EC 2.1 to EC 2.4

An asterisk before 'EC' indicates that this is an amendment to an existing enzyme rather than a new enzyme entry.

Common name: (iso)eugenol O-methyltransferase

Reaction: S-adenosyl-L-methionine + isoeugenol = S-adenosyl-L-homocysteine + isomethyleugenol

For diagram click here.

Systematic name: S-adenosyl-L-methionine:isoeugenol O-methyltransferase

Comments: Acts on eugenol and chavicol as well as isoeugenol.

References:

1. Wang, J. and Pichersky, E. Characterization of S-adenosyl-L-methionine:(iso)eugenol O-methyltransferase involved in floral scent production in Clarkia breweri. Arch. Biochem. Biophys. 349 (1998) 153-160 [PMID: 9439593]

2. Gang, D.R., Lavid, N., Zubieta, C., Chen, F., Beuerle, T., Lewinsohn, E., Noel, J.P. and Pichersky, E. Characterization of phenylpropene O-methyltransferases from sweet basil: facile change of substrate specificity and convergent evolution within a plant O-methyltransferase family. Plant Cell 14 (2002) 505-519 [PMID: 11884690]

EC 2.1.1.147

Common name: corydaline synthase

Reaction: S-adenosyl-L-methionine + palmatine + 2 NADPH + H⁺ = S-adenosyl-L-homocysteine + corydaline + 2 NADP⁺

For diagram click here.

Systematic name: S-adenosyl-L-methionine:protoberberine 13-C-methyltransferase

Comments: Also acts on 7,8-dihydropalmatine.

References:

1. Rueffer, M., Bauer, W. and Zenk, M.H. The formation of corydaline and related alkaloids in Corydalis cava in vivo and in vitro. Canad. J. Chem. 72 (1994) 170-175.

*EC 2.1.2.9

Common name: methionyl-tRNA formyltransferase

Reaction: 10-formyltetrahydrofolate + L-methionyl-tRNA^fMet + H₂O = tetrahydrofolate + N-formylmethionyl-tRNA^fMet

Other name(s): N¹⁰-formyltetrahydrofolic-methionyl-transfer ribonucleic transformylase; formylmethionyl-transfer ribonucleic synthetase; methionyl ribonucleic formyltransferase; methionyl-tRNA Met formyltransferase; methionyl-tRNA transformylase; methionyl-transfer RNA transformylase; methionyl-transfer ribonucleate methyltransferase; methionyl-transfer ribonucleic transformylase

Systematic name: 10-formyltetrahydrofolate:L-methionyl-tRNA N-formyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9015-76-3

References:

1. Dickerman, H.W., Steers, E., Jr., Redfield, B.G. and Weissbach, H. Methionyl soluble ribonucleic acid transformylase. I. Purification and partial characterization. J. Biol. Chem. 242 (1967) 1522-1525. [PMID: 5337045]

EC 2.2.1.5

Common name: 2-hydroxy-3-oxoadipate synthase

Reaction: 2-oxoglutarate + glyoxylate = 2-hydroxy-3-oxoadipate + CO₂

For diagram click here.

Other name(s): 2-hydroxy-3-oxoadipate glyoxylate-lyase (carboxylating); α-ketoglutaric-glyoxylic carboligase; oxoglutarate: glyoxylate carboligase

Systematic name: 2-oxoglutarate:glyoxylate succinaldehydetransferase (decarboxylating)

Comments: The bacterial enzyme requires thiamine diphosphate. The product decarboxylates to 5-hydroxy-4-oxopentanoate. The enzyme can decarboxylate 2-oxoglutarate. Acetaldehyde can replace glyoxylate.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9054-72-2

References:

1. Schlossberg, M.A., Bloom, R.J., Richert, D.A. and Westerfield, W.W. Carboligase activity of α-ketoglutarate dehydrogenase. Biochemistry 9 (1970) 1148-1153. [PMID: 5418712]

2. Schlossberg, M.A., Richert, D.A., Bloom, R.J. and Westerfield, W.W. Isolation and identification of 5-hydroxy-4-ketovaleric acid as a product of α-ketoglutarate: glyoxylate carboligase. Biochemistry 7 (1968) 333-337. [PMID: 4320439]

3. Stewart, P.R. and Quayle, J.R. The synergistic decarboxylation of glyoxalate and 2-oxoglutarate by an enzyme system from pig-liver mitochondria. Biochem. J. 102 (1967) 885-897.

EC 2.2.1.6

Common name: acetolactate synthase

Reaction: 2 pyruvate = 2-acetolactate + CO₂

For diagram click here.

Other name(s): α-acetohydroxy acid synthetase; α-acetohydroxyacid synthase; α-acetolactate synthase; α-acetolactate synthetase; acetohydroxy acid synthetase; acetohydroxyacid synthase; acetolactate pyruvate-lyase (carboxylating); acetolactic synthetase

Systematic name: pyruvate:pyruvate acetaldehydetransferase (decarboxylating)

Comments: This enzyme requires thiamine diphosphate. The reaction shown is in the pathway of biosynthesis of valine; the enzyme can also transfer the acetaldehyde from pyruvate to 2-oxobutanoate, forming 2-ethyl-2-hydroxy-3-oxobutanoate, also known as 2-aceto-2-hydroxybutanoate, a reaction in the biosynthesis of isoleucine.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9027-45-6

References:

1. Bauerle, R.H., Freundlich, M., Størmer, F.C. and Umbarger, H.E. Control of isoleucine, valine and leucine biosynthesis. II. Endproduct inhibition by valine of acetohydroxy acid synthetase in Salmonella typhimurium. Biochim. Biophys. Acta 92 (1964) 142-149.

2. Huseby, N.E., Christensen, T.B., Olsen, B.R. and Størmer, F.C. The pH 6 acetolactate-forming enzyme from Aerobacter aerogenes. Subunit structure. Eur. J. Biochem. 20 (1971) 209-214. [PMID: 5560406]

3. Størmer, F.C., Solberg, Y. and Hovig, T. The pH 6 acetolactate-forming enzyme from Aerobacter aerogenes. Molecular properties. Eur. J. Biochem. 10 (1969) 251-260. [PMID: 5823101]

4. Barak, Z., Chipman, D.M. and Gollop, N. Physiological implications of the specificity of acetohydroxy acid synthase isozymes of enteric bacteria. J. Bacteriol. 169 (1987) 3750-3756. [PMID: 3301814]

EC 2.2.1.7

Common name: 1-deoxy-D-xylulose-5-phosphate synthase

Reaction: pyruvate + D-glyceraldehyde 3-phosphate = 1-deoxy-D-xylulose 5-phosphate + CO₂

For diagram click here and mechanism here

Other name(s): 1-deoxy-D-xylulose-5-phosphate pyruvate-lyase (carboxylating); DXP-synthase

Systematic name: pyruvate:D-glyceraldehyde-3-phosphate acetaldehydetransferase (decarboxylating)

Comments: Requires thiamine diphosphate. The enzyme forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis (for diagram, click here).

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

References:

1. Sprenger, G.A., Schörken, U., Weigert, T., Grolle, S., deGraaf, A.A., Taylor, S.V., Begley, T.P., Bringer-Meyer, S. and Sahm, H. Identification of a thiamin-dependent synthase in Escherichia coli required for the formation of the 1-deoxy-D-xylulose 5-phosphate precursor to isoprenoids, thiamin, and pyridoxol. Proc. Natl. Acad. Sci. USA 94 (1997) 12857-12862. [PMID: 9371765]

2. Kuzuyama, T., Takagi, M., Takahashi, S. and Seto, H. Cloning and characterization of 1-deoxy-D-xylulose 5-phosphate synthase from Streptomyces sp. strain CL190, which uses both the mevalonate and nonmevalonate pathways for isopentenyl diphosphate biosynthesis. J. Bacteriol. 182 (2000) 891-897. [PMID: 10648511]

EC 2.3.1.159

Common name: acridone synthase

Reaction: 3 malonyl-CoA + N-methylanthraniloyl-CoA = 4 CoA + 1,3-dihydroxy-N-methylacridone + 3 CO₂

For diagram click here.

Systematic name: malonyl-CoA:N-methylanthraniloyl-CoA malonyltransferase (cyclizing)

Comments: Belongs to a superfamily of plant polyketide synthases. Has many similarities to chalcone and stilbene synthases (see reaction synthesis)

References:

1. Baumert, A., Maier, W., Gröger, D. and Deutzmann, R. Purification and properties of acridone synthase from cell suspension cultures of Ruta graveolens L. Z. Naturforsch. C: Biosci. 49 (1994) 26-32. [PMID: 8148006]

2. Maier, W., Baumert, A., Schumann, B., Furukawa, H. and Gröger, D. Synthesis of 1,3-dihydroxy-N-methylacridone and its conversion to rutacridone by cell-free extracts of Ruta-graveolens cell cultures. Phytochemistry 32 (1993) 691-698.

3. Lukacin. R., Springob, K., Urbanke, C., Ernwein, C., Schröder, G., Schröder, J. and Matern, U. Native acridone synthases I and II from Ruta graveolens L. form homodimers. FEBS Lett. 448 (1999) 135-140. [PMID: 10217426]

4. Junghanns, K.T., Kneusel, R.E., Groger, D. and Matern, U. Differential regulation and distribution of acridone synthase in Ruta graveolens. Phytochemistry 49 (1998) 403-411. [PMID: 9747538]

EC 2.3.1.160

Common name: vinorine synthase

Reaction: acetyl-CoA + 16-epivellosimine = CoA + vinorine

For diagram click here.

Systematic name: acyl-CoA:16-epivellosimine O-acetyltransferase (cyclizing)

Comments: The reaction proceeds in two stages. The indole nitrogen of 16-epivellosimine interacts with its aldehyde group giving an hydroxy-substituted new ring. This alcohol is then acetylated. Also acts on gardneral (11-methoxy-16-epivellosimine). Generates the ajmalan skeleton, which forms part of the route to ajmaline.

References:

1. Pfitzner, A., Polz, L. and Stöckligt, J. Properties of vinorine synthase the Rauwolfia enzyme involved in the formation of the ajmaline skeleton. Z. Naturforsch. C: Biosci. 41 (1986) 103-114.

EC 2.3.1.161

Common name: lovastatin nonaketide synthase

Reaction: acetyl-CoA + 8 malonyl-CoA + 11 NADPH + 10 H⁺ + S-adenosyl-L-methionine = dihydromonacolin L + 9 CoA + 8 CO₂ + 11 NADP⁺ + S-adenosyl-L-homocysteine + 6 H₂O

Systematic name: acyl-CoA:malonyl-CoA C-acyltransferase (decarboxylating, oxoacyl- and enoyl-reducing and thioester-hydrolysing)

Comments: The microbial enzyme is a multi-functional protein catalysing many of the chain building reactions of EC 2.3.1.85, fatty-acid synthase, as well as a reductive methylation and a Diels-Alder reaction.

References:

1. Auclair, K., Sutherland, A., Kennedy, J., Witter, D.J., van der Heever, J.P., Hutchinson, C.R. and Vederas, J.C. Lovastatin nonaketide synthase catalyses an intramolecular Diels-Alder reaction of a substrate analogue. J. Am. Chem. Soc. 122 (2000) 11519-11520.

EC 2.3.1.162

Common name: taxadien-5α-ol O-acetyltransferase

Reaction: acetyl-CoA + taxa-4(20),11-dien-5α-ol = CoA + taxa-4(20),11-dien-5α-yl acetate

For diagram click here.

Other name(s): acetyl coenzyme A:taxa-4(20),11(12)-dien-5α-ol O-acetyl transferase

Systematic name: acetyl-CoA:taxa-4(20),11-dien-5α-ol O-acetyltransferase

References:

1. Walker, K., Ketchum, R.E., Hezari, M., Gatfield, D., Goleniowski, M., Barthol, A. and Croteau, R. Partial purification and characterization of acetyl coenzyme A: taxa-4(20),11(12)-dien-5α-ol O-acetyl transferase that catalyzes the first acylation step of taxol biosynthesis. Arch. Biochem. Biophys. 364 (1999) 273-9. [PMID: 10190984]

EC 2.3.1.163

Common name: 10-hydroxytaxane O-acetyltransferase

Reaction: acetyl-CoA + 10-desacetyltaxuyunnanin C = CoA + taxuyunnanin C

For diagram click here.

Other name(s): acetyl coenzyme A: 10-hydroxytaxane O-acetyltransferase

Systematic name: acetyl-CoA:taxan-10β-ol O-acetyltransferase

Comments: Acts on a number of related taxane diterpenoids with a free 10β-hydroxy group. May be identical to EC 2.3.1.167, 10-deacetylbaccatin III 10-O-acetyltransferase.

References:

1. Menhard, B. and Zenk, M.H. Purification and characterization of acetyl coenzyme A: 10-hydroxytaxane O-acetyltransferase from cell suspension cultures of Taxus chinensis. Phytochemistry 50 (1999) 763-74. [PMID: 10192963]

EC 2.3.1.164

Common name: isopenicillin-N N-acyltransferase

Reaction: phenylacetyl-CoA + isopenicillin N + H₂O = CoA + penicillin G + L-2-aminohexanedioate

For diagram click here.

Other name(s): acyl-coenzyme A:isopenicillin N acyltransferase; isopenicillin N:acyl-CoA: acyltransferase

Systematic name: acyl-CoA:isopenicillin N N-acyltransferase

Comments: Proceeds by a two stage mechanism via 6-aminopenicillanic acid. Different from EC 3.5.1.11, penicillin amidase.

References:

1. Tobin, M.B., Fleming, M.D., Skatrud, P.L. and Miller, J.R. Molecular characterization of the acyl-coenzyme A:isopenicillin N acyltransferase gene (penDE) from Penicillium chrysogenum and Aspergillus nidulans and activity of recombinant enzyme in Escherichia coli. J. Bacteriol. 172 (1990) 5908-5914. [PMID: 2120195]

2. Aplin, R.T., Baldwin, J.E., Roach, P.L., Robinson, C.V. and Schofield, C.J. Investigations into the post-translational modification and mechanism of isopenicillin N:acyl-CoA acyltransferase using electrospray mass spectrometry. Biochem. J. 294 (1993) 357-363. [PMID: 8396910 ]

EC 2.3.1.165

Common name: 6-methylsalicylic acid synthase

Reaction: acetyl-CoA + 3 malonyl-CoA + NADPH + H⁺ = 6-methylsalicylate + 4 CoA + 3 CO₂ + NADP⁺

Systematic name: acyl-CoA:malonyl-CoA C-acyltransferase (decarboxylating, oxoacyl-reducing, thioester-hydrolysing and cyclising)

Comments: A multienzyme complex with a 4'-phosphopantetheine prosthetic group on the acyl carrier protein. It has a similar sequence to vertebrate type I fatty acid synthase. Acetoacetyl-CoA can also act as a starter molecule.

References:

1. Spencer, J.B. and Jordan, P.M. Purification and properties of 6-methylsalicylic acid synthase from Penicillium patulum. Biochem. J. 288 (1992) 839-846. [PMID: 1471999]

2. Child, C.J., Spencer, J.B., Bhogal, P. and Shoolingin-Jordan, P.M. Structural similarities between 6-methylsalicylic acid synthase from Penicillium patulum and vertebrate type I fatty acid synthase: evidence from thiol modification studies.Biochemistry 35 (1996) 12267-74 [PMID: 8823160]

EC 2.3.1.166

Common name: 2α-hydroxytaxane 2-O-benzoyltransferase

For diagram click here.

Reaction: benzoyl-CoA + 10-deacetyl-2-debenzoylbaccatin III = CoA + 10-deacetylbaccatin III

Other name(s): benzoyl-CoA:taxane 2α-O-benzoyltransferase

Systematic name: benzoyl-CoA:taxan-2α-ol O-benzoyltransferase

Comments: The enzyme was studied using the semisynthetic substrate 2-debenzoyl-7,13-diacetylbaccatin III. It will not acylate the hydroxy group at 1β, 7β, 10β or 13α of 10-deacetyl baccatin III, or at 2α or 5α of taxa-4(20),11-diene-2α,5α-diol.

References:

1. Walker, K. and Croteau, R. Taxol biosynthesis: molecular cloning of a benzoyl-CoA:taxane 2α-O-benzoyltransferase cDNA from taxus and functional expression in Escherichia coli. Proc. Natl. Acad. Sci. USA 97 (2000) 13591-135916 [PMID: 11095755]

EC 2.3.1.167

Common name: 10-deacetylbaccatin III 10-O-acetyltransferase

Reaction: acetyl-CoA + 10-deacetylbaccatin III = CoA + baccatin III

For diagram click here.

Systematic name: acetyl-CoA:taxan-10β-ol O-acetyltransferase

Comments: The enzyme will not acylate the hydroxy group at 1β, 7β or 13α of 10-deacetyl baccatin III, or at 5α of taxa-4(20),11-dien-5α-ol. May be identical to EC 2.3.1.163, 10-hydroxytaxane O-acetyltransferase.

References:

1. Walker. K and Croteau, R. Molecular cloning of a 10-deacetylbaccatin III-10-O-acetyl transferase cDNA from Taxus and functional expression in Escherichia coli. Proc. Natl. Acad. Sci. USA 97 (2000) 583-587 [PMID: 10639122]

EC 2.3.3 Acyl groups converted into alkyl on transfer

EC 2.3.3.1

Common name: citrate (Si)-synthase

Reaction: acetyl-CoA + H₂O + oxaloacetate = citrate + CoA

For diagram click here.

Other name(s): (R)-citric synthase; citrate condensing enzyme; citrate oxaloacetate-lyase [(pro-3S)-CH₂COO^-acetyl-CoA]; citrate oxaloacetate-lyase, CoA-acetylating; citrate synthase; citrate synthetase; citric synthase; citric-condensing enzyme; citrogenase; condensing enzyme; oxaloacetate transacetase; oxalacetic transacetase

Systematic name: acetyl-CoA:oxaloacetate C-acetyltransferase [thioester-hydrolysing, (pro-S)-carboxymethyl forming]

Comments: The stereospecificity of this enzyme is opposite to that of EC 2.3.3.4, citrate (Re)-synthase, which is found in some anaerobes.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, WIT, CAS registry number: 9027-96-7

References:

1. Gottschalk, G. Partial purification and some properties of the (R)-citrate synthase from Clostridium acidi-urici. Eur. J. Biochem. 7 (1969) 301-306. [PMID: 4974734]

2. Ochoa, S., Stern, J.R. and Schneider, M.C. Enzymatic synthesis of citric acid. II. Crystalline condensing enzyme. J. Biol. Chem. 193 (1951) 691-702.

3. Stern, J.R. Oxalacetate transacetase (condensing enzyme, citrogenase), in Boyer, P,D., Lardy, H and Myrbäck, K. (Eds.), The Enzymes, 2nd edn., vol. 5, Academic Press, New York, 1961, pp. 367-380.

4. Rault-Leonardon, M., Atkinson, M.A., Slaughter, C.A., Moomaw, C.R. and Srere, P.A. Azotobacter vinelandii citrate synthase. Biochemistry 34 (1995) 257-263. [PMID: 7819205]

5. Muir, J.M., Russell, R.J., Hough, D.W. and Danson, M.J. Citrate synthase from the hyperthermophilic Archaeon, Pyrococcus furiosus. Prot. Eng. 8 (1995) 583-592.

6. Russell, R.J., Ferguson, J.M., Hough, D.W., Danson, M.J. and Taylor, G.L. The crystal structure of citrate synthase from the hyperthermophilic archaeon Pyrococcus furiosus at 1.9 Å resolution. Biochemistry 36 (1997) 9983-9994. [PMID: 9254593]

EC 2.3.3.2

Common name: decylcitrate synthase

Reaction: lauroyl-CoA + H₂O + oxaloacetate = (2S,3S)-2-hydroxytridecane-1,2,3-tricarboxylate + CoA

For diagram click here.

Other name(s): 2-decylcitrate synthase; (2S,3S)-2-hydroxytridecane-1,2,3-tricarboxylate oxaloacetate-lyase (CoA-acylating)

Systematic name: dodecanoyl-CoA:oxaloacetate C-dodecanoyltransferase (thioester-hydrolysing, 1-carboxyundecyl-forming)

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9068-72-8

References:

1. Måhlén, A. and Gatenbeck, S. A metabolic variation in Penicillium spiculisporum Lehman. II. Purification and some properties of the enzyme synthesizing (-)-decylcitric acid. Acta Chem. Scand. 22 (1968) 2617-2623. [PMID: 5719165]

2. Måhlén, A. Properties of 2-decylcitrate synthase from Penicillium spiculisporum Lehman. Eur. J. Biochem. 22 (1971) 104-114. [PMID: 5099208]

EC 2.3.3.3

Common name: citrate (Re)-synthase

Reaction: acetyl-CoA + H₂O + oxaloacetate = citrate + CoA

For diagram click here.

Other name(s): (R)-citrate synthase; Re-citrate-synthase; citrate oxaloacetate-lyase [(pro-3R)-CH₂COO^-acetyl-CoA]

Systematic name: acetyl-CoA:oxaloacetate C-acetyltransferase [thioester-hydrolysing, (pro-R)-carboxymethyl-forming]

Comments: This enzyme is inactivated by oxygen and is found in some anaerobes. Its stereospecificity is opposite to that of EC 2.3.3.1, citrate (Si)-synthase.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9077-70-7

References:

1. Dittbrenner, S., Chowdhury, A.A. and Gottschalk, G. The stereospecificity of the (R)-citrates synthase in the presence of p-chloromercuribenzoate. Biochem. Biophys. Res. Commun. 36 (1969) 802-808. [PMID: 5808294]

2. Gottschalk, G. Partial purification and some properties of the (R)-citrate synthase from Clostridium acidi-urici. Eur. J. Biochem. 7 (1969) 301-306. [PMID: 4974734]

3. Gottschalk, G. and Barker, H.A. Synthesis of glutamate and citrate by Clostridium kluyveri. A new type of citrate synthase. Biochemistry 5 (1966) 1125-1133. [PMID: 5958189]

EC 2.3.3.4

Common name: decylhomocitrate synthase

Reaction: dodecanoyl-CoA + H₂O + 2-oxoglutarate = (3S,4S)-3-hydroxytetradecane-1,3,4-tricarboxylate + CoA

For diagram click here.

Other name(s): 2-decylhomocitrate synthase; 3-hydroxytetradecane-1,3,4-tricarboxylate 2-oxoglutarate-lyase (CoA-acylating)

Systematic name: dodecanoyl-CoA:2-oxoglutarate C-dodecanoyltransferase (thioester-hydrolysing, 1-carboxyundecyl-forming)

Comments: Decanoyl-CoA can act instead of dodecanoyl-CoA, but 2-oxoglutarate cannot be replaced by oxaloacetate or pyruvate.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 51845-40-0

References:

1. Måhlén, A. Purification and some properties of 2-decylhomocitrate synthase from Penicillium spiculisporum. Eur. J. Biochem. 38 (1973) 32-39. [PMID: 4774124]

2. Brandäge, S., Dahlman, O., Lindqvist, B., Måhlén, A. and Mörch, L. Absolute configuration and enantiospecific synthesis of spiculisporic acid. Acta Chem. Scand. 38B (1984) 837-844.

EC 2.3.3.5

Common name: 2-methylcitrate synthase

Reaction: propanoyl-CoA + H₂O + oxaloacetate = (2R,3S)-2-hydroxybutane-1,2,3-tricarboxylate + CoA

For diagram click here.

Glossary: 2-methylcitrate = (2R,3S)-2-hydroxybutane-1,2,3-tricarboxylate.

Other name(s): 2-methylcitrate oxaloacetate-lyase; MCS; methylcitrate synthase; methylcitrate synthetase

Systematic name: propanoyl-CoA:oxaloacetate C-propanoyltransferase (thioester-hydrolysing, 1-carboxyethyl-forming)

Comments: The enzyme acts on acetyl-CoA, propanoyl-CoA, butanoyl-CoA and pentanoyl-CoA. The relative rate of condensation of acetyl-CoA and oxaloacetate is 140% of that of propanoyl-CoA and oxaloacetate, but the enzyme has been separated from EC 2.3.3.1 citrate (Si)-synthase. Oxaloacetate cannot be replaced by glyoxylate, pyruvate or 2-oxoglutarate.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 57827-78-8

References:

1. Uchiyama, H. and Tabuchi, T. Properties of methylcitrate synthase from Candida lipolytica. Agric. Biol. Chem. 40 (1976) 1411-1418.

2. Textor, S., Wendisch, V.F., De Graaf, A.A., Muller, U., Linder, M.I., Linder, D. and Buckel, W. Propionate oxidation in Escherichia coli: evidence for operation of a methylcitrate cycle in bacteria. Arch. Microbiol. 168 (1997) 428-436. [PMID: 9325432]

3. Horswill, A.R. and Escalante-Semerena, J.C. Salmonella typhimurium LT2 catabolizes propionate via the 2-methylcitric acid cycle. J. Bacteriol. 181 (1999) 5615-5623. [PMID: 10482501]

4. van Rooyen, J.P.G., Mienie, L.J., Erasmus, E., De Wet, W.J., Ketting, D., Duran, M. and Wadman, S.K. Identification of the stereoisomeric configurations of methylcitric acid produced by Si-citrate synthase and methylcitrate synthase using capillary gas chromatography-mass spectrometry. J. Inherit. Metab. Dis. 17 (1994) 738-747. [PMID: 7707698]

EC 2.3.3.6

Common name: 2-ethylmalate synthase

Reaction: acetyl-CoA + H₂O + 2-oxobutanoate = (R)-2-ethylmalate + CoA

For diagram click here.

Other name(s): (R)-2-ethylmalate 2-oxobutanoyl-lyase (CoA-acetylating); 2-ethylmalate-3-hydroxybutanedioate synthase; propylmalate synthase; propylmalic synthase

Systematic name: acetyl-CoA:2-oxobutanoate C-acetyltransferase (thioester-hydrolysing, carboxymethyl-forming)

Comments: Also acts on (R)-2-(n-propyl)-malate. Formerly wrongly included with EC 2.3.3.7 3-ethylmalate synthase.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9024-01-5

References:

1. Strassman, M. and Ceci, L.N. A study of acetyl-CoA condensation with α-keto acids. Arch. Biochem. Biophys. 119 (1967) 420-428. [PMID: 6052435]

EC 2.3.3.7

Common name: 3-ethylmalate synthase

Reaction: butanoyl-CoA + H₂O + glyoxylate = 3-ethylmalate + CoA

For diagram click here.

Other name(s): 2-ethyl-3-hydroxybutanedioate synthase; 3-ethylmalate glyoxylate-lyase (CoA-butanoylating)

Systematic name: butanoyl-CoA:glyoxylate C-butanoyltransferase (thioester-hydrolysing, 1-carboxypropyl-forming)

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9024-01-5

References:

1. Ramasarma, T. and Giri, K.V. Phosphoglucose isomerase of green gram (Phaseolus radiatus). Arch. Biochem. Biophys. 62 (1956) 91-96.

EC 2.3.3.8

Common name: ATP citrate synthase

Reaction: ADP + phosphate + acetyl-CoA + oxaloacetate = ATP + citrate + CoA

Other name(s): ATP-citric lyase; ATP:citrate oxaloacetate-lyase [(pro-S)-CH₂COO^-acetyl-CoA] (ATP-dephosphorylating); acetyl-CoA:oxaloacetate acetyltransferase (isomerizing; ADP-phosphorylating); adenosine triphosphate citrate lyase; citrate cleavage enzyme; citrate-ATP lyase; citric cleavage enzyme; ATP citrate (pro-S)-lyase

Systematic name: acetyl-CoA:oxaloacetate C-acetyltransferase [(pro-S)-carboxymethyl-forming, ADP-phosphorylating]

Comments: The enzyme can be dissociated into components, two of which are identical with EC 4.1.3.34 (citryl-CoA lyase) and EC 6.2.1.18 (citrate—CoA ligase).

Links to other databases: BRENDA, EXPASY, GTD, KEGG, WIT, CAS registry number: 9027-95-6

References:

1. Lill, U., Schreil, A. and Eggerer, H. Isolation of enzymically active fragments formed by limited proteolysis of ATP citrate lyase. Eur. J. Biochem. 125 (1982) 645-650. [PMID: 6749502]

2. Srere, P.A. and Lipmann, F. An enzymatic reaction between citrate, adenosine triphosphate and coenzyme A. J. Am. Chem. Soc. 75 (1953) 4874 only.

EC 2.3.3.9

Common name: malate synthase

Reaction: acetyl-CoA + H₂O + glyoxylate = S-malate + CoA

For diagram click here.

Other name(s): L-malate glyoxylate-lyase (CoA-acetylating); glyoxylate transacetylase; glyoxylate transacetase; glyoxylic transacetase; malate condensing enzyme; malate synthetase; malic synthetase; malic-condensing enzyme

Systematic name: acetyl-CoA:glyoxylate C-acetyltransferase (thioester-hydrolysing, carboxymethyl-forming)

Links to other databases: BRENDA, EXPASY, GTD, KEGG, WIT, CAS registry number: 9013-48-3

References:

1. Dixon, G.H., Kornberg, H.L. and Lund, P. Purification and properties of malate synthetase. Biochim. Biophys. Acta 41 (1960) 217-233.

EC 2.3.3.10

Common name: hydroxymethylglutaryl-CoA synthase

Reaction: acetyl-CoA + H₂O + acetoacetyl-CoA = (S)-3-hydroxy-3-methylglutaryl-CoA + CoA

For diagram click here.

Other name(s): (S)-3-hydroxy-3-methylglutaryl-CoA acetoacetyl-CoA-lyase (CoA-acetylating); 3-hydroxy-3-methylglutaryl CoA synthetase; 3-hydroxy-3-methylglutaryl coenzyme A synthase; 3-hydroxy-3-methylglutaryl coenzyme A synthetase; 3-hydroxy-3-methylglutaryl-CoA synthase; 3-hydroxy-3-methylglutaryl-coenzyme A synthase; β-hydroxy-β-methylglutaryl-CoA synthase; HMG-CoA synthase; acetoacetyl coenzyme A transacetase; hydroxymethylglutaryl coenzyme A synthase; hydroxymethylglutaryl coenzyme A-condensing enzyme

Systematic name: acetyl-CoA:acetoacetyl-CoA C-acetyltransferase (thioester-hydrolysing, carboxymethyl-forming)

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9027-44-5

References:

1. Rudney, H. The biosynthesis of β-hydroxy-β-methylglutaric acid. J. Biol. Chem. 227 (1957) 363-377.

EC 2.3.3.11

Common name: 2-hydroxyglutarate synthase

Reaction: propanoyl-CoA + H₂O + glyoxylate = 2-hydroxyglutarate + CoA

Other name(s): 2-hydroxyglutaratic synthetase; 2-hydroxyglutaric synthetase; α-hydroxyglutarate synthase; hydroxyglutarate synthase; 2-hydroxyglutarate glyoxylate-lyase (CoA-propanoylating)

Systematic name: propanoyl-CoA:glyoxylate C-propanoyltransferase (thioester-hydrolysing, 2-carboxyethyl-forming)

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9024-02-6

References:

1. Reeves, H.C. and Ajl, S.J. α-Hydroxyglutaric acid synthetase. J. Bacteriol. 84 (1962) 186-187.

EC 2.3.3.12

Common name: 3-propylmalate synthase

Reaction: pentanoyl-CoA + H₂O + glyoxylate = 3-propylmalate + CoA

For diagram click here.

Other name(s): 3-(n-propyl)-malate synthase; 3-propylmalate glyoxylate-lyase (CoA-pentanoylating); β-n-propylmalate synthase; n-propylmalate synthase

Systematic name: pentanoyl-CoA:glyoxylate C-pentanoyltransferase (thioester-hydrolysing, 1-carboxybutyl-forming)

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 37290-62-3

References:

1. Imai, K., Reeves, H.C. and Ajl, S.J. n-Propylmalate synthetase. J. Biol. Chem. 238 (1963) 3193-3198.

EC 2.3.3.13

Common name: 2-isopropylmalate synthase

Reaction: acetyl-CoA + 3-methyl-2-oxobutanoate + H₂O = 2-hydroxy-2-isopropylsuccinate + CoA

For diagram click here.

Other name(s): 3-carboxy-3-hydroxy-4-methylpentanoate 3-methyl-2-oxobutanoate-lyase (CoA-acetylating); α-isopropylmalate synthetase; α-isopropylmalate synthase; α-isopropylmalic synthetase; isopropylmalate synthase; isopropylmalate synthetase

Systematic name: acetyl-CoA:3-methyl-2-oxobutanoate C-acetyltransferase (thioester-hydrolysing, carboxymethyl-forming)

Comments: Requires K⁺.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9030-98-2

References:

1. Kohlhaw, G., Leary, T.R. and Umbarger, H.E. α-Isopropylmalate synthase from Salmonella typhimurium. Purification and properties. J. Biol. Chem. 244 (1969) 2218-2225. [PMID: 4976555]

2. Webster, R.E. and Gross, S.R. The α-isopropylmalate synthetase of Neurospora. I. The kinetics and end product control of α-isopropylmalate synthetase function. Biochemistry 4 (1965) 2309-2327.

EC 2.3.3.14

Common name: homocitrate synthase

Reaction: acetyl-CoA + H₂O + 2-oxoglutarate = 2-hydroxybutane-1,2,4-tricarboxylate + CoA

For diagram click here.

Other name(s): 2-hydroxybutane-1,2,4-tricarboxylate 2-oxoglutarate-lyase (CoA-acetylating); acetyl-coenzyme A:2-ketoglutarate C-acetyl transferase; homocitrate synthetase

Systematic name: acetyl-CoA:2-oxoglutarate C-acetyltransferase (thioester-hydrolysing, carboxymethyl forming)

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9075-60-9

References:

1. Strassman, M. and Ceci, L.N. Enzymatic formation of homocitric acid, an intermediate in lysine biosynthesis. Biochem. Biophys. Res. Commun. 14 (1964) 262-267. [PMID: 5836514]

*EC 2.4.1.37

Common name: fucosylgalactoside 3-α-galactosyltransferase

Reaction: UDP-galactose + α-L-fucosyl-(12)-D-galactosyl-R = UDP + α-D-galactosyl-(13)-[α-L-fucosyl(12)]-D-galactosyl-R

where R can be OH, an oligosaccharide or a glycoconjugate

Other name(s): UDP-galactose:O-α-L-fucosyl(12)D-galactose α-D-galactosyltransferase; UDPgalactose:glycoprotein-α-L-fucosyl-(1,2)-D-galactose 3-α-D-galactosyltransferase; [blood group substance] α-galactosyltransferase; blood-group substance B-dependent galactosyltransferase; glycoprotein-fucosylgalactoside α-galactosyltransferase; histo-blood group B transferase; histo-blood substance B-dependent galactosyltransferase

Systematic name: UDP-galactose:α-L-fucosyl-(12)-D-galactoside 3-α-D-galactosyltransferase

Comments: Acts on blood group substance, and can use a number of 2-fucosyl-galactosides as acceptors.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 37257-33-3

References:

1. Race, C., Ziderman, D., and Watkins, W.M. An α-D-galactosyltransferase associated with the blood-group B character. Biochem. J. 107 (1968) 733-735.

*EC 2.4.1.44

Common name: lipopolysaccharide 3-α-galactosyltransferase

Reaction: UDP-galactose + lipopolysaccharide = UDP + 3-α-D-galactosyl-[lipopolysaccharide glucose]

Other name(s): UDP-galactose:lipopolysaccharide α,3-galactosyltransferase; UDP-galactose:polysaccharide galactosyltransferase; uridine diphosphate galactose:lipopolysaccharide α-3-galactosyltransferase; uridine diphosphogalactose-lipopolysaccharide α,3-galactosyltransferase

Systematic name: UDP-galactose:lipopolysaccharide 3-α-D-galactosyltransferase

Comments: Transfers D-galactosyl residues to D-glucose in the partially completed core of lipopolysaccharide [cf. EC 2.4.1.56 (lipopolysaccharide N-acetylglucosaminyltransferase), EC 2.4.1.58 (lipopolysaccharide glucosyltransferase I) and EC 2.4.1.73 (lipopolysaccharide glucosyltransferase II)].

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9037-98-7

References:

1. Endo, A. and Rothfield, L. Studies of a phospholipid-requiring bacterial enzyme. I. Purification and properties of uridine diphosphate galactose: lipopolysaccharide α-3-galactosyl transferase. Biochemistry 8 (1969) 3500-3507. [PMID: 4898284]

2. Wollin, R., Creeger, E.S., Rothfield, L.I., Stocker, B.A.D. and Lindberg, A.A. Salmonella typhimurium mutants defective in UDP-D-galactose:lipopolysaccharide α-1,6-D-galactosyltransferase. Structural, immunochemical, and enzymologic studies of rfaB mutants. J. Biol. Chem. 258 (1983) 3769-3774. [PMID: 6403519]

*EC 2.4.1.65

Common name: 3-galactosyl-N-acetylglucosaminide 4-α-L-fucosyltransferase

Reaction: GDP-β-L-fucose + β-D-galactosyl-(13)-N-acetyl-D-glucosaminyl-R = GDP + β-D-galactosyl-(13)-[α-L-fucosyl-(14)]-N-acetyl-β-D-glucosaminyl-R

For diagram click here.

Other name(s): (Le^a)-dependent (α-3/4)-fucosyltransferase; α(1,3/1,4) fucosyltransferase III; α-(14)-L-fucosyltransferase; α-4-L-fucosyltransferase; β-acetylglucosaminylsaccharide fucosyltransferase; FucT-II; Lewis α-(13/4)-fucosyltransferase; Lewis blood group α-(13/4)-fucosyltransferase; Lewis(Le) blood group gene-dependent α-(13/4)-L-fucosyltransferase; blood group Lewis α-4-fucosyltransferase; blood-group substance Le^a-dependent fucosyltransferase; guanosine diphosphofucose-β-acetylglucosaminylsaccharide 4-α-L-fucosyltransferase; guanosine diphosphofucose-glycoprotein 4-α-L-fucosyltransferase; guanosine diphosphofucose-glycoprotein 4-α-fucosyltransferase; 3-α-galactosyl-N-acetylglucosaminide 4-α-L-fucosyltransferase; GDP-β-L-fucose:3-β-D-galactosyl-N-acetyl-D-glucosaminyl-R 4^I-α-L-fucosyltransferase

Systematic name: GDP-L-fucose:3-β-D-galactosyl-N-acetyl-D-glucosaminyl-R 4^I-α-L-fucosyltransferase

Comments: This enzyme is the product of the Lewis blood group gene. Normally acts on a glycoconjugate where R (see reaction) is a glycoprotein or glycolipid. Although it is a 4-fucosyltransferase, it has a persistent 3-fucosyltransferase activity towards the glucose residue in free lactose. This enzyme fucosylates on O-4 of an N-acetylglucosamine that carries a galactosyl group on O-3, unlike EC 2.4.1.154, 4-galactosyl-N-acetylglucosaminide 3-α-L-fucosyltransferase, which fucosylates on O-3 of an N-acetylglucosamine that carries a galactosyl group on O-4. Enzymes catalysing the 4-α-fucosylation of the GlcNAc in β-D-Gal-(13)-β-GlcNAc sequences (with some activity also as 3-α-fucosyltransferases) are present in plants, where the function in vivo is the modification of N-glycans. In addition, the fucTa gene of Helicobacter strain UA948 encodes a fucosyltransferase with both 3-α- and 4-α-fucosyltransferase activities.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 37277-69-3

References:

1. Prieels, J.-P., Monnom, D., Dolmans, M., Beyer, T.A. and Hill, R.L. Co-purification of the Lewis blood group N-acetylglucosaminide α14 fucosyltransferase and an N-acetylglucosaminide α13 fucosyltransferase from human milk. J. Biol. Chem. 256 (1981) 10456-10463. [PMID: 7287719]

2. Rasko, D.A., Wang, G., Palcic, M.M. and Taylor, D.E. Cloning and characterization of the α(1,3/4) fucosyltransferase of Helicobacter pylori. J. Biol. Chem. 275 (2000) 4988-4994. [PMID: 10671538]

3. Wilson, I.B.H. Identification of a cDNA encoding a plant Lewis-type α1,4-fucosyltransferase. Glycoconj. J. 18 (2001) 439-447. [PMID: 12084979]

*EC 2.4.1.87

Common name: N-acetyllactosaminide 3-α-galactosyltransferase

Reaction: UDP-galactose + β-D-galactosyl-(14)-β-N-acetyl-D-glucosaminyl-R = UDP + α-D-galactosyl-(13)-β-D-galactosyl-(14)-β-N-acetylglucosaminyl-R

where R can be OH, an oligosaccharide or a glycoconjugate

Other name(s): α-galactosyltransferase; UDP-Gal:β-D-Gal(1,4)-D-GlcNAc α(1,3)-galactosyltransferase; UDP-Gal:N-acetyllactosaminide α(1,3)-galactosyltransferase; UDP-Gal:N-acetyllactosaminide α-1,3-D-galactosyltransferase; UDP-Gal:Galβ14GlcNAc-R α13-galactosyltransferase; UDP-galactose-acetyllactosamine α-D-galactosyltransferase; UDPgalactose:β-D-galactosyl-β-1,4-N-acetyl-D-glucosaminyl-glycopeptide α-1,3-D-galactosyltransferase; glucosaminylglycopeptide α-1,3-galactosyltransferase; uridine diphosphogalactose-acetyllactosamine α13-galactosyltransferase; uridine diphosphogalactose-acetyllactosamine galactosyltransferase; uridine diphosphogalactose-galactosylacetylglucosaminylgalactosylglucosylceramide galactosyltransferase; β-D-galactosyl-N-acetylglucosaminylglycopeptide α-1,3-galactosyltransferase

Systematic name: UDP-galactose:N-acetyllactosaminide 3-α-D-galactosyltransferase

Comments: Acts on β-galactosyl-1,4-N-acetylglucosaminyl termini on asialo-α₁-acid glycoprotein and N-acetyllactosamine (β-D-galactosyl-1,4-N-acetyl-β-D-glucosamine), but not on 2'-fucosylated-N-acetyllactosamine. The non-reducing terminal N-acetyllactosamine residues of glycoproteins can also act as acceptor. Now includes EC 2.4.1.124 and EC 2.4.1.151.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 62213-42-7

References:

1. Basu, M. and Basu, S. Enzymatic synthesis of a blood group B-related pentaglycosylceramide by an α-galactosyltransferase from rabbit bone marrow. J. Biol. Chem. 248 (1973) 1700-1706. [PMID: 4632915]

2. Blanken, W.M. and van den Eijnden, D.H. Biosynthesis of terminal Gal α13Gal β14GlcNAc-R oligosaccharide sequences on glycoconjugates. Purification and acceptor specificity of a UDP-Gal:N-acetyllactosaminide α13-galactosyltransferase from calf thymus. J. Biol. Chem. 260 (1985) 12927-12934. [PMID: 3932335]

3. Blake, D.A. and Goldstein, I.J. An α-D-galactosyltransferase activity in Ehrlich ascites tumor cells. Biosynthesis and characterization of a trisaccharide (α-D-galactose-(13)-N-acetyllactosamine). J. Biol. Chem. 256 (1981) 5387-5393. [PMID: 6787040]

[EC 2.4.1.124 Transferred entry: now included with EC 2.4.1.87, N-acetyllactosaminide 3-α-galactosyltransferase (EC 2.4.1.124 created 1984, deleted 2002)]

*EC 2.4.1.129

Common name: peptidoglycan glycosyltransferase

Reaction: [GlcNAc-(14)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)]_n-diphosphoundecaprenol + GlcNAc-(14)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = [GlcNAc-(14)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)]_n+1-diphosphoundecaprenol + undecaprenyl diphosphate

For diagram click here.

Other name(s): PG-II; bactoprenyldiphospho-N-acetylmuramoyl-(N-acetyl-D-glucosaminyl)-pentapeptide:peptidoglycan N-acetylmuramoyl-N-acetyl-D-glucosaminyltransferase; penicillin binding protein (3 or 1B); peptidoglycan transglycosylase

Systematic name: undecaprenyldiphospho-(N-acetyl-D-glucosaminyl-(14)-(N-acetyl-D-muramoylpentapeptide):undecaprenyldiphospho-(N-acetyl-D-glucosaminyl-(14)-N-acetyl-D-muramoylpentapeptide) disaccharidetransferase

Comments: The enzyme also works when the lysine residue is replaced by meso-2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm) combined with adjacent residues through its L-centre, as it is in Gram-negative and some Gram-positive organisms. The undecaprenol involved is ditrans,octacis-undecaprenol (for definitions, click here). Involved in the synthesis of cell-wall peptidoglycan.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 79079-04-2

References:

1. Taku, A., Stuckey, M. and Fan, D.P. Purification of the peptidoglycan transglycosylase of Bacillus megaterium. J. Biol. Chem. 257 (1982) 5018-5022. [PMID: 6802846]

2. Goffin, C. and Ghuysen, J.-M. Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs. Microbiol. Mol. Biol. Rev. 62 (1998) 1079-1093. [PMID: 9841666]

3. van Heijenoort, J. Formation of the glycan chains in the synthesis of bacterial peptidoglycan. Glycobiology 11 (2001) 25R-36R. [PMID: 11320055]

*EC 2.4.1.133

Common name: xylosylprotein 4-β-galactosyltransferase

Reaction: UDP-galactose + O-β-D-xylosylprotein = UDP + 4-β-D-galactosyl-O-β-D-xylosylprotein

For diagram click here.

Other name(s): UDP-D-galactose:D-xylose galactosyltransferase; UDP-D-galactose:xylose galactosyltransferase; galactosyltransferase I; uridine diphosphogalactose-xylose galactosyltransferase

Systematic name: UDP-galactose:O-β-D-xylosylprotein 4-β-D-galactosyltransferase

Comments: Involved in the biosynthesis of the linkage region of glycosaminoglycan chains as part of proteoglycan biosynthesis (chondroitin, dermatan and heparan sulfates). Requires Mn²⁺.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 52227-72-2

References:

1. Schwartz, N.B. and Roden, L. Biosynthesis of chondroitin sulfate. Solubilization of chondroitin sulfate glycosyltransferases and partial purification of uridine diphosphate-D-galactose:D-xylose galactosyltransferase. J. Biol. Chem. 250 (1975) 5200-5207. [PMID: 1150655]

2. Okajima, T., Yoshida, K., Kondo, T. and Furukawa, K. Human homolog of Caenorhabditis elegans sqv-3 gene is galactosyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans. J. Biol. Chem. 274 (1999) 22915-22918. [PMID: 10438455]

*EC 2.4.1.134

Common name: galactosylxylosylprotein 3-β-galactosyltransferase

Reaction: UDP-galactose + 4-β-D-galactosyl-O-β-D-xylosylprotein = UDP + 3-β-D-galactosyl-4-β-D-galactosyl-O-β-D-xylosylprotein

For diagram click here.

Other name(s): galactosyltransferase II; uridine diphosphogalactose-galactosylxylose galactosyltransferase

Systematic name: UDP-galactose:4-β-D-galactosyl-O-β-D-xylosylprotein 3-β-D-galactosyltransferase

Comments: Involved in the biosynthesis of the linkage region of glycosaminoglycan chains as part of proteoglycan biosynthesis (chondroitin, dermatan and heparan sulfates). Requires Mn²⁺.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 56626-21-2 and 56626-19-8

References:

1. Robinson, J.A. and Robinson, H.C. Initiation of chondroitin sulphate synthesis by β-D-galactosides. Substrates for galactosyltransferase II. Biochem. J. 227 (1985) 805-814. [PMID: 3924029]

2. Schwartz, N.B. and Roden, L. Biosynthesis of chondroitin sulfate. Solubilization of chondroitin sulfate glycosyltransferases and partial purification of uridine diphosphate-D-galactose:D-xylose galactosyltransferase. J. Biol. Chem. 250 (1975) 5200-5207. [PMID: 1150655]

3. Bai, X., Zhou, D., Brown, J.R., Crawford, B.E., Hennet, T. and Esko, J.D. Biosynthesis of the linkage region of glycosaminoglycans: cloning and activity of galactosyltransferase II, the sixth member of the β1,3-galactosyltransferase family (β3GalT6). J. Biol. Chem. 276 (2001) 48189-48195. [PMID: 11551958]

*EC 2.4.1.135

Common name: galactosylgalactosylxylosylprotein 3-β-glucuronosyltransferase

Reaction: UDP-glucuronate + 3-β-D-galactosyl-4-β-D-galactosyl-O-β-D-xylosylprotein = UDP + 3-β-D-glucuronosyl-3-β-D-galactosyl-4-β-D-galactosyl-O-β-D-xylosylprotein

For diagram click here.

Other name(s): glucuronosyltransferase I; uridine diphosphate glucuronic acid:acceptor glucuronosyltransferase

Systematic name: UDP-glucuronate:3-β-D-galactosyl-4-β-D-galactosyl-O-β-D-xylosyl-protein D-glucuronosyltransferase

Comments: Involved in the biosynthesis of the linkage region of glycosaminoglycan chains as part of proteoglycan biosynthesis (chondroitin, dermatan and heparan sulfates). Requires Mn²⁺.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9030-08-4

References:

1. Helting, J. and Roden, L. Biosynthesis of chondroitin sulfate. II. Glucuronosyl transfer in the formation of the carbohydrate-protein linkage region. J. Biol. Chem. 244 (1969) 2799-2805. [PMID: 5770003]

2. Helting, T. Biosynthesis of heparin. Solubilization and partial purification of uridine diphosphate glucuronic acid: acceptor glucuronosyltransferase from mouse mastocytoma. J. Biol. Chem. 247 (1972) 4327-4332. [PMID: 4260846]

3. Kitagawa, H., Tone, Y., Tamura, J., Neumann, K.W., Ogawa, T., Oka, S., Kawasaki, T. and Sugahara, K. Molecular cloning and expression of glucuronyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans. J. Biol. Chem. 273 (1998) 6615-6618. [PMID: 9506957]

[EC 2.4.1.151 Transferred entry: now included with EC 2.4.1.87, N-acetyllactosaminide 3-α-galactosyltransferase (EC 2.4.1.151 created 1984, deleted 2002)]

*EC 2.4.1.174

Common name: glucuronylgalactosylproteoglycan 4-β-N-acetylgalactosaminyltransferase

Reaction: UDP-N-acetyl-D-galactosamine + β-D-glucuronyl-1,3-D-galactosyl-proteoglycan = UDP + N-acetyl-D-galactosaminyl-1,4-β-D-glucuronyl-1,3-β-D-galactosylproteoglycan

For diagram click here.

Other name(s): N-acetylgalactosaminyltransferase I; glucuronylgalactosylproteoglycan β-1,4-N-acetylgalactosaminyltransferase; uridine diphosphoacetylgalactosamine-chondroitin acetylgalactosaminyltransferase I

Systematic name: UDP-N-acetyl-D-galactosamine:D-glucuronyl-1,3-β-D-galactosyl-proteoglycan β-1,4-N-acetylgalactosaminyltransferase

Comments: Requires Mn²⁺. Involved in the biosynthesis of chondroitin sulfate. Key enzyme activity for the initiation of chondroitin and dermatan sulfates, transferring GalNAc to the GlcA-Gal-Gal-Xyl-Ser core.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 96189-39-8

References:

1. Rohrmann, K., Niemann, R. and Buddecke, E. Two N-acetylgalactosaminyltransferases are involved in the biosynthesis of chondroitin sulfate. Eur. J. Biochem. 148 (1985) 463-469. [PMID: 3922754]

2. Uyama, T., Kitagawa, H., Tamura, Ji J. and Sugahara, K. Molecular cloning and expression of human chondroitin N-acetylgalactosaminyltransferase: the key enzyme for chain initiation and elongation of chondroitin/dermatan sulfate on the protein linkage region tetrasaccharide shared by heparin/heparan sulfate. J. Biol. Chem. 277 (2002) 8841-8846. [PMID: 11788602]

*EC 2.4.1.175

Common name: glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-β-N-acetylgalactosaminyltransferase

Reaction: UDP-N-acetyl-D-galactosamine + β-D-glucuronosyl-(13)-N-acetyl-β-D-galactosaminyl-proteoglycan = UDP + N-acetyl-β-D-galactosaminyl-(14)-β-D-glucuronosyl-(13)-N-acetyl-β-D-galactosaminyl-proteoglycan

For diagram click here.

Other name(s): N-acetylgalactosaminyltransferase II; UDP-N-acetyl-D-galactosamine:D-glucuronyl-N-acetyl-1,3-β-D-galactosaminylproteoglycan β-1,4-N-acetylgalactosaminyltransferase; chondroitin synthase; glucuronyl-N-acetylgalactosaminylproteoglycan β-1,4-N-acetylgalactosaminyltransferase; uridine diphosphoacetylgalactosamine-chondroitin acetylgalactosaminyltransferase II

Systematic name: UDP-N-acetyl-D-galactosamine:β-D-glucuronosyl-(13)-N-acetyl-β-D-galactosaminyl-proteoglycan 4-β-N-acetylgalactosaminyltransferase

Comments: Involved in the biosynthesis of chondroitin sulfate. The human form of this enzyme is a bifunctional glycosyltransferase, which also has the 3-β-glucuronosyltransferase (EC 2.4.1.226) activity required for the synthesis of the chondroitin sulfate disaccharide repeats. Similar chondroitin synthase 'co-polymerases' can be found in Pasteurella multocida and Escherichia coli.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 96189-40-1

References:

1. Rohrmann, K., Niemann, R. and Buddecke, E. Two N-acetylgalactosaminyltransferases are involved in the biosynthesis of chondroitin sulfate. Eur. J. Biochem. 148 (1985) 463-469. [PMID: 3922754]

2. Kitagawa, H., Uyama, T. and Sugahara, K. Molecular cloning and expression of a human chondroitin synthase. J. Biol. Chem. 276 (2001) 38721-38726. [PMID: 11514575]

3. DeAngelis, P.L. and Padgett-McCue, A.J. Identification and molecular cloning of a chondroitin synthase from Pasteurella multocida type F. J. Biol. Chem. 275 (2000) 24124-24129. [PMID: 10818104]

4. Ninomiya, T., Sugiura, N., Tawada, A., Sugimoto, K., Watanabe, H. and Kimata, K. Molecular cloning and characterization of chondroitin polymerase from Escherichia coli strain K4. J. Biol. Chem. 277 (2002) 21567-21575. [PMID: 11943778]

*EC 2.4.1.198

Common name: phosphatidylinositol N-acetylglucosaminyltransferase

Reaction: UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6(N-acetyl-α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol

For diagram click here.

Other name(s): UDP-N-acetyl-D-glucosamine:phosphatidylinositol N-acetyl-D-glucosaminyltransferase; uridine diphosphoacetylglucosamine α1,6-acetyl-D-glucosaminyltransferase

Systematic name: UDP-N-acetyl-D-glucosamine:1-phosphatidyl-1D-myo-inositol 6-(N-acetyl-α-D-glucosaminyl)transferase

Comments: Involved in the first step of glycosylphosphatidylinositol (GPI) anchor formation in all eukaryotes. In mammalian cells, the enzyme is composed of at least five subunits (PIG-A, PIG-H, PIG-C, GPI1 and PIG-P). PIG-A subunit is the catalytic subunit. In some species, the long-chain acyl groups of the phosphatidyl group are partly replaced by long-chain alkyl or alk-1-enyl groups.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 144388-35-2

References:

1. Doering, T.L., Masteron, W.J., Englund, P.T. and Hart, G.W. Biosynthesis of the glycosyl phosphatidylinositol membrane anchor of the trypanosome variant surface glycoprotein. Origin of the non-acetylated glucosamine. J. Biol. Chem. 264 (1989) 11168-11173. [PMID: 2525555]

2. Watanabe, R., Inoue, N., Westfall, B., Taron, C.H., Orlean, P., Takeda, J. and Kinoshita, T. The first step of glycosylphosphatidylinositol biosynthesis is mediated by a complex of PIG-A, PIG-H, PIG-C and GPI1. EMBO J. 17 (1998) 877-885. [PMID: 9463366]

3. Watanabe, R., Murakami, Y., Marmor, M.D., Inoue, N., Maeda, Y., Hino, J., Kangawa, K., Julius, M. and Kinoshita, T. Initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-P and is regulated by DPM2. EMBO J. 19 (2000) 4402-4411. [PMID: 10944123]

EC 2.4.1.219

Common name: vomilenine glucosyltransferase

Reaction: UDP-glucose + vomilenine = UDP + raucaffricine

For diagram click here.

Other name(s): UDPG:vomilenine 21-β-D-glucosyltransferase

Systematic name: UDP-glucose:vomilenine 21-O-β-D-glucosyltransferase

Comments: The indole alkaloid raucaffricine accumulates during the culture of Rauvolfia cell suspensions.

References:

1. Warzecha, H., Obitz, P. and Stöckigt, J. Purification, partial amino acid sequence and structure of the product of raucaffricine-O-β-D-glucosidase from plant cell cultures of Rauwolfia serpentina. Phytochemistry 50 (1999) 1099-1109. [PMID: 10234858]

2. Warzecha, H., Gerasimenko, I., Kutchan, T.M. and Stöckigt, J. Molecular cloning and functional bacterial expression of a plant glucosidase specifically involved in alkaloid biosynthesis. Phytochemistry 54 (2000) 657-666. [PMID: 10975500]

3. Ruyter, C.M., and Stöckigt, J. Enzymatic formation of raucaffricine, the major indole alkaloid of Rauwolfia serpentina cell-suspension cultures. Helv. Chim. Acta 74 (1991) 1707-1712.

EC 2.4.1.220

Common name: indoxyl-UDPG glucosyltransferase

Reaction: UDP-glucose + indoxyl = UDP + indican

Glossary: indoxyl = indole-3-ol

Other name(s): indoxyl-UDPG-glucosyltransferase

Systematic name: UDP-glucose:indoxyl 3-O-β-D-glucosyltransferase

Comments: Also acts to a limited extent on 4-, 5-, 6- and 7-hydroxyindole. After enzymic or chemical hydrolysis, indican forms indoxyl, which, in turn, is converted in the presence of oxygen to the dye indigo.

References:

1. Marcinek, H., Weyler, W., Deus-Neumann, B. and Zenk, M.H. Indoxyl-UDPG-glucosyltransferase from Baphicacanthus cusia. Phytochemistry 53 (2000) 201-207. [PMID: 10680172]

EC 2.4.1.221

Common name: peptide-O-fucosyltransferase

Reaction: transfers an α-L-fucosyl residue from GDP-β-L-fucose to the serine hydroxy group of a protein acceptor

Other name(s): GDP-L-fucose:polypeptide fucosyltransferase; GDP-fucose protein O-fucosyltransferase; GDP-fucose:polypeptide fucosyltransferase

Systematic name: GDP-β-L-fucose:polypeptide O-α-L-fucosyltransferase

Comments: Involved in the biosynthesis of O-fucosylated epidermal growth factor (EGF) and thrombospondin type 1 repeats. The attachment of O-linked fucose to serine or threonine occurs on EGF domains within the sequence Cys-Xaa-Xaa-Gly-Gly-Ser/Thr-Cys.

References:

1. Wang, Y. and Spellman, M.W. Purification and characterization of a GDP-fucose:polypeptide fucosyltransferase from Chinese hamster ovary cells. J. Biol. Chem. 273 (1998) 8112-8118. [PMID: 9525914]

2. Wang, Y., Shao, L., Shi, S., Harris, R.J., Spellman, M.W., Stanley, P. and Haltiwanger, R.S. Modification of epidermal growth factor-like repeats with O-fucose. Molecular cloning and expression of a novel GDP-fucose protein O-fucosyltransferase. J. Biol. Chem. 276 (2001) 40338-40345. [PMID: 11524432]

3. Wang, Y., Lee, G.F., Kelley, R.F. and Spellman, M.W. Identification of a GDP-L-fucose:polypeptide fucosyltransferase and enzymatic addition of O-linked fucose to EGF domains. Glycobiology 6 (1996) 837-842. [PMID: 9023546]

4. Hofsteenge, J., Huwiler, K.G., Macek, B., Hess, D., Lawler, J., Mosher, D.F. and Peter-Katalinic, J. C-mannosylation and O-fucosylation of the thrombospondin type 1 module. J. Biol. Chem. 276 (2001) 6485-6498. [PMID: 11067851]

EC 2.4.1.222

Common name: O-fucosylpeptide 3-β-N-acetylglucosaminyltransferase

Reaction: transfers a β-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor

Other name(s): O-fucosylpeptide β-1,3-N-acetylglucosaminyltransferase

Systematic name: UDP-D-GlcNAc:O-L-fucosylpeptide 3-β-N-acetyl-D-glucosaminyltransferase

Comments: O-Fucosylpeptide 3-β-N-acetylglucosaminyltransferases are the products of fringe genes. O-linked fucose is an unusual form of glycosylation where the fucose is attached directly to proteins through the hydroxy groups of Ser or Thr residues.

References:

1. Moloney, D.J., Panin, V.M., Johnston, S.H., Chen, J., Shao, L., Wilson, R., Wang, Y., Stanley, P., Irvine, K.D., Haltiwanger, R.S. and Vogt, T.F. Fringe is a glycosyltransferase that modifies Notch. Nature 406 (2000) 369-375. [PMID: ] 10935626]

EC 2.4.1.223

Common name: glucuronyl-galactosyl-proteoglycan 4-α-N-acetylglucosaminyltransferase

Reaction: UDP-N-acetyl-D-glucosamine + β-D-glucuronosyl-(13)-β-D-galactosyl-(13)-β-D-galactosyl-(14)-β-D-xylosyl-proteoglycan = UDP + α-N-acetyl-D-glucosaminyl-(14)-β-D-glucuronosyl-(13)-β-D-galactosyl-(13)-β-D-galactosyl-(14)-β-D-xylosyl-proteoglycan

For diagram click here.

Other name(s): α-N-acetylglucosaminyltransferase I; α1,4-N-acetylglucosaminyltransferase; glucuronosylgalactosyl-proteoglycan 4-α-N-acetylglucosaminyltransferase

Systematic name: UDP-N-acetyl-D-glucosamine:β-D-glucuronosyl-(13)-β-D-galactosyl-(13)-β-D-galactosyl-(14)-β-D-xylosyl-proteoglycan 4^IV-α-N-acetyl-D-glucosaminyltransferase

Comments: Enzyme involved in the initiation of heparin and heparan sulfate synthesis, transferring GlcNAc to the (GlcA-Gal-Gal-Xyl-)Ser core. Apparently products of both the human EXTL2 and EXTL3 genes can catalyse this reaction. In Caenorhabditis elegans, the product of the rib-2 gene displays this activity as well as that of EC 2.4.1.224, glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-α-N-acetylglucosaminyltransferase. For explanation of the use of a superscript in the systematic name, see 2-Carb-37.2.

References:

1. Kitagawa, H., Shimakawa, H. and Sugahara, K. The tumor suppressor EXT-like gene EXTL2 encodes an α1,4-N-acetylhexosaminyltransferase that transfers N-acetylgalactosamine and N-acetylglucosamine to the common glycosaminoglycan-protein linkage region. The key enzyme for the chain initiation of heparan sulfate. J. Biol. Chem. 274 (1999) 13933-13937. [PMID: 10318803]

2. Kitagawa, H., Egusa, N., Tamura, J.I., Kusche-Gullberg, M., Lindahl, U. and Sugahara, K. rib-2, a Caenorhabditis elegans homolog of the human tumor suppressor EXT genes encodes a novel α1,4-N-acetylglucosaminyltransferase involved in the biosynthetic initiation and elongation of heparan sulfate. J. Biol. Chem. 276 (2001) 4834-4838. [PMID: 11121397]

EC 2.4.1.224

Common name: glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-α-N-acetylglucosaminyltransferase

Reaction: UDP-N-acetyl-D-glucosamine + β-D-glucuronosyl-(14)-N-acetyl-α-D-glucosaminyl-proteoglycan = UDP + N-acetyl-α-D-glucosaminyl-(14)-β-D-glucuronosyl-(14)-N-acetyl-α-D-glucosaminyl-proteoglycan

For diagram click here.

Other name(s): α-N-acetylglucosaminyltransferase II glucuronyl-N-acetylglucosaminylproteoglycan α-1,4-N-acetylglucosaminyltransferase

Systematic name: UDP-N-acetyl-D-glucosamine:β-D-glucuronosyl-(14)-N-acetyl-α-D-glucosaminyl-proteoglycan 4-α-N-acetylglucosaminyltransferase

Comments: Involved in the biosynthesis of heparin and heparan sulfate. Some forms of the enzyme from human (particularly the enzyme complex encoded by the EXT1 and EXT2 genes) act as bifunctional glycosyltransferases, which also have the 4-β-glucuronosyltransferase (EC 2.4.1.225) activity required for the synthesis of the heparan sulfate disaccharide repeats. Other human forms of this enzyme (e.g. the product of the EXTL1 gene) have only the 4-α-N-acetylglucosaminyltransferase activity. In Caenorhabditis elegans, the product of the rib-2 gene displays the activities of this enzyme as well as EC 2.4.1.223, glucuronyl-galactosyl-proteoglycan 4-α-N-acetylglucosaminyltransferase.

References:

1. Kim, B.T., Kitagawa, H., Tamura, J., Saito, T., Kusche-Gullberg, M., Lindahl, U. and Sugahara, K. Human tumor suppressor EXT gene family members EXTL1 and EXTL3 encode α1,4-N-acetylglucosaminyltransferases that likely are involved in heparan sulfate/heparin biosynthesis. Proc. Natl. Acad. Sci. USA 98 (2001) 7176-7181. [PMID: 11390981]

2. Kitagawa, H., Egusa, N., Tamura, J.I., Kusche-Gullberg, M., Lindahl, U. and Sugahara, K. rib-2, a Caenorhabditis elegans homolog of the human tumor suppressor EXT genes encodes a novel α1,4-N-acetylglucosaminyltransferase involved in the biosynthetic initiation and elongation of heparan sulfate. J. Biol. Chem. 276 (2001) 4834-4838. [PMID: 11121397]

3. Senay, C., Lind, T., Muguruma, K., Tone, Y., Kitagawa, H., Sugahara, K., Lidholt, K., Lindahl, U. and Kusche-Gullberg, M. The EXT1/EXT2 tumor suppressors: catalytic activities and role in heparan sulfate biosynthesis. EMBO Rep. 1 (2000) 282-286. [PMID: 11256613]

4. Lind, T., Tufaro, F., McCormick, C., Lindahl, U. and Lidholt, K. The putative tumor suppressors EXT1 and EXT2 are glycosyltransferases required for the biosynthesis of heparan sulfate. J. Biol. Chem. 273 (1998) 26265-26268. [PMID: 9756849]

EC 2.4.1.225

Common name: N-acetylglucosaminyl-proteoglycan 4-β-glucuronosyltransferase

Reaction: UDP-α-D-glucuronate + N-acetyl-α-D-glucosaminyl-(14)-β-D-glucuronosyl-proteoglycan = UDP + β-D-glucuronosyl-(14)-N-acetyl-α-D-glucosaminyl-(14)-β-D-glucuronosyl-proteoglycan

For diagram click here.

Other name(s): N-acetylglucosaminylproteoglycan β-1,4-glucuronyltransferase; heparan glucuronyltransferase II

Systematic name: UDP-α-D-glucuronate:N-acetyl-α-D-glucosaminyl-(14)-β-D-glucuronosyl-proteoglycan 4-β-glucuronosyltransferase

Comments: Involved in the biosynthesis of heparin and heparan sulfate. Some forms of the human enzyme (particularly the enzyme complex encoded by the EXT1 and EXT2 genes) act as bifunctional glycosyltransferases, which also have the glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-α-N-acetylglucosaminyltransferase (EC 2.4.1.244) activity required for the synthesis of the heparan sulfate disaccharide repeats.

References:

1. Senay, C., Lind, T., Muguruma, K., Tone, Y., Kitagawa, H., Sugahara, K., Lidholt, K., Lindahl, U. and Kusche-Gullberg, M. The EXT1/EXT2 tumor suppressors: catalytic activities and role in heparan sulfate biosynthesis. EMBO Rep. 1 (2000) 282-286. [PMID: 11256613]

2. Lind, T., Tufaro, F., McCormick, C., Lindahl, U. and Lidholt, K. The putative tumor suppressors EXT1 and EXT2 are glycosyltransferases required for the biosynthesis of heparan sulfate. J. Biol. Chem. 273 (1998) 26265-26268. [PMID: 9756849]

EC 2.4.1.226

Common name: N-acetylgalactosaminyl-proteoglycan 3-β-glucuronosyltransferase

Reaction: UDP-α-D-glucuronate + N-acetyl-β-D-galactosaminyl-(14)-β-D-glucuronosyl-proteoglycan = UDP + β-D-glucuronosyl-(13)-N-acetyl-β-D-galactosaminyl-(14)-β-D-glucuronosyl-proteoglycan

For diagram click here.

Other name(s): chondroitin glucuronyltransferase II

Systematic name: α-D-glucuronate:N-acetyl-β-D-galactosaminyl-(14)-β-D-glucuronosyl-proteoglycan 3-β-glucuronosyltransferase

Comments: Involved in the biosynthesis of chondroitin and dermatan sulfate. The human chondroitin synthetase is a bifunctional glycosyltransferase, which has the 3-β-glucuronosyltransferase and 4-β-N-acetylgalactosaminyltransferase (EC 2.4.1.175) activities required for the synthesis of the chondroitin sulfate disaccharide repeats. Similar chondroitin synthase 'co-polymerases' can be found in Pasteurella multocida and Escherichia coli. There is also another human protein with apparently only the 3-β-glucuronosyltransferase activity.

References:

1. Kitagawa, H., Uyama, T. and Sugahara, K. Molecular cloning and expression of a human chondroitin synthase. J. Biol. Chem. 276 (2001) 38721-38726. [PMID: 11514575]

2. DeAngelis, P.L. and Padgett-McCue, A.J. Identification and molecular cloning of a chondroitin synthase from Pasteurella multocida type F. J. Biol. Chem. 275 (2000) 24124-24129. [PMID: 10818104]

3. Ninomiya, T., Sugiura, N., Tawada, A., Sugimoto, K., Watanabe, H. and Kimata, K. Molecular cloning and characterization of chondroitin polymerase from Escherichia coli strain K4. J. Biol. Chem. 277 (2002) 21567-21575. [PMID: 11943778]

4. Gotoh, M., Yada, T., Sato, T., Akashima, T., Iwasaki, H., Mochizuki, H., Inaba, N., Togayachi, A., Kudo, T., Watanabe, H., Kimata, K. and Narimatsu, H. Molecular cloning and characterization of a novel chondroitin sulfate glucuronyltransferase which transfers glucuronic acid to N-acetylgalactosamine J. Biol. Chem. 277 (2002) 38179-38188 [PMID: 12145278]

EC 2.4.1.227

Common name: undecaprenyldiphospho-muramoylpentapeptide β-N-acetylglucosaminyltransferase

Reaction: UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = UDP + GlcNAc-(14)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol

For diagram click here.

Other name(s): MurG transferase

Systematic name: UDP-N-acetyl-D-glucosamine:N-acetyl-α-D-muramyl(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol β-1,4-N-acetylglucosaminlytransferase

Comments: The enzyme also works when the lysine residue is replaced by meso-2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm) combined with adjacent residues through its L-centre, as it is in Gram-negative and some Gram-positive organisms. The undecaprenol involved is ditrans,octacis-undecaprenol (for definitions, click here).

References:

1. van Heijenoort, J. Recent advances in the formation of the bacterial peptidoglycan monomer unit. Nat. Prod. Rep. 18 (2001) 503-519. [PMID: 11699883]

EC 2.4.1.228

Common name: lactosylceramide 4-α-galactosyltransferase

Reaction: UDP-galactose + β-D-galactosyl-(14)-D-glucosylceramide = UDP + α-D-galactosyl-(14)-β-D-galactosyl-(14)-D-glucosylceramide

Other name(s): Galβ1-4Glcβ1-Cer α1,4-galactosyltransferase; globotriaosylceramide/CD77 synthase; histo-blood group Pk UDP-galactose

Systematic name: UDP-galactose:lactosylceramide 4^II-α-D-galactosyltransferase

Comments: For explanation of superscript II in systematic name, see 2-carb.37.

References:

1. Bailly, P., Piller, F., Cartron, J.P., Leroy, Y. and Fournet, B. Identification of UDP-galactose: lactose (lactosylceramide) α-4 and β-3 galactosyltransferases in human kidney. Biochem. Biophys. Res. Commun. 141 (1986) 84-91. [PMID: 3099784]

2. Steffensen, R., Carlier, K., Wiels, J., Levery, S.B., Stroud, M., Cedergren, B., Nilsson Sojka, B., Bennett, E.P., Jersild, C. and Clausen, H. Cloning and expression of the histo-blood group P^k UDP-galactose: Galβ1-4Glcβ1-Cer α1,4-galactosyltransferase. Molecular genetic basis of the p phenotype. J. Biol. Chem. 275 (2000) 16723-16729. [PMID: 10747952]

3. Kojima, Y., Fukumoto, S., Furukawa, K., Okajima, T., Wiels, J., Yokoyama, K., Suzuki, Y., Urano, T., Ohta, M. and Furukawa, K. Molecular cloning of globotriaosylceramide/CD77 synthase, a glycosyltransferase that initiates the synthesis of globo series glycosphingolipids. J. Biol. Chem. 275 (2000) 15152-15156. [PMID: 10748143]

*EC 2.4.2.26

Common name: protein xylosyltransferase

Reaction: Transfers a β-D-xylosyl residue from UDP-D-xylose to the serine hydroxy group of an acceptor protein substrate

Other name(s): UDP-D-xylose:core protein β-D-xylosyltransferase; UDP-D-xylose:core protein xylosyltransferase; UDP-D-xylose:proteoglycan core protein β-D-xylosyltransferase; UDP-xylose-core protein β-D-xylosyltransferase; uridine diphosphoxylose-core protein β-xylosyltransferase; uridine diphosphoxylose-protein xylosyltransferase

For diagram click here.

Systematic name: UDP-D-xylose:protein β-D-xylosyltransferase

Comments: Involved in the biosynthesis of the linkage region of glycosaminoglycan chains as part of proteoglycan biosynthesis (chondroitin, dermatan and heparan sulfates).

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 55576-38-0

References:

1. Stoolmiller, A.C., Horwitz, A.L. and Dorfman, A. Biosynthesis of the chondroitin sulfate proteoglycan. Purification and properties of xylosyltransferase. J. Biol. Chem. 247 (1972) 3525-3532. [PMID: 5030630]

2. Götting, C., Kuhn, J., Zahn, R., Brinkmann, T. and Kleesiek, K. Molecular cloning and expression of human UDP-D-xylose:proteoglycan core protein β-D-xylosyltransferase and its first isoform XT-II. J. Mol. Biol. 304 (2000) 517-528. [PMID: 11099377]