Enzyme Nomenclature

EC 2.5.1 (continued)

Continued from EC 2.5.1.1 to EC 2.5.1.50 and EC 2.5.1.51 to EC 2.5.1.100

Contents

EC 2.5.1.101 N,N'-diacetyllegionaminate synthase
EC 2.5.1.102 geranyl-pyrophosphate—olivetolic acid geranyltransferase
EC 2.5.1.103 presqualene diphosphate synthase
EC 2.5.1.104 N1-aminopropylagmatine synthase
EC 2.5.1.105 7,8-dihydropterin-6-yl-methyl-4-(β-D-ribofuranosyl)aminobenzene 5'-phosphate synthase
EC 2.5.1.106 tryprostatin B synthase
EC 2.5.1.107 verruculogen prenyltransferase
EC 2.5.1.108 2-(3-amino-3-carboxypropyl)histidine synthase
EC 2.5.1.109 brevianamide F prenyltransferase (deoxybrevianamide E-forming)
EC 2.5.1.110 12α,13α-dihydroxyfumitremorgin C prenyltransferase
EC 2.5.1.111 4-hydroxyphenylpyruvate 3-dimethylallyltransferase
EC 2.5.1.112 adenylate dimethylallyltransferase (ADP/ATP-dependent)
EC 2.5.1.113 [CysO sulfur-carrier protein]-thiocarboxylate-dependent cysteine synthase
EC 2.5.1.114 tRNAPhe (4-demethylwyosine37-C7) aminocarboxypropyltransferase
EC 2.5.1.115 homogentisate phytyltransferase
EC 2.5.1.116 homogentisate geranylgeranyltransferase
EC 2.5.1.117 homogentisate solanesyltransferase
EC 2.5.1.118 β-(isoxazolin-5-on-2-yl)-L-alanine synthase
EC 2.5.1.119 β-(isoxazolin-5-on-4-yl)-L-alanine synthase
EC 2.5.1.120 aminodeoxyfutalosine synthase
EC 2.5.1.121 5,10-dihydrophenazine-1-carboxylate 9-dimethylallyltransferase
EC 2.5.1.122 4-O-dimethylallyl-L-tyrosine synthase
EC 2.5.1.123 flaviolin linalyltransferase
EC 2.5.1.124 6-linalyl-2-O,3-dimethylflaviolin synthase
EC 2.5.1.125 7-geranyloxy-5-hydroxy-2-methoxy-3-methylnaphthalene-1,4-dione synthase
EC 2.5.1.126 norspermine synthase
EC 2.5.1.127 caldopentamine synthase
EC 2.5.1.128 N4-bis(aminopropyl)spermidine synthase
EC 2.5.1.129 flavin prenyltransferase
EC 2.5.1.130 2-carboxy-1,4-naphthoquinone phytyltransferase
EC 2.5.1.131 (4-{4-[2-(γ-L-glutamylamino)ethyl]phenoxymethyl}furan-2-yl)methanamine synthase
EC 2.5.1.132 3-deoxy-D-glycero-D-galacto-nononate 9-phosphate synthase
EC 2.5.1.133 bacteriochlorophyll a synthase
EC 2.5.1.134 cystathionine β-synthase (O-acetyl-L-serine)
EC 2.5.1.135 validamine 7-phosphate valienyltransferase
EC 2.5.1.136 2-acylphloroglucinol 4-prenyltransferase
EC 2.5.1.137 2-acyl-4-prenylphloroglucinol 6-prenyltransferase
EC 2.5.1.138 coumarin 8-geranyltransferase
EC 2.5.1.139 umbelliferone 6-dimethylallyltransferase
EC 2.5.1.140 N-(2-amino-2-carboxyethyl)-L-glutamate synthase
EC 2.5.1.141 heme o synthase
EC 2.5.1.142 nerylneryl diphosphate synthase
EC 2.5.1.143 pyridinium-3,5-biscarboxylic acid mononucleotide synthase
EC 2.5.1.144 S-sulfo-L-cysteine synthase (O-acetyl-L-serine-dependent)
EC 2.5.1.145 phosphatidylglycerol—prolipoprotein diacylglyceryl transferase
EC 2.5.1.146 3-geranyl-3-[(Z)-2-isocyanoethenyl]indole synthase
EC 2.5.1.147 5-amino-6-(D-ribitylamino)uracil—L-tyrosine 4-hydroxyphenyl transferase
EC 2.5.1.148 lycopaoctaene synthase
EC 2.5.1.149 lycopene elongase/hydratase (flavuxanthin-forming)
EC 2.5.1.150 lycopene elongase/hydratase (dihydrobisanhydrobacterioruberin-forming)
EC 2.5.1.151 alkylcobalamin dealkylase
EC 2.5.1.152 D-histidine 2-aminobutanoyltransferase

