

Other name(s): AknS/AknT; aklavinone 7-β-L-rhodosaminyltransferase; dTDP-β-L-rhodosamine:aklavinone 7-α-L-rhodosaminyltransferase

Systematic name: dTDP-β-L-rhodosamine:aklavinone 7-α-L-rhodosaminyltransferase (configuration-inverting)

Comments: Isolated from the bacterium Streptomyces galilaeus. Forms a complex with its accessory protein AknT, and has very low activity in its absence. The enzyme can also use dTDP-2-deoxy-β-L-fucose. Involved in the biosynthesis of other aclacinomycins.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Lu, W., Leimkuhler, C., Gatto, G.J., Jr., Kruger, R.G., Oberthur, M., Kahne, D. and Walsh, C.T. AknT is an activating protein for the glycosyltransferase AknS in L-aminodeoxysugar transfer to the aglycone of aclacinomycin A. Chem. Biol. 12 (2005) 527-534. [PMID: 15911373]

2. Leimkuhler, C., Fridman, M., Lupoli, T., Walker, S., Walsh, C.T. and Kahne, D. Characterization of rhodosaminyl transfer by the AknS/AknT glycosylation complex and its use in reconstituting the biosynthetic pathway of aclacinomycin A. J. Am. Chem. Soc. 129 (2007) 10546-10550. [PMID: 17685523]

[EC 2.4.1.326 created 2014, modified 2015]

EC 2.4.1.327

Accepted name: aclacinomycin-T 2-deoxy-L-fucose transferase

Reaction: dTDP-2-deoxy-β-L-fucose + aclacinomycin T = dTDP + aclacinomycin S

For diagram of reaction click here.

Glossary: idarubicin = (7S,9S)-9-acetyl-7-(3-amino-2,3,6-trideoxy-β-L-lyxo-hexosyloxy)-6,9,11-trihydroxy-7,8,9,10-tetrahydrotetracene-5,12-dione
aclacinomycin S = 7-O-(2-deoxy-α-L-fucosyl-(1→4)-rhodosaminyl)aklavinone
aclacinomycin T = 7-O-(α-L-rhodosaminyl)aklavinone

Other name(s): AknK

Systematic name: dTDP-2-deoxy-β-L-fucose:7-(α-L-rhodosaminyl)aklavinone 2-deoxy-α-L-fucosyltransferase

Comments: The enzyme, isolated from the bacterium Streptomyces galilaeus, is involved in the biosynthesis of other aclacinomycins. Also acts on idarubicin. It will slowly add a second 2-deoxy-L-fucose unit to aclacinomycin S in vitro.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Lu, W., Leimkuhler, C., Oberthur, M., Kahne, D. and Walsh, C.T. AknK is an L-2-deoxyfucosyltransferase in the biosynthesis of the anthracycline aclacinomycin A. Biochemistry 43 (2004) 4548-4558. [PMID: 15078101]

[EC 2.4.1.327 created 2014]

EC 2.4.1.328

Accepted name: erythronolide mycarosyltransferase

Reaction: dTDP-β-L-mycarose + erythronolide B = dTDP + 3-α-L-mycarosylerythronolide B

For diagram of reaction click here.

Glossary: dTDP-β-L-mycarose = dTDP-2,6-dideoxy-3-C-methyl-β-L-ribo-hexose
L-mycarose = 2,6-dideoxy-3-C-methyl-L-ribo-hexose

Other name(s): EryBV

Systematic name: dTDP-β-L-mycarose:erythronolide B L-mycarosyltransferase

Comments: Isolated from the bacterium Saccharopolyspora erythraea. The enzyme is involved in the biosynthesis of the antibiotic erythromycin.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Zhang, C., Fu, Q., Albermann, C., Li, L. and Thorson, J.S. The in vitro characterization of the erythronolide mycarosyltransferase EryBV and its utility in macrolide diversification. Chembiochem 8 (2007) 385-390. [PMID: 17262863]

[EC 2.4.1.328 created 2014]

EC 2.4.1.329

Accepted name: sucrose 6F-phosphate phosphorylase

Reaction: sucrose 6F-phosphate + phosphate = α-D-glucopyranose 1-phosphate + β-D-fructofuranose 6-phosphate

Other name(s): sucrose 6'-phosphate phosphorylase

Systematic name: sucrose 6F-phosphate:phosphate 1-α-D-glucosyltransferase

Comments: The enzyme, isolated from the thermophilic bacterium Thermoanaerobacterium thermosaccharolyticum, catalyses the reversible phosphorolysis of sucrose 6F-phosphate. It also acts on sucrose with lower activity.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Verhaeghe, T., Aerts, D., Diricks, M., Soetaert, W. and Desmet, T. The quest for a thermostable sucrose phosphorylase reveals sucrose 6'-phosphate phosphorylase as a novel specificity. Appl. Microbiol. Biotechnol. 98 (2014) 7027-7037. [PMID: 24599311]

[EC 2.4.1.329 created 2014]

EC 2.4.1.330

Accepted name: β-D-glucosyl crocetin β-1,6-glucosyltransferase

Reaction: (1) UDP-α-D-glucose + β-D-glucosyl crocetin = UDP + β-D-gentiobiosyl crocetin
(2) UDP-α-D-glucose + bis(β-D-glucosyl) crocetin = UDP + β-D-gentiobiosyl β-D-glucosyl crocetin
(3) UDP-α-D-glucose + β-D-gentiobiosyl β-D-glucosyl crocetin = UDP + crocin

For diagram of reaction click here.

Glossary: crocin = bis(β-D-gentiobiosyl) crocetin
crocetin = (2E,4E,6E,8E,10E,12E,14E)-2,6,11,15-tetramethylhexadeca-2,4,6,8,10,12,14-heptaenedioate

Other name(s): UGT94E5; UDP-glucose:crocetin glucosyl ester glucosyltransferasee

Systematic name: UDP-α-D-glucose:β-D-glucosyl crocetin β-1,6-glucosyltransferase

Comments: The enzyme, characterized from the plant Gardenia jasminoides, adds a glucose to several crocetin glycosyl esters, but not to crocetin (cf. EC 2.4.1.271, crocetin glucosyltransferase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Nagatoshi, M., Terasaka, K., Owaki, M., Sota, M., Inukai, T., Nagatsu, A. and Mizukami, H. UGT75L6 and UGT94E5 mediate sequential glucosylation of crocetin to crocin in Gardenia jasminoides. FEBS Lett 586 (2012) 1055-1061. [PMID: 22569263]

[EC 2.4.1.330 created 2014]

EC 2.4.1.331

Accepted name: 8-demethyltetracenomycin C L-rhamnosyltransferase

Reaction: dTDP-β-L-rhamnose + 8-demethyltetracenomycin C = dTDP + 8-demethyl-8-α-L-rhamnosyltetracenomycin C

For diagram of reaction click here.

Glossary: dTDP-β-L-rhamnose = dTDP-6-deoxy-β-L-mannose

Other name(s): elmGT

Systematic name: dTDP-β-L-rhamnose:8-demethyltetracenomycin C 3-α-L-rhamnosyltransferase

Comments: Isolated from Streptomyces olivaceus Tü2353. Involved in elloramycin biosynthesis. In vitro it can also utilize other 6-deoxy D- or L-hexoses.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Blanco, G., Patallo, E.P., Brana, A.F., Trefzer, A., Bechthold, A., Rohr, J., Mendez, C. and Salas, J.A. Identification of a sugar flexible glycosyltransferase from Streptomyces olivaceus, the producer of the antitumor polyketide elloramycin. Chem. Biol. 8 (2001) 253-263. [PMID: 11306350]

[EC 2.4.1.331 created 2014]

EC 2.4.1.332

Accepted name: 1,2-α-glucosylglycerol phosphorylase

Reaction: 2-O-α-D-glucopyranosyl-glycerol + phosphate = β-D-glucose 1-phosphate + glycerol

Other name(s): 2-O-α-D-glucopyranosylglycerol phosphorylase

Systematic name: 2-O-α-D-glucopyranosyl-glycerol:phosphate β-D-glucosyltransferase

Comments: The enzyme has been isolated from the bacterium Bacillus selenitireducens. In the absence of glycerol the enzyme produces α-D-glucopyranose and phosphate from β-D-glucopyranose 1-phosphate. In this reaction the glucosyl residue is transferred to a water molecule with an inversion of the anomeric conformation.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Nihira, T., Saito, Y., Ohtsubo, K., Nakai, H. and Kitaoka, M. 2-O-α-D-glucosylglycerol phosphorylase from Bacillus selenitireducens MLS10 possessing hydrolytic activity on β-D-glucose 1-phosphate. PLoS One 9 (2014) e86548. [PMID: 24466148]

2. Touhara, K.K., Nihira, T., Kitaoka, M., Nakai, H. and Fushinobu, S. Structural basis for reversible phosphorolysis and hydrolysis reactions of 2-O-α-glucosylglycerol phosphorylase. J. Biol. Chem. 289 (2014) 18067-18075. [PMID: 24828502]

[EC 2.4.1.332 created 2014]

EC 2.4.1.333

Accepted name: 1,2-β-oligoglucan phosphorylase

Reaction: [(1→2)-β-D-glucosyl]n + phosphate = [(1→2)-β-D-glucosyl]n-1 + α-D-glucose 1-phosphate

Systematic name: 1,2-β-D-glucan:phosphate α-D-glucosyltransferase

Comments: The enzyme has been isolated from the bacterium Listeria innocua. It catalyses the reversible phosphorolysis of β-(1→2)-D-glucans. The minimum length of the substrate for the phosphorolytic reaction is 3 D-glucose units. In the synthetic reaction starting from sophorose and α-D-glucose 1-phosphate the average polymerisation degree is 39.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Nakajima, M., Toyoizumi, H., Abe, K., Nakai, H., Taguchi, H. and Kitaoka, M. 1,2-β-Oligoglucan phosphorylase from Listeria innocua. PLoS One 9 (2014) e92353. [PMID: 24647662]

[EC 2.4.1.333 created 2014]

EC 2.4.1.334

Accepted name: 1,3-α-oligoglucan phosphorylase

Reaction: [(1→3)-α-D-glucosyl]n + phosphate = [(1→3)-α-D-glucosyl]n-1 + β-D-glucose 1-phosphate

Systematic name: 1,3-α-D-glucan:phosphate β-D-glucosyltransferase

Comments: The enzyme, isolated from the bacterium Clostridium phytofermentans, catalyses a reversible reaction. Substrates for the phosphorolytic reaction are α-1,3-linked oligoglucans with a polymerisation degree of 3 or more. Nigerose (i.e. 3-O-α-D-glucopyranosyl-D-glucopyranose) is not phosphorylyzed but can serve as substrate in the reverse direction (cf. EC 2.4.1.279, nigerose phosphorylase).

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Nihira, T., Nishimoto, M., Nakai, H., Ohtsubo, K., and Kitaoka, M. Characterization of two phosphorylases for α-1,3-oligoglucans from Clostridium phytofermentans. J. Appl. Glycosci. 61 (2014) 59-66.

[EC 2.4.1.334 created 2014]

EC 2.4.1.335

Accepted name: dolichyl N-acetyl-α-D-glucosaminyl phosphate 3-β-D-2,3-diacetamido-2,3-dideoxy-β-D-glucuronosyltransferase

Reaction: UDP-2,3-diacetamido-2,3-dideoxy-α-D-glucuronate + an archaeal dolichyl N-acetyl-α-D-glucosaminyl phosphate = UDP + an archaeal dolichyl 3-O-(2,3-diacetamido-2,3-dideoxy-β-D-glucuronsyl)-N-acetyl-α-D-glucosaminyl phosphate

Other name(s): AglC; UDP-Glc-2,3-diNAcA glycosyltransferase

Systematic name: UDP-2,3-diacetamido-2,3-dideoxy-α-D-glucuronate:dolichyl N-acetyl-α-D-glucosaminyl-phosphate 3-β-D-2,3-diacetamido-2,3-dideoxy-β-D-glucuronosyltransferase

Comments: The enzyme, characterized from the methanogenic archaeon Methanococcus voltae, participates in the N-glycosylation of proteins. Dolichol used by archaea is different from that used by eukaryotes. It is much shorter (C55-C60), it is α,ω-saturated and it may have additional unsaturated positions in the chain.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Larkin, A., Chang, M.M., Whitworth, G.E. and Imperiali, B. Biochemical evidence for an alternate pathway in N-linked glycoprotein biosynthesis. Nat. Chem. Biol. 9 (2013) 367-373. [PMID: 23624439]

[EC 2.4.1.335 created 2015]

EC 2.4.1.336

Accepted name: monoglucosyldiacylglycerol synthase

Reaction: UDP-α-D-glucose + a 1,2-diacyl-sn-glycerol = UDP + a 1,2-diacyl-3-O-(β-D-glucopyranosyl)-sn-glycerol

Glossary: a 1,2-diacyl-3-O-(β-D-glucopyranosyl)-sn-glycerol = a β-monoglucosyldiacylglycerol = a GlcDG

Other name(s): mgdA (gene name)

Systematic name: UDP-α-D-glucose:1,2-diacyl-sn-glycerol 3-β-D-glucosyltransferase

Comments: The enzymes from cyanobacteria are involved in the biosynthesis of galactolipids found in their photosynthetic membranes. The enzyme belongs to the GT2 family of configuration-inverting glycosyltranferases [2]. cf. EC 2.4.1.337, 1,2-diacylglycerol 3-α-glucosyltransferase.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Sato, N. and Murata, N. Lipid biosynthesis in the blue-green-alga (cyanobacterium), Anabaena variabilis. 3. UDP-glucose-diacylglycerol glucosyltransferase activity in vitro. Plant Cell Physiol. 23 (1982) 1115-1120.

2. Awai, K., Kakimoto, T., Awai, C., Kaneko, T., Nakamura, Y., Takamiya, K., Wada, H. and Ohta, H. Comparative genomic analysis revealed a gene for monoglucosyldiacylglycerol synthase, an enzyme for photosynthetic membrane lipid synthesis in cyanobacteria. Plant Physiol. 141 (2006) 1120-1127. [PMID: 16714404]

3. Yuzawa, Y., Shimojima, M., Sato, R., Mizusawa, N., Ikeda, K., Suzuki, M., Iwai, M., Hori, K., Wada, H., Masuda, S. and Ohta, H. Cyanobacterial monogalactosyldiacylglycerol-synthesis pathway is involved in normal unsaturation of galactolipids and low-temperature adaptation of Synechocystis sp. PCC 6803. Biochim. Biophys. Acta 1841 (2014) 475-483. [PMID: 24370445]

[EC 2.4.1.336 created 2015]

EC 2.4.1.337

Accepted name: 1,2-diacylglycerol 3-α-glucosyltransferase

Reaction: UDP-α-D-glucose + a 1,2-diacyl-sn-glycerol = UDP + a 1,2-diacyl-3-O-(α-D-glucopyranosyl)-sn-glycerol

Other name(s): mgs (gene name); UDP-glucose:diacylglycerol glucosyltransferase; UDP-glucose:1,2-diacylglycerol glucosyltransferase; uridine diphosphoglucose-diacylglycerol glucosyltransferase; UDP-glucose-diacylglycerol glucosyltransferase; UDP-glucose:1,2-diacylglycerol 3-D-glucosyltransferase; UDP-glucose:1,2-diacyl-sn-glycerol 3-D-glucosyltransferase; 1,2-diacylglycerol 3-glucosyltransferase (ambiguous)

Systematic name: UDP-α-D-glucose:1,2-diacyl-sn-glycerol 3-α-D-glucosyltransferase

Comments: The enzyme from the bacterium Acholeplasma laidlawii, which lacks a cell wall, produces the major non-bilayer lipid in the organism. The enzyme from the bacterium Agrobacterium tumefaciens acts under phosphate deprivation, generating glycolipids as surrogates for phospholipids. The enzyme belongs to the GT4 family of configuration-retaining glycosyltransferases. Many diacylglycerols with long-chain acyl groups can act as acceptors. cf. EC 2.4.1.336, monoglucosyldiacylglycerol synthase.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Karlsson, O.P., Dahlqvist, A., Vikstrom, S. and Wieslander, A. Lipid dependence and basic kinetics of the purified 1,2-diacylglycerol 3-glucosyltransferase from membranes of Acholeplasma laidlawii. J. Biol. Chem. 272 (1997) 929-936. [PMID: 8995384]

2. Li, L., Storm, P., Karlsson, O.P., Berg, S. and Wieslander, A. Irreversible binding and activity control of the 1,2-diacylglycerol 3-glucosyltransferase from Acholeplasma laidlawii at an anionic lipid bilayer surface. Biochemistry 42 (2003) 9677-9686. [PMID: 12911309]

3. Berg, S., Edman, M., Li, L., Wikstrom, M. and Wieslander, A. Sequence properties of the 1,2-diacylglycerol 3-glucosyltransferase from Acholeplasma laidlawii membranes. Recognition of a large group of lipid glycosyltransferases in eubacteria and archaea. J. Biol. Chem. 276 (2001) 22056-22063. [PMID: 11294844]

4. Semeniuk, A., Sohlenkamp, C., Duda, K. and Holzl, G. A bifunctional glycosyltransferase from Agrobacterium tumefaciens synthesizes monoglucosyl and glucuronosyl diacylglycerol under phosphate deprivation. J. Biol. Chem. 289 (2014) 10104-10114. [PMID: 24558041]

[EC 2.4.1.337 created 2015]

EC 2.4.1.338

Accepted name: validoxylamine A glucosyltransferase

Reaction: UDP-α-D-glucose + validoxylamine A = UDP + validamycin A

For diagram of reaction click here.

Glossary: validoxylamine A = (1S,2S,3R,6S)-4-(hydroxymethyl)-6-{[(1S,2S,3S,4R,5R)-2,3,4-trihydroxy-5-(hydroxymethyl)cyclohexyl]amino}cyclohex-4-ene-1,2,3-triol

Other name(s): vldK (gene name); valG (gene name)

Systematic name: UDP-α-D-glucose:validoxylamine-A D-glucosyltransferase

Comments: The enzyme, characterized from the bacterium Streptomyces hygroscopicus subsp. limoneus, catalyses the ultimate step in the biosynthesis of the antifungal agent validamycin A.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Bai, L., Li, L., Xu, H., Minagawa, K., Yu, Y., Zhang, Y., Zhou, X., Floss, H.G., Mahmud, T. and Deng, Z. Functional analysis of the validamycin biosynthetic gene cluster and engineered production of validoxylamine A. Chem. Biol. 13 (2006) 387-397. [PMID: 16632251]

2. Xu, H., Minagawa, K., Bai, L., Deng, Z. and Mahmud, T. Catalytic analysis of the validamycin glycosyltransferase (ValG) and enzymatic production of 4''-epi-validamycin A. J Nat Prod 71 (2008) 1233-1236. [PMID: 18563934]

[EC 2.4.1.338 created 2016]

EC 2.4.1.339

Accepted name: β-1,2-mannobiose phosphorylase

Reaction: β-D-mannopyranosyl-(1→2)-D-mannopyranose + phosphate = D-mannopyranose + α-D-mannose 1-phosphate

Systematic name: β-D-mannopyranosyl-(1→2)-D-mannopyranose:phosphate α-D-mannosyltransferase

Comments: The enzyme, originally characterized from the thermophilic anaerobic bacterium Thermoanaerobacter sp. X514, catalyses a reversible reaction. cf. EC 2.4.1.340, 1,2-β-oligomannan phosphorylase.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Chiku, K., Nihira, T., Suzuki, E., Nishimoto, M., Kitaoka, M., Ohtsubo, K. and Nakai, H. Discovery of two β-1,2-mannoside phosphorylases showing different chain-length specificities from Thermoanaerobacter sp. X-514. PLoS One 9 (2014) e114882. [PMID: 25500577]

2. Tsuda, T., Nihira, T., Chiku, K., Suzuki, E., Arakawa, T., Nishimoto, M., Kitaoka, M., Nakai, H. and Fushinobu, S. Characterization and crystal structure determination of β-1,2-mannobiose phosphorylase from Listeria innocua. FEBS Lett. 589 (2015) 3816-3821. [PMID: 26632508]

[EC 2.4.1.339 created 2016]

EC 2.4.1.340

Accepted name: 1,2-β-oligomannan phosphorylase

Reaction: [(1→2)-β-D-mannosyl]n + phosphate = [(1→2)-β-D-mannosyl]n-1 + α-D-mannose 1-phosphate

Systematic name: (1→2)-β-D-mannan:phosphate β-D-mannosyl transferase (configuration-inverting)

Comments: The enzyme, originally characterized from the thermophilic anaerobic bacterium Thermoanaerobacter sp. X514, catalyses a reversible reaction. In the synthetic direction it produces oligosaccharides with a degree of polymerization (DP) of 3, 4 and 5. The phosphorolysis reaction proceeds to completion, although activity is highest when the substrate has at least three residues. cf. EC 2.4.1.339, β-1,2-mannobiose phosphorylase.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Chiku, K., Nihira, T., Suzuki, E., Nishimoto, M., Kitaoka, M., Ohtsubo, K. and Nakai, H. Discovery of two β-1,2-mannoside phosphorylases showing different chain-length specificities from Thermoanaerobacter sp. X-514. PLoS One 9 (2014) e114882. [PMID: 25500577]

[EC 2.4.1.340 created 2016]

EC 2.4.1.341

Accepted name: α-1,2-colitosyltransferase

Reaction: GDP-β-L-colitose + β-D-galactopyranosyl-(1→3)-N-acetyl-D-glucosamine = GDP + α-L-colitosyl-(1→2)-β-D-galactosyl-(1→3)-N-acetyl-D-glucosamine

Glossary: β-D-galactopyranosyl-(1→3)-N-acetyl-D-glucosamine = lacto-N-biose

Other name(s): wbgN (gene name)

Systematic name: GDP-β-L-colitose:β-D-galactopyranosyl-(1→3)-N-acetyl-D-glucosamine L-colitosyltransferase (configuration-inverting)

Comments: The enzyme, characterized from the bacterium Escherichia coli O55:H7, participates in the biosynthesis of an O-antigen. The reaction involves anomeric inversion, and does not require any metal ions. The enzyme is highly specific towards the acceptor, exclusively recognizing lacto-N-biose, but can accept GDP-L-fucose as the donor with almost the same activity as with GDP-β-L-colitose.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Wu, Z., Zhao, G., Li, T., Qu, J., Guan, W., Wang, J., Ma, C., Li, X., Zhao, W., Wang, P.G. and Li, L. Biochemical characterization of an α1,2-colitosyltransferase from Escherichia coli O55:H7. Glycobiology (2015) . [PMID: 26703456]

[EC 2.4.1.341 created 2016]

EC 2.4.1.342

Accepted name: α-maltose-1-phosphate synthase

Reaction: ADP-α-D-glucose + α-D-glucose-1-phosphate = ADP + α-maltose-1-phosphate

Glossary: maltose = α-D-glucopyranosyl-(1→4)-D-glucose

Other name(s): glgM (gene name)

Systematic name: ADP-α-D-glucose:α-D-glucose-1-phosphate 4-α-D-glucosyltransferase (configuration-retaining)

Comments: The enzyme, found in Mycobacteria, can also use UDP-α-D-glucose with much lower catalytic efficiency.

References:

1. Koliwer-Brandl, H., Syson, K., van de Weerd, R., Chandra, G., Appelmelk, B., Alber, M., Ioerger, T.R., Jacobs, W.R., Jr., Geurtsen, J., Bornemann, S. and Kalscheuer, R. Metabolic network for the biosynthesis of intra- and extracellular α-glucans required for virulence of Mycobacterium tuberculosis. PLoS Pathog. 12 (2016) e1005768. [PMID: 27513637]

[EC 2.4.1.342 created 2016]

EC 2.4.1.343

Accepted name: UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol α-1,3-galactosyltransferase

Reaction: UDP-α-D-galactose + N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + α-D-Gal-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol

Other name(s): wclR (gene name)

Systematic name: UDP-α-D-galactose:N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 3-α-galactosyltransferase (configuration-retaining)

Comments: The enzyme is involved in the the biosynthesis of the O-antigen repeating unit of Escherichia coli O3. Requires a divalent metal ion (Mn2+, Mg2+ or Fe2+). cf. EC 2.4.1.303, UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol β-1,3-galactosyltransferase.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Chen, C., Liu, B., Xu, Y., Utkina, N., Zhou, D., Danilov, L., Torgov, V., Veselovsky, V. and Feng, L. Biochemical characterization of the novel α-1, 3-galactosyltransferase WclR from Escherichia coli O3. Carbohydr. Res. 430 (2016) 36-43. [PMID: 27196310]

[EC 2.4.1.343 created 2017]

EC 2.4.1.344

Accepted name: type 2 galactoside α-(1,2)-fucosyltransferase

Reaction: GDP-β-L-fucose + β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-R = GDP + α-L-fucosyl-(1→2)-β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-R

Other name(s): blood group H α-2-fucosyltransferase (ambiguous); guanosine diphosphofucose-galactoside 2-L-fucosyltransferase (ambiguous); α-(1→2)-L-fucosyltransferase (ambiguous); α-2-fucosyltransferase (ambiguous); α-2-L-fucosyltransferase (ambiguous); blood-group substance H-dependent fucosyltransferase (ambiguous); guanosine diphosphofucose-glycoprotein 2-α-fucosyltransferase (ambiguous); guanosine diphosphofucose-lactose fucosyltransferase; GDP fucose-lactose fucosyltransferase; guanosine diphospho-L-fucose-lactose fucosyltransferase; guanosine diphosphofucose-β-D-galactosyl-α-2-L-fucosyltransferase (ambiguous); guanosine diphosphofucose-galactosylacetylglucosaminylgalactosylglucosylceramide α-L-fucosyltransferase (ambiguous); guanosine diphosphofucose-glycoprotein 2-α-L-fucosyltransferase (ambiguous); H-gene-encoded β-galactoside α(1→2)fucosyltransferase; β-galactoside α(1→2)fucosyltransferase (ambiguous); GDP-L-fucose:lactose fucosyltransferase; GDP-β-L-fucose:β-D-galactosyl-R 2-α-L-fucosyltransferase (ambiguous); FUT1 (gene name); FUT2 (gene name)

Systematic name: GDP-β-L-fucose:β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-R α-(1,2)-L-fucosyltransferase (configuration-inverting)

Comments: The enzyme acts on a glycoconjugates where R (see reaction) is a glycoprotein or glycosphingolipid. The recognized moiety of the substrate is known as a type 2 histo-blood group antigen precursor disaccharide, and the action of the enzyme produces an H type 2 antigen. Humans possess two enzymes able to catalyse this reaction, encoded by the FUT1 and FUT2 genes (also known as the H and Secretor genes, respectively), but only FUT1 is expressed in red blood cells. cf. EC 2.4.1.69, type 1 galactoside α-(1,2)-fucosyltransferase.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Basu, S., Basu, M. and Chien, J.L. Enzymatic synthesis of a blood group H-related glycosphingolipid by an α-fucosyltransferase from bovine spleen. J. Biol. Chem. 250 (1975) 2956-2962. [PMID: 804484]

2. Grollman, A.P. GDP-L-fucose:lactose fucosyltransferase from mammary gland. Methods Enzymol. 8 (1966) 351-353.

3. Ernst, L.K., Rajan, V.P., Larsen, R.D., Ruff, M.M. and Lowe, J.B. Stable expression of blood group H determinants and GDP-L-fucose: β-D-galactoside 2-α-L-fucosyltransferase in mouse cells after transfection with human DNA. J. Biol. Chem. 264 (1989) 3436-3447. [PMID: 2464598]

4. Larsen, R.D., Ernst, L.K., Nair, R.P. and Lowe, J.B. Molecular cloning, sequence, and expression of a human GDP-L-fucose:β-D-galactoside 2-α-L-fucosyltransferase cDNA that can form the H blood group antigen. Proc. Natl. Acad. Sci. USA 87 (1990) 6674-6678. [PMID: 2118655]

[EC 2.4.1.344 created 2017]

EC 2.4.1.345

Accepted name: phosphatidyl-myo-inositol α-mannosyltransferase

Reaction: GDP-α-D-mannose + 1-phosphatidyl-1D-myo-inositol = GDP + 2-O-(α-D-mannosyl)-1-phosphatidyl-1D-myo-inositol

Glossary: 1-phosphatidyl-1D-myo-inositol = PtdIns

Other name(s): mannosyltransferase PimA; PimA; guanosine diphosphomannose-phosphatidyl-inositol α-mannosyltransferase (ambiguous)

Systematic name: GDP-α-D-mannose:1-phosphatidyl-1D-myo-inositol 2-α-D-mannosyltransferase (configuration-retaining)

Comments: Requires Mg2+. The enzyme, found in Corynebacteriales, is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIMs).

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Kordulakova, J., Gilleron, M., Mikusova, K., Puzo, G., Brennan, P.J., Gicquel, B. and Jackson, M. Definition of the first mannosylation step in phosphatidylinositol mannoside synthesis. PimA is essential for growth of mycobacteria. J. Biol. Chem. 277 (2002) 31335-31344. [PMID: 12068013]

2. Gu, X., Chen, M., Wang, Q., Zhang, M., Wang, B. and Wang, H. Expression and purification of a functionally active recombinant GDP-mannosyltransferase (PimA) from Mycobacterium tuberculosis H37Rv. Protein Expr. Purif. 42 (2005) 47-53. [PMID: 15939292]

3. Giganti, D., Albesa-Jove, D., Urresti, S., Rodrigo-Unzueta, A., Martinez, M.A., Comino, N., Barilone, N., Bellinzoni, M., Chenal, A., Guerin, M.E. and Alzari, P.M. Secondary structure reshuffling modulates glycosyltransferase function at the membrane. Nat. Chem. Biol. 11 (2015) 16-18. [PMID: 25402770]

4. Rodrigo-Unzueta, A., Martinez, M.A., Comino, N., Alzari, P.M., Chenal, A. and Guerin, M.E. Molecular basis of membrane association by the phosphatidylinositol mannosyltransferase PimA enzyme from Mycobacteria. J. Biol. Chem. 291 (2016) 13955-13963. [PMID: 27189944]

[EC 2.4.1.345 created 2017]

EC 2.4.1.346

Accepted name: phosphatidyl-myo-inositol dimannoside synthase

Reaction: (1) GDP-α-D-mannose + 2-O-α-D-mannosyl-1-phosphatidyl-1D-myo-inositol = GDP + 2,6-di-O-α-D-mannosyl-1-phosphatidyl-1D-myo-inositol
(2) GDP-α-D-mannose + 2-O-(6-O-acyl-α-D-mannosyl)-1-phosphatidyl-1D-myo-inositol = GDP + 2-O-(6-O-acyl-α-D-mannosyl)-6-O-α-D-mannosyl-1-phosphatidyl-1D-myo-inositol

Glossary: 1-phosphatidyl-1D-myo-inositol = PtdIns

Other name(s): mannosyltransferase PimB; PimB; guanosine diphosphomannose-phosphatidyl-inositol α-mannosyltransferase (ambiguous)

Systematic name: GDP-α-D-mannose:2-O-α-D-mannosyl-1-phosphatidyl-1D-myo-inositol 6-α-D-mannosyltransferase (configuration-retaining)

Comments: Requires Mg2+. The enzyme, found in Corynebacteriales, is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIMs).

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Guerin, M.E., Kaur, D., Somashekar, B.S., Gibbs, S., Gest, P., Chatterjee, D., Brennan, P.J. and Jackson, M. New insights into the early steps of phosphatidylinositol mannoside biosynthesis in mycobacteria: PimB' is an essential enzyme of Mycobacterium smegmatis. J. Biol. Chem. 284 (2009) 25687-25696. [PMID: 19638342]

2. Mishra, A.K., Batt, S., Krumbach, K., Eggeling, L. and Besra, G.S. Characterization of the Corynebacterium glutamicum Δ pimB' Δ mgtA double deletion mutant and the role of Mycobacterium tuberculosis orthologues Rv2188c and Rv0557 in glycolipid biosynthesis. J. Bacteriol. 191 (2009) 4465-4472. [PMID: 19395496]

3. Batt, S.M., Jabeen, T., Mishra, A.K., Veerapen, N., Krumbach, K., Eggeling, L., Besra, G.S. and Futterer, K. Acceptor substrate discrimination in phosphatidyl-myo-inositol mannoside synthesis: structural and mutational analysis of mannosyltransferase Corynebacterium glutamicum PimB'. J. Biol. Chem. 285 (2010) 37741-37752. [PMID: 20843801]

[EC 2.4.1.346 created 2017]

EC 2.4.1.347

Accepted name: α,α-trehalose-phosphate synthase (ADP-forming)

Reaction: ADP-α-D-glucose + D-glucose 6-phosphate = ADP + α,α-trehalose 6-phosphate

Other name(s): otsA (gene name); ADP-glucose —glucose-phosphate glucosyltransferase

Systematic name: ADP-α-D-glucose:D-glucose-6-phosphate 1-α-D-glucosyltransferase (configuration-retaining)

Comments: The enzyme has been reported from the yeast Saccharomyces cerevisiae and from mycobacteria. The enzyme from Mycobacterium tuberculosis can also use UDP-α-D-glucose, but the activity with ADP-α-D-glucose, which is considered the main substrate in vivo, is higher.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Ferreira, J.C., Thevelein, J.M., Hohmann, S., Paschoalin, V.M., Trugo, L.C. and Panek, A.D. Trehalose accumulation in mutants of Saccharomyces cerevisiae deleted in the UDPG-dependent trehalose synthase-phosphatase complex. Biochim. Biophys. Acta 1335 (1997) 40-50. [PMID: 9133641]

2. Pan, Y.T., Carroll, J.D. and Elbein, A.D. Trehalose-phosphate synthase of Mycobacterium tuberculosis. Cloning, expression and properties of the recombinant enzyme. Eur. J. Biochem. 269 (2002) 6091-6100. [PMID: 12473104]

3. Asencion Diez, M.D., Demonte, A.M., Syson, K., Arias, D.G., Gorelik, A., Guerrero, S.A., Bornemann, S. and Iglesias, A.A. Allosteric regulation of the partitioning of glucose-1-phosphate between glycogen and trehalose biosynthesis in Mycobacterium tuberculosis. Biochim. Biophys. Acta 1850 (2015) 13-21. [PMID: 25277548]

[EC 2.4.1.347 created 2017]

EC 2.4.1.348

Accepted name: N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 3-α-mannosyltransferase

Reaction: GDP-α-D-mannose + N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = GDP + α-D-mannosyl-(1→3)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol

Other name(s): WbdC

Systematic name: GDP-α-D-mannose:N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 3-α-mannosyltransferase (configuration-retaining)

Comments: The enzyme is involved in the biosynthesis of the linker region of the polymannose O-polysaccharide in the outer leaflet of the membrane of Escherichia coli serotypes O8, O9 and O9a.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Greenfield, L.K., Richards, M.R., Li, J., Wakarchuk, W.W., Lowary, T.L. and Whitfield, C. Biosynthesis of the polymannose lipopolysaccharide O-antigens from Escherichia coli serotypes O8 and O9a requires a unique combination of single- and multiple-active site mannosyltransferases. J. Biol. Chem. 287 (2012) 35078-35091. [PMID: 22875852]

[EC 2.4.1.348 created 2017]

EC 2.4.1.349

Accepted name: mannosyl-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 3-α-mannosyltransferase

Reaction: 2 GDP-α-D-mannose + α-D-mannosyl-(1→3)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = 2 GDP + α-D-mannosyl-(1→3)-α-D-mannosyl-(1→3)-α-D-mannosyl-(1→3)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol

Other name(s): WbdB

Systematic name: GDP-α-D-mannose:α-D-mannosyl-(1→3)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 3-α-mannosyltransferase (configuration-retaining)

Comments: The enzyme is involved in the biosynthesis of the linker region of the polymannose O-polysaccharide in the outer leaflet of the membrane of Escherichia coli serotypes O8, O9 and O9a. It has no activity with N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol (cf. EC 2.4.1.348, N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 3-α-mannosyltransferase).

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Greenfield, L.K., Richards, M.R., Li, J., Wakarchuk, W.W., Lowary, T.L. and Whitfield, C. Biosynthesis of the polymannose lipopolysaccharide O-antigens from Escherichia coli serotypes O8 and O9a requires a unique combination of single- and multiple-active site mannosyltransferases. J. Biol. Chem. 287 (2012) 35078-35091. [PMID: 22875852]

[EC 2.4.1.349 created 2017]

EC 2.4.1.350

Accepted name: mogroside IE synthase

Reaction: UDP-α-D-glucose + mogrol = mogroside IE + UDP

Glossary: mogrol = (23R)-cucurbit-5-ene-3β,11α,23,25-tetraol

Other name(s): UGT74AC1; mogrol C-3 hydroxyl glycosyltransferase

Systematic name: UDP-α-D-glucose:mogrol 3-O-glucosyltransferase

Comments: Isolated from the plant Siraitia grosvenorii (monk fruit).

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Dai, L., Liu, C., Zhu, Y., Zhang, J., Men, Y., Zeng, Y. and Sun, Y. Functional characterization of cucurbitadienol synthase and triterpene glycosyltransferase involved in biosynthesis of mogrosides from Siraitia grosvenorii. Plant Cell Physiol 56 (2015) 1172-1182. [PMID: 25759326]

[EC 2.4.1.350 created 2017]

EC 2.4.1.351

Accepted name: rhamnogalacturonan I rhamnosyltransferase

Reaction: UDP-β-L-rhamnose + α-D-galacturonosyl-[(1→2)-α-L-rhamnosyl-(1→4)-α-D-galacturonosyl]n = UDP + [(1→2)-α-L-rhamnosyl-(1→4)-α-D-galacturonosyl]n+1

Other name(s): RRT; RG I rhamnosyltransferase

Systematic name: UDP-β-L-rhamnose:rhamnogalacturonan I 4-rhamnosyltransferase (configuration-inverting)

Comments: The enzyme, characterized from Vigna angularis (azuki beans), participates in the biosynthesis of rhamnogalacturonan type I. It does not require any metal ions, and prefers substrates with a degree of polymerization larger than 7.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Uehara, Y., Tamura, S., Maki, Y., Yagyu, K., Mizoguchi, T., Tamiaki, H., Imai, T., Ishii, T., Ohashi, T., Fujiyama, K. and Ishimizu, T. Biochemical characterization of rhamnosyltransferase involved in biosynthesis of pectic rhamnogalacturonan I in plant cell wall. Biochem. Biophys. Res. Commun. 486 (2017) 130-136. [PMID: 28283389]

[EC 2.4.1.351 created 2018]

EC 2.4.1.352

Accepted name: glucosylglycerate phosphorylase

Reaction: 2-O-(α-D-glucopyranosyl)-D-glycerate + phosphate = α-D-glucopyranose 1-phosphate + D-glycerate

Systematic name: 2-O-(α-D-glucopyranosyl)-D-glycerate:phosphate α-D-glucosyltransferase (configuration-retaining)

Comments: The enzyme has been characterized from the bacterium Meiothermus silvanus.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Franceus, J., Pinel, D. and Desmet, T. Glucosylglycerate phosphorylase, an enzyme with novel specificity involved in compatible solute metabolism. Appl. Environ. Microbiol. 83 (2017) . [PMID: 28754708]

[EC 2.4.1.352 created 2018]

EC 2.4.1.353

Accepted name: sordaricin 6-deoxyaltrosyltransferase

Reaction: GDP-6-deoxy-α-D-altrose + sordaricin = 4'-O-demethylsordarin + GDP

For diagram of reaction click here.

Glossary: sordaricin = (1R,3aR,4S,4aR,7R,7aR,8aR)-4-formyl-8a-(hydroxymethyl)-7-methyl-3-(propan-2-yl)-1,3a,4,4a,5,6,7,7a,8,8-decahydro-1,4-methanocyclopenta[f]indene-3a-carboxylic acid

Other name(s): SdnJ

Systematic name: GDP-6-deoxy-α-D-altrose:sordaricin 6-deoxy-D-altrosyltransferase

Comments: The enzyme, isolated from the fungus Sordaria araneosa, is involved in the biosynthesis of the glycoside antibiotic sordarin.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Kudo, F., Matsuura, Y., Hayashi, T., Fukushima, M. and Eguchi, T. Genome mining of the sordarin biosynthetic gene cluster from Sordaria araneosa Cain ATCC 36386: characterization of cycloaraneosene synthase and GDP-6-deoxyaltrose transferase. J. Antibiot. (Tokyo) 69 (2016) 541-548. [PMID: 27072286]

[EC 2.4.1.353 created 2018]

EC 2.4.1.354

Accepted name: (R)-mandelonitrile β-glucosyltransferase

Reaction: UDP-α-D-glucose + (R)-mandelonitrile = UDP + (R)-prunasin

Glossary: (R)-mandelonitrile = (2R)-hydroxy(phenyl)acetonitrile
(R)-prunasin = (2R)-(β-D-glucosyloxy)(phenyl)acetonitrile

Other name(s): UGT85A19 (gene name)

Systematic name: UDP-α-D-glucose:(R)-mandelonitrile β-D-glucosyltransferase (configuration-inverting)

Comments: The enzyme, characterized from Prunus dulcis (almond), is involved in the biosynthesis of the cyanogenic glycosides (R)-prunasin and (R)-amygdalin.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Franks, T. K., Yadollahi, A., Wirthensohn, M. G., Guerin, J. R., Kaiser, B. N., Sedgley, M. and Ford, C. M. A seed coat cyanohydrin glucosyltransferase is associated with bitterness in almond (Prunus dulcis) kernels. Funct. Plant Biol. 35 (2008) 236-246.

[EC 2.4.1.354 created 2018]

EC 2.4.1.355

Accepted name: poly(ribitol-phosphate) β-N-acetylglucosaminyltransferase

Reaction: n UDP-N-acetyl-α-D-glucosamine + 4-O-(D-ribitylphospho)n-di[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = n UDP + 4-O-(2-N-acetyl-β-D-glucosaminyl-D-ribitylphospho)n-di[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol

Other name(s): TarS

Systematic name: UDP-N-acetyl-α-D-glucosamine:4-O-(D-ribitylphospho)n-di[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol β-N-acetyl-D-glucosaminyltransferase (configuration-inverting)

Comments: Involved in the biosynthesis of poly(ribitol-phosphate) teichoic acids in the cell wall of the bacterium Staphylococcus aureus. This enzyme adds an N-acetyl-β-D-glucosamine to the OH group at the 2 position of the ribitol phosphate units. cf. EC 2.4.1.70 [poly(ribitol-phosphate) α-N-acetylglucosaminyltransferase].

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Nathenson, S. G., Strominger, J. L. Enzymatic synthesis of N-acetylglucosaminylribitol linkages in teichoic acid from Staphylococcus aureus, strain Copenhagen. J. Biol. Chem. 238 (1963) 3161-3169. [PMID: 14085356]

2. Brown, S., Xia, G., Luhachack, L.G., Campbell, J., Meredith, T.C., Chen, C., Winstel, V., Gekeler, C., Irazoqui, J.E., Peschel, A. and Walker, S. Methicillin resistance in Staphylococcus aureus requires glycosylated wall teichoic acids. Proc. Natl Acad. Sci. USA 109 (2012) 18909-18914. [PMID: 23027967]

3. Sobhanifar, S., Worrall, L.J., King, D.T., Wasney, G.A., Baumann, L., Gale, R.T., Nosella, M., Brown, E.D., Withers, S.G. and Strynadka, N.C. Structure and mechanism of Staphylococcus aureus TarS, the wall teichoic acid β-glycosyltransferase involved in methicillin resistance. PLoS Pathog. 12 (2016) e1006067. [PMID: 27973583]

[EC 2.4.1.355 created 2018]

EC 2.4.1.356

Accepted name: glucosyl-dolichyl phosphate glucuronosyltransferase

Reaction: UDP-α-D-glucuronate + an archaeal dolichyl α-D-glucosyl phosphate = UDP + an archaeal dolichyl β-D-glucuronosyl-(1→4)-α-D-glucosyl phosphate

Other name(s): aglG (gene name)

Systematic name: UDP-α-D-glucuronate:dolichyl phosphate glucuronosyltransferase (configuration-inverting)

Comments: The enzyme, characterized from the halophilic archaeon Haloferax volcanii, participates in the protein N-glycosylation pathway. Dolichol used by archaea is different from that used by eukaryotes. It is much shorter (C55-C60) and is α,ω-saturated. However, in vitro the enzyme was also able to act on a substrate with an unsaturated end.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Yurist-Doutsch, S., Abu-Qarn, M., Battaglia, F., Morris, H.R., Hitchen, P.G., Dell, A. and Eichler, J. aglF, aglG and aglI, novel members of a gene island involved in the N-glycosylation of the Haloferax volcanii S-layer glycoprotein. Mol. Microbiol. 69 (2008) 1234-1245. [PMID: 18631242]

2. Elharar, Y., Podilapu, A.R., Guan, Z., Kulkarni, S.S. and Eichler, J. Assembling glycan-charged dolichol phosphates: chemoenzymatic synthesis of a Haloferax volcanii N-glycosylation pathway intermediate. Bioconjug Chem 28 (2017) 2461-2470. [PMID: 28809486]

[EC 2.4.1.356 created 2018]

EC 2.4.1.357

Accepted name: phlorizin synthase

Reaction: UDP-α-D-glucose + phloretin = UDP + phlorizin

For diagram of reaction click here.

Glossary: phloretin = 3-(4-hydroxyphenyl)-1-(2,4,6-trihydroxyphenyl)propan-1-one
phlorizin = 3-(4-hydroxyphenyl)-1-[2-(β-D-glucopyranosyloxy)-4,6-dihydroxyphenyl]propan-1-one

Other name(s): MdPGT1: P2’GT

Systematic name: UDP-α-D-glucose:phloretin 2'-O-D-glucosyltransferase

Comments: Isolated from Malus X domestica (apple). Phlorizin inhibits sodium-linked glucose transporters. It gives the characteristic flavour of apples and cider.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Jugdé, H., Nguy, D., Moller, I., Cooney, J.M. and Atkinson, R.G. Isolation and characterization of a novel glycosyltransferase that converts phloretin to phlorizin, a potent antioxidant in apple. FEBS J. 275 (2008) 3804-3814. [PMID: 18573104]

2. Yahyaa, M., Davidovich-Rikanati, R., Eyal, Y., Sheachter, A., Marzouk, S., Lewinsohn, E. and Ibdah, M. Identification and characterization of UDP-glucose:Phloretin 4'-O-glycosyltransferase from Malus x domestica Borkh. Phytochemistry 130 (2016) 47-55. [PMID: 27316677]

[EC 2.4.1.357 created 2018]

EC 2.4.1.358

Accepted name: acylphloroglucinol glucosyltransferase

Reaction: UDP-α-D-glucose + 2-acylphloroglucinol = UDP + 2-acylphloroglucinol 1-O-β-D-glucoside

For diagram of reaction click here.

Glossary: phlorisobutyrophenone = 2-methyl-1-(2,4,6-trihydroxyphenyl)propan-1-one
phlorisovalerophenone = 3-methyl-1-(2,4,6-trihydroxyphenyl)butan-1-one

Other name(s): UGT71K3

Systematic name: UDP-α-D-glucose:2-acylphloroglucinol 1-O-β-glucosyltransferase

Comments: Isolated from strawberries (Fragaria × ananassa). Acts best on phloroisovalerophenone and phlorobutyrophenone but will also glycosylate many other phenolic compounds. A minor product of the reaction is the 5-O-β-D-glucoside

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Song, C., Zhao, S., Hong, X., Liu, J., Schulenburg, K. and Schwab, W. A UDP-glucosyltransferase functions in both acylphloroglucinol glucoside and anthocyanin biosynthesis in strawberry (Fragaria × ananassa). Plant J. 85 (2016) 730-742. [PMID: 26859691]

[EC 2.4.1.358 created 2018]

EC 2.4.1.359

Accepted name: glucosylglycerol phosphorylase (configuration-retaining)

Reaction: 2-O-α-D-glucopyranosyl-glycerol + phosphate = α-D-glucose 1-phosphate + glycerol

Other name(s): 2-O-α-D-glucosylglycerol phosphorylase (retaining)

Systematic name: 2-O-α-D-glucopyranosyl-glycerol:phosphate α-D-glucosyltransferase (configuration-retaining)

Comments: The enzyme, characterized from the halotolerant bacterium Marinobacter adhaerens, is likely responsible for degradation of the compatible solute 2-O-α-D-glucopyranosyl-glycerol when the environmental salt concentration decreases. cf. EC 2.4.1.332, 1,2-α-glucosylglycerol phosphorylase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Franceus, J., Decuyper, L., D'hooghe, M. and Desmet, T. Exploring the sequence diversity in glycoside hydrolase family 13_18 reveals a novel glucosylglycerol phosphorylase. Appl. Microbiol. Biotechnol. (2018) . [PMID: 29470619]

[EC 2.4.1.359 created 2018]

EC 2.4.1.360

Accepted name: 2-hydroxyflavanone C-glucosyltransferase

Reaction: UDP-α-D-glucose + a 2'-hydroxy-β-oxodihydrochalcone = UDP + a 3'-(β-D-glucopyranosyl)-2'-hydroxy-β-oxodihydrochalcone

For diagram of reaction click here

Glossary: 2'-hydroxy-β-oxodihydrochalcone = 1-(2-hydroxyphenyl)-3-phenypropan-1,3-dione
3'-(β-D-glucopyranosyl)-2'-hydroxy-β-oxodihydrochalcone = 1-(3-(β-D-glucopyranosyl)-2-hydroxyphenyl)-3-phenylpropan-1,3-dione

Other name(s): OsCGT

Systematic name: UDP-α-D-glucose:2'-hydroxy-β-oxodihydrochalcone C6/8-β-D-glucosyltransferase

Comments: The enzyme has been characterized in Oryza sativa (rice), various Citrus spp., Glycine max (soybean), and Fagopyrum esculentum (buckwheat). Flavanone substrates require a 2-hydroxy group. The meta-stable flavanone substrates such as 2-hydroxynaringenin exist in an equilibrium with open forms such as 1-(4-hydroxyphenyl)-3-(2,4,6-trihydroxyphenyl)propane-1,3-dione, which are the actual substrates for the glucosyl-transfer reaction (see EC 1.14.14.162, flavanone 2-hydroxylase). The enzyme can also act on dihydrochalcones. The enzymes from citrus plants can catalyse a second C-glycosylation reaction at position 5.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Brazier-Hicks, M., Evans, K.M., Gershater, M.C., Puschmann, H., Steel, P.G. and Edwards, R. The C-glycosylation of flavonoids in cereals. J. Biol. Chem. 284 (2009) 17926-17934. [PMID: 19411659]

2. Nagatomo, Y., Usui, S., Ito, T., Kato, A., Shimosaka, M. and Taguchi, G. Purification, molecular cloning and functional characterization of flavonoid C-glucosyltransferases from Fagopyrum esculentum M. (buckwheat) cotyledon. Plant J. 80 (2014) 437-448. [PMID: 25142187]

3. Hirade, Y., Kotoku, N., Terasaka, K., Saijo-Hamano, Y., Fukumoto, A. and Mizukami, H. Identification and functional analysis of 2-hydroxyflavanone C-glucosyltransferase in soybean (Glycine max). FEBS Lett. 589 (2015) 1778-1786. [PMID: 25979175]

4. Ito, T., Fujimoto, S., Suito, F., Shimosaka, M. and Taguchi, G. C-Glycosyltransferases catalyzing the formation of di-C-glucosyl flavonoids in citrus plants. Plant J. 91 (2017) 187-198. [PMID: 28370711]

[EC 2.4.1.360 created 2018]

EC 2.4.1.361

Accepted name: GDP-mannose:di-myo-inositol-1,3'-phosphate β-1,2-mannosyltransferase

Reaction: 2 GDP-α-D-mannose + bis(myo-inositol) 1,3'-phosphate = 2 GDP + 2-O-(β-D-mannosyl-(1→2)-β-D-mannosyl)-bis(myo-inositol) 1,3'-phosphate (overall reaction)
(1a) GDP-α-D-mannose + bis(myo-inositol) 1,3'-phosphate = GDP + 2-O-(β-D-mannosyl)-bis(myo-inositol) 1,3'-phosphate
(1b) GDP-α-D-mannose + 2-O-(β-D-mannosyl)-bis(myo-inositol) 1,3'-phosphate = GDP + 2-O-(β-D-mannosyl-(1→2)-β-D-mannosyl)-bis(myo-inositol) 1,3'-phosphate

Other name(s): MDIP synthase

Systematic name: GDP-α-D-mannose:bis(myo-inositol)-1,3'-phosphate 2-β-D-mannosyltransferase

Comments: The enzyme from the hyperthermophilic bacterium Thermotoga maritima is involved in the synthesis of the solutes 2-O-(β-D-mannosyl)-bis(myo-inositol) 1,3'-phosphate and 2-O-(β-D-mannosyl-(1→2)-β-D-mannosyl)-bis(myo-inositol) 1,3'-phosphate.

Links to other databases: BRENDA, EXPASY, ExplorEnz, KEGG, MetaCyc, CAS registry number:

References:

1. Rodrigues, M.V., Borges, N., Almeida, C.P., Lamosa, P. and Santos, H. A unique β-1,2-mannosyltransferase of Thermotoga maritima that uses di-myo-inositol phosphate as the mannosyl acceptor. J. Bacteriol. 191 (2009) 6105-6115. [PMID: 19648237]

[EC 2.4.1.361 created 2019]

EC 2.4.1.362

Accepted name: α-(1→3) branching sucrase

Reaction: sucrose + a (1→6)-α-D-glucan = D-fructose + a (1→6)-α-D-glucan containing a (1→3)-α-D-glucose branch

Other name(s): branching sucrase A; BRS-A; brsA (gene name)

Systematic name: sucrose:(1→6)-α-D-glucan 3-α-D-[(1→3)-α-D-glucosyl]-transferase

Comments: The enzyme from Leuconostoc spp. is responsible for producing α-(1→3) branches in α-(1→6) glucans by transferring the glucose residue from fructose to a 3-hydroxyl group of a glucan.

Links to other databases: BRENDA, EXPASY, ExplorEnz, KEGG, MetaCyc, CAS registry number:

References:

1. Vuillemin, M., Claverie, M., Brison, Y., Severac, E., Bondy, P., Morel, S., Monsan, P., Moulis, C. and Remaud-Simeon, M. Characterization of the first α-(1→3) branching sucrases of the GH70 family. J. Biol. Chem 291 (2016) 7687-7702. [PMID: 26763236]

2. Moulis, C., Andre, I. and Remaud-Simeon, M. GH13 amylosucrases and GH70 branching sucrases, atypical enzymes in their respective families. Cell. Mol. Life Sci. 73 (2016) 2661-2679. [PMID: 27141938]

[EC 2.4.1.362 created 2019]

EC 2.4.1.363

Accepted name: ginsenoside 20-O-glucosyltransferase

Reaction: UDP-α-D-glucose + (20S)-protopanaxadiol = UDP + ginsenoside C-K

For diagram of reaction click here

Glossary: (20S)-protopanaxadiol = (3β,12β)-dammar-24-ene-3,12,20-triol
ginsenoside C-K = (3β,12β)-3,12-dihydroxydammar-24-en-20-yl β-D-glucopyranoside

Other name(s): UGT71A27 (gene name)

Systematic name: UDP-α-D-glucose:(20S)-protopanaxadiol 20-O-glucosyltransferase (configuration-inverting)

Comments: The enzyme, characterized from the plant Panax ginseng, transfers a glucosyl moiety to the free C20(S)-OH group of dammarane derivative substrates, including protopanaxatriol, dammarenediol II, (20S)-ginsenoside Rh2, and (20S)-ginsenoside Rg3. It does not act on the 20R epimer of protopanaxadiol, or on ginsenosides that are glucosylated at the C-6 position, such as ginsenoside Rh1 or ginsenoside Rg2.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Yan, X., Fan, Y., Wei, W., Wang, P., Liu, Q., Wei, Y., Zhang, L., Zhao, G., Yue, J. and Zhou, Z. Production of bioactive ginsenoside compound K in metabolically engineered yeast. Cell Res 24 (2014) 770-773. [PMID: 24603359]

2. Wei, W., Wang, P., Wei, Y., Liu, Q., Yang, C., Zhao, G., Yue, J., Yan, X. and Zhou, Z. Characterization of Panax ginseng UDP-glycosyltransferases catalyzing protopanaxatriol and biosyntheses of bioactive ginsenosides F1 and Rh1 in metabolically engineered yeasts. Mol. Plant 8 (2015) 1412-1424. [PMID: 26032089]

[EC 2.4.1.363 created 2019]

EC 2.4.1.364

Accepted name: protopanaxadiol-type ginsenoside 3-O-glucosyltransferase

Reaction: (1) UDP-α-D-glucose + (20S)-protopanaxadiol = UDP + (20S)-ginsenoside Rh2
(2) UDP-α-D-glucose + ginsenoside C-K = UDP + ginsenoside F2

For diagram of reaction click here

Glossary: (20S)-protopanaxadiol = (3β,12β)-dammar-24-ene-3,12,20-triol
ginsenoside C-K = (3β,12β)-3,12-dihydroxydammar-24-en-20-yl β-D-glucopyranoside

Other name(s): UGT74AE2 (gene name)

Systematic name: UDP-α-D-glucose:protopanaxadiol-type ginsenoside 3-O-glucosyltransferase (configuration-retaining)

Comments: The enzyme, characterized from the plant Panax ginseng, transfers a glucosyl moiety to the free C-3-OH group of (20S)-protopanaxadiol and ginsenoside C-K.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Jung, S.C., Kim, W., Park, S.C., Jeong, J., Park, M.K., Lim, S., Lee, Y., Im, W.T., Lee, J.H., Choi, G. and Kim, S.C. Two ginseng UDP-glycosyltransferases synthesize ginsenoside Rg3 and Rd. Plant Cell Physiol 55 (2014) 2177-2188. [PMID: 25320211]

[EC 2.4.1.364 created 2019]

EC 2.4.1.365

Accepted name: protopanaxadiol-type ginsenoside-3-O-glucoside 2"-O-glucosyltransferase

Reaction: (1) UDP-α-D-glucose + (20S)-ginsenoside Rh2 = UDP + (20S)-ginsenoside Rg3
(2) UDP-α-D-glucose + ginsenoside F2 = UDP + ginsenoside Rd

For diagram of reaction click here

Glossary: (20S)-ginsenoside Rh2 = (3β,12β)-12,20-dihydroxydammar-24-en-3-yl β-D-glucopyranoside
ginsenoside F2 = (3β,12β)-20-(β-D-glucopyranosyloxy)-12-hydroxydammar-24-en-3-yl β-D-glucopyranoside

Other name(s): UGT94Q2 (gene name)

Systematic name: UDP-α-D-glucose:3-O-glucosyl-protopanaxadiol-type ginsenoside 2"-O-glucosyltransferase

Comments: The enzyme, characterized from the plant Panax ginseng, transfers a glucosyl moiety to the 2" position of the glucose moiety in the protopanaxadiol-type ginsenoside-3-O-glucosides (20S)-ginsenoside Rh2 and ginsenoside F2.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Jung, S.C., Kim, W., Park, S.C., Jeong, J., Park, M.K., Lim, S., Lee, Y., Im, W.T., Lee, J.H., Choi, G. and Kim, S.C. Two ginseng UDP-glycosyltransferases synthesize ginsenoside Rg3 and Rd. Plant Cell Physiol 55 (2014) 2177-2188. [PMID: 25320211]

[EC 2.4.1.365 created 2019]

EC 2.4.1.366

Accepted name: ginsenoside F1 6-O-glucosyltransferase

Reaction: UDP-α-D-glucose + ginsenoside F1 = UDP + (20S)-ginsenoside Rg1

For diagram of reaction click here

Glossary: ginsenoside F1 = 3β,6α,12β-trihydroxydammar-24-en-20-yl β-D-glucopyranoside

Other name(s): UGTPg101 (gene name)

Systematic name: UDP-α-D-glucose:ginsenoside F1 6-O-glucosyltransferase

Comments: The enzyme, characterized from the plant Panax ginseng, glucosylates the C-6 position of ginsenoside F1. The enzyme also glucosylates the C-20 position of protopanaxatriol, which forms ginsenoside F1 (cf. EC 2.4.1.363, ginsenoside 20-O-glucosyltransferase). However, unlike EC 2.4.1.367, ginsenoside 6-O-glucosyltransferase, it is not able to glucosylate the C-6 position of protopanaxatriol when position C-20 is not glucosylated.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Wei, W., Wang, P., Wei, Y., Liu, Q., Yang, C., Zhao, G., Yue, J., Yan, X. and Zhou, Z. Characterization of Panax ginseng UDP-glycosyltransferases catalyzing protopanaxatriol and biosyntheses of bioactive ginsenosides F1 and Rh1 in metabolically engineered yeasts. Mol. Plant 8 (2015) 1412-1424. [PMID: 26032089]

[EC 2.4.1.366 created 2019]

EC 2.4.1.367

Accepted name: ginsenoside 6-O-glucosyltransferase

Reaction: (1) UDP-α-D-glucose + protopanaxatriol = UDP + ginsenoside Rh1
(2) UDP-α-D-glucose + ginsenoside F1 = UDP + (20S)-ginsenoside Rg1

For diagram of reaction click here

Glossary: protopanaxatriol = (3β,6α,12β)-dammar-24-ene-3,6,12,20-tetrol
ginsenoside F1 = (3β,6α,12β)-trihydroxydammar-24-en-20-yl β-D-glucopyranoside

Other name(s): UGTPg100 (gene name)

Systematic name: UDP-α-D-glucose:ginsenoside 6-O-glucosyltransferase

Comments: The enzyme, characterized from the plant Panax ginseng, glucosylates the C-6 position of protopanaxatriol and ginsenoside F1.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Wei, W., Wang, P., Wei, Y., Liu, Q., Yang, C., Zhao, G., Yue, J., Yan, X. and Zhou, Z. Characterization of Panax ginseng UDP-glycosyltransferases catalyzing protopanaxatriol and biosyntheses of bioactive ginsenosides F1 and Rh1 in metabolically engineered yeasts. Mol. Plant 8 (2015) 1412-1424. [PMID: 26032089]

[EC 2.4.1.367 created 2019]

EC 2.4.1.368

Accepted name: oleanolate 3-O-glucosyltransferase

Reaction: UDP-α-D-glucose + oleanolate = UDP + oleanolate 3-O-β-D-glucoside

Glossary: oleanolate = 3β-hydroxyolean-12-en-28-oate

Other name(s): UGT73C10 (gene name); UGT73C11 (gene name)

Systematic name: UDP-α-D-glucose:oleanolate 3-O-glucosyltransferase

Comments: The enzyme has been characterized from the saponin-producing crucifer plant Barbarea vulgaris.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Augustin, J.M., Drok, S., Shinoda, T., Sanmiya, K., Nielsen, J.K., Khakimov, B., Olsen, C.E., Hansen, E.H., Kuzina, V., Ekstrom, C.T., Hauser, T. and Bak, S. UDP-glycosyltransferases from the UGT73C subfamily in Barbarea vulgaris catalyze sapogenin 3-O-glucosylation in saponin-mediated insect resistance. Plant Physiol. 160 (2012) 1881-1895. [PMID: 23027665]

[EC 2.4.1.368 created 2019]


Continued with EC 2.4.2
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