See the following file:
EC 2.5.1.1 to EC 2.5.1.50
EC 2.1.1.51 to EC 2.1.1.100

Entries

EC 2.5.1.101

Accepted name: N,N'-diacetyllegionaminate synthase

Reaction: 2,4-diacetamido-2,4,6-trideoxy-α-D-mannopyranose + phosphoenolpyruvate + H2O = N,N'-diacetyllegionaminate + phosphate

For diagram of reaction click here and mechanism click here.

Glossary: legionaminate = 5,7-diamino-3,5,7,9-tetradeoxy-D-glycero-D-galacto-non-2-ulosonate

Other name(s): SSL-1 (gene name); hpnD (gene name)

Systematic name: (2E,6E)-farnesyl-diphosphate:(2E,6E)-farnesyl-diphosphate farnesyltransferase (presqualene diphosphate-forming)

Comments: Requires a divalent metal such as Mn2+. Isolated from the bacteria Legionella pneumophila and Campylobacter jejuni, where it is involved in the biosynthesis of legionaminic acid, a virulence-associated, cell surface sialic acid-like derivative.

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

References:

1. Glaze, P.A., Watson, D.C., Young, N.M. and Tanner, M.E. Biosynthesis of CMP-N,N'-diacetyllegionaminic acid from UDP-N,N'-diacetylbacillosamine in Legionella pneumophila. Biochemistry 47 (2008) 3272-3282. [PMID: 18275154]

2. Schoenhofen, I.C., Vinogradov, E., Whitfield, D.M., Brisson, J.R. and Logan, S.M. The CMP-legionaminic acid pathway in Campylobacter: biosynthesis involving novel GDP-linked precursors. Glycobiology 19 (2009) 715-725. [PMID: 19282391]

[EC 2.5.1.101 created 2012]

EC 2.5.1.102

Accepted name: geranyl-pyrophosphate—olivetolic acid geranyltransferase

Reaction: geranyl diphosphate + 2,4-dihydroxy-6-pentylbenzoate = diphosphate + cannabigerolate

For diagram of reaction click here.

Glossary: 2,4-dihydroxy-6-pentylbenzoate = olivetolate
cannabigerolate = CBGA = 3-[(2E)-3,7-dimethylocta-2,6-dien-1-yl]-2,4-dihydroxy-6-pentylbenzoate
cannabinerolate = 3-[(2Z)-3,7-dimethylocta-2,6-dien-1-yl]-2,4-dihydroxy-6-pentylbenzoate

Other name(s): GOT (ambiguous)

Systematic name: geranyl-diphosphate:olivetolate geranyltransferase

Comments: Part of the cannabinoids biosynthetic pathway of the plant Cannabis sativa. The enzyme can also use neryl diphosphate as substrate, forming cannabinerolate.

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

References:

1. Fellermeier, M. and Zenk, M.H. Prenylation of olivetolate by a hemp transferase yields cannabigerolic acid, the precursor of tetrahydrocannabinol. FEBS Lett 427 (1998) 283-285. [PMID: 9607329]

[EC 2.5.1.102 created 2012]

EC 2.5.1.103

Accepted name: presqualene diphosphate synthase

Reaction: 2 (2E,6E)-farnesyl diphosphate = presqualene diphosphate + diphosphate

For diagram of reaction click here.

Other name(s): SSL-1 (gene name); hpnD (gene name)

Systematic name: (2E,6E)-farnesyl-diphosphate:(2E,6E)-farnesyl-diphosphate farnesyltransferase (presqualene diphosphate-forming)

Comments: Isolated from the green alga Botryococcus braunii BOT22. Unlike EC 2.5.1.21, squalene synthase, where squalene is formed in one step from farnesyl diphosphate, in this alga the intermediate presqualene diphosphate is generated and released by this enzyme. This compound is then converted into either squalene (by EC 1.3.1.96, Botryococcus squalene synthase) or botryococcene (EC 1.3.1.97, botryococcene synthase).

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

References:

1. Niehaus, T.D., Okada, S., Devarenne, T.P., Watt, D.S., Sviripa, V. and Chappell, J. Identification of unique mechanisms for triterpene biosynthesis in Botryococcus braunii. Proc. Natl. Acad. Sci. USA 108 (2011) 12260-12265. [PMID: 21746901]

2. Pan, J.J., Solbiati, J.O., Ramamoorthy, G., Hillerich, B.S., Seidel, R.D., Cronan, J.E., Almo, S.C. and Poulter, C.D. Biosynthesis of squalene from farnesyl diphosphate in bacteria: three steps catalyzed by three enzymes. ACS Cent Sci 1 (2015) 77-82. [PMID: 26258173]

[EC 2.5.1.103 created 2012]

EC 2.5.1.104

Accepted name: N1-aminopropylagmatine synthase

Reaction: S-adenosyl 3-(methylsulfanyl)propylamine + agmatine = S-methyl-5'-thioadenosine + N1-(3-aminopropyl)agmatine

For diagram of reaction click here.

Glossary: S-adenosyl 3-(methylsulfanyl)propylamine = (3-aminopropyl){[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}methylsulfonium

Other name(s): agmatine/cadaverine aminopropyl transferase; ACAPT; PF0127 (gene name); triamine/agmatine aminopropyltransferase; SpeE; agmatine aminopropyltransferase; S-adenosyl 3-(methylthio)propylamine:agmatine 3-aminopropyltransferase

Systematic name: S-adenosyl 3-(methylsulfanyl)propylamine:agmatine 3-aminopropyltransferase

Comments: The enzyme is involved in the biosynthesis of spermidine from agmatine in some archaea and bacteria. The enzyme from the Gram-negative bacterium Thermus thermophilus accepts agmatine, spermidine and norspermidine with similar catalytic efficiency. The enzymes from the archaea Pyrococcus furiosus and Thermococcus kodakarensis prefer agmatine, but can utilize cadaverine, putrescine and propane-1,3-diamine with much lower catalytic efficiency. cf. EC 2.5.1.16, spermidine synthase, and EC 2.5.1.23, sym-norspermidine synthase.

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

References:

1. Ohnuma, M., Terui, Y., Tamakoshi, M., Mitome, H., Niitsu, M., Samejima, K., Kawashima, E. and Oshima, T. N1-aminopropylagmatine, a new polyamine produced as a key intermediate in polyamine biosynthesis of an extreme thermophile, Thermus thermophilus. J. Biol. Chem. 280 (2005) 30073-30082. [PMID: 15983049]

2. Cacciapuoti, G., Porcelli, M., Moretti, M.A., Sorrentino, F., Concilio, L., Zappia, V., Liu, Z.J., Tempel, W., Schubot, F., Rose, J.P., Wang, B.C., Brereton, P.S., Jenney, F.E. and Adams, M.W. The first agmatine/cadaverine aminopropyl transferase: biochemical and structural characterization of an enzyme involved in polyamine biosynthesis in the hyperthermophilic archaeon Pyrococcus furiosus. J. Bacteriol. 189 (2007) 6057-6067. [PMID: 17545282]

3. Morimoto, N., Fukuda, W., Nakajima, N., Masuda, T., Terui, Y., Kanai, T., Oshima, T., Imanaka, T. and Fujiwara, S. Dual biosynthesis pathway for longer-chain polyamines in the hyperthermophilic archaeon Thermococcus kodakarensis. J. Bacteriol. 192 (2010) 4991-5001. [PMID: 20675472]

4. Ohnuma, M., Ganbe, T., Terui, Y., Niitsu, M., Sato, T., Tanaka, N., Tamakoshi, M., Samejima, K., Kumasaka, T. and Oshima, T. Crystal structures and enzymatic properties of a triamine/agmatine aminopropyltransferase from Thermus thermophilus. J. Mol. Biol. 408 (2011) 971-986. [PMID: 21458463]

[EC 2.5.1.104 created 2013]

EC 2.5.1.105

Accepted name: 7,8-dihydropterin-6-yl-methyl-4-(β-D-ribofuranosyl)aminobenzene 5'-phosphate synthase

Reaction: (7,8-dihydropterin-6-yl)methyl diphosphate + 4-(β-D-ribofuranosyl)aniline 5'-phosphate = N-[(7,8-dihydropterin-6-yl)methyl]-4-(β-D-ribofuranosyl)aniline 5'-phosphate + diphosphate

For diagram of reaction click here.

Other name(s): MJ0301 (gene name); dihydropteroate synthase (ambiguous)

Systematic name: (7,8-dihydropterin-6-yl)methyl diphosphate:4-(β-D-ribofuranosyl)aniline 5'-phosphate 6-hydroxymethyl-7,8-dihydropterintransferase

Comments: The enzyme, which has been studied in the archaeon Methanocaldococcus jannaschii, is involved in the biosynthesis of tetrahydromethanopterin.

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

References:

1. Xu, H., Aurora, R., Rose, G.D. and White, R.H. Identifying two ancient enzymes in Archaea using predicted secondary structure alignment. Nat. Struct. Biol. 6 (1999) 750-754. [PMID: 10426953]

[EC 2.5.1.105 created 2013]

EC 2.5.1.106

Accepted name: tryprostatin B synthase

Reaction: dimethylallyl diphosphate + brevianamide F = diphosphate + tryprostatin B

For diagram of reaction click here.

Glossary: brevianamide F = (3S,8aS)-3-(1H-indol-3-ylmethyl)hexahydropyrrolo[1,2-a]pyrazine-1,4-dione
tryprostatin B = (3S,8aS)-3-{[2-(3-methylbut-2-en-1-yl)-1H-indol-3-yl]methyl}hexahydropyrrolo[1,2-a]pyrazine-1,4-dione

Other name(s): ftmPT1 (gene name); brevianamide F prenyltransferase (ambiguous)

Systematic name: dimethylallyl-diphosphate:brevianamide-F dimethylallyl-C-2-transferase

Comments: The enzyme from the fungus Aspergillus fumigatus can also prenylate other tryptophan-containing cyclic dipeptides. Prenylation occurs mainly at C-2 [1], but also at C-3 [2]. Involved in the biosynthetic pathways of several indole alkaloids such as tryprostatins, cyclotryprostatins, spirotryprostatins, fumitremorgins and verruculogen.

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

References:

1. Grundmann, A. and Li, S.M. Overproduction, purification and characterization of FtmPT1, a brevianamide F prenyltransferase from Aspergillus fumigatus. Microbiology 151 (2005) 2199-2207. [PMID: 16000710]

2. Wollinsky, B., Ludwig, L., Xie, X. and Li, S.M. Breaking the regioselectivity of indole prenyltransferases: identification of regular C3-prenylated hexahydropyrrolo[2,3-b]indoles as side products of the regular C2-prenyltransferase FtmPT1. Org. Biomol. Chem. 10 (2012) 9262-9270. [PMID: 23090579]

[EC 2.5.1.106 created 2013]

EC 2.5.1.107

Accepted name: verruculogen prenyltransferase

Reaction: dimethylallyl diphosphate + verruculogen = diphosphate + fumitremorgin A

For diagram of reaction click here.

Glossary: verruculogen = (5R,10S,10aR,14aS,15bS)-10,10a-dihydroxy-6-methoxy-2,2-dimethyl-5-(2-methylprop-1-en-1-yl)-1,10,10a,14,14a,15b-hexahydro-12H-3,4-dioxa-5a,11a,15a-triazacycloocta[1,2,3-lm]indeno[5,6-b]fluorene-11,15(2H,13H)-dione
fumitremorgin A = (5R,10S,10aR,14aS,15bS)-10a-hydroxy-7-methoxy-2,2-dimethyl-10-[(3-methylbut-2-en-1-yl)oxy]-5-(2-methylprop-1-en-1-yl)-1,10,10a,14,14a,15b-hexahydro-12H-3,4-dioxa-5a,11a,15a-triazacycloocta[1,2,3-lm]indeno[5,6-b]fluorene-11,15(H,13H)-dione

Other name(s): FtmPT3

Systematic name: dimethylallyl-diphosphate:verruculogen dimethylallyl-O-transferase

Comments: Found in a number of fungi. Catalyses the last step in the biosynthetic pathway of the indole alkaloid fumitremorgin A. The enzyme from the fungus Neosartorya fischeri is also active with fumitremorgin B and 12α,13α-dihydroxyfumitremorgin C.

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

References:

1. Mundt, K., Wollinsky, B., Ruan, H.L., Zhu, T. and Li, S.M. Identification of the verruculogen prenyltransferase FtmPT3 by a combination of chemical, bioinformatic and biochemical approaches. ChemBioChem. 13 (2012) 2583-2592. [PMID: 23109474]

[EC 2.5.1.107 created 2013]

EC 2.5.1.108

Accepted name: 2-(3-amino-3-carboxypropyl)histidine synthase

For diagram of reaction click here.

Reaction: S-adenosyl-L-methionine + L-histidine-[translation elongation factor 2] = S-methyl-5-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine-[translation elongation factor 2]

Other name(s): Dph2

Systematic name: S-adenosyl-L-methionine:L-histidine-[translation elongation factor 2] 2-[(3S)-3-amino-3-carboxypropyl]transferase

Comments: A [4Fe-4S] enzyme that modifies a histidine residue of the translation elongation factor 2 (EF2) via a 3-amino-3-carboxypropyl radical. The enzyme is present in archae and eukaryotes but not in eubacteria. The relevant histidine of EF2 is His715 in mammals, His699 in yeast and His600 in Pyrococcus horikoshii. Part of diphthamide biosynthesis.

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

References:

1. Liu, S., Milne, G.T., Kuremsky, J.G., Fink, G.R. and Leppla, S.H. Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2. Mol. Cell Biol. 24 (2004) 9487-9497. [PMID: 15485916]

2. Zhang, Y., Zhu, X., Torelli, A.T., Lee, M., Dzikovski, B., Koralewski, R.M., Wang, E., Freed, J., Krebs, C., Ealick, S.E. and Lin, H. Diphthamide biosynthesis requires an organic radical generated by an iron-sulphur enzyme. Nature 465 (2010) 891-896. [PMID: 20559380]

3. Zhu, X., Dzikovski, B., Su, X., Torelli, A.T., Zhang, Y., Ealick, S.E., Freed, J.H. and Lin, H. Mechanistic understanding of Pyrococcus horikoshii Dph2, a [4Fe-4S] enzyme required for diphthamide biosynthesis. Mol Biosyst 7 (2011) 74-81. [PMID: 20931132]

[EC 2.5.1.108 created 2013]

EC 2.5.1.109

Accepted name: brevianamide F prenyltransferase (deoxybrevianamide E-forming)

Reaction: dimethylallyl diphosphate + brevianamide F = diphosphate + deoxybrevianamide E

For diagram of reaction click here.

Glossary: brevianamide F = (3S,8aS)-3-(1H-indol-3-ylmethyl)hexahydropyrrolo[1,2-a]pyrazine-1,4-dione
deoxybrevianamide E = (3S,8aS)-3-{[2-(2-methylbut-3-en-2-yl)-1H-indol-3-yl]methyl}-octahydropyrrolo[1,2-a]piperazine-1,4-dione

Other name(s): NotF; BrePT; brevianamide F reverse prenyltransferase

Systematic name: dimethylallyl-diphosphate:brevianamide-F tert-dimethylallyl-C-2-transferase

Comments: The enzyme from the fungus Aspergilus sp. MF297-2 is specific for brevianamide F [1], while the enzyme from Aspergillus versicolor accepts a broad range of trytophan-containing cyclic dipeptides [2]. Involved in the biosynthetic pathways of several indole alkaloids such as paraherquamides and malbrancheamides.

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

References:

1. Ding, Y., de Wet, J.R., Cavalcoli, J., Li, S., Greshock, T.J., Miller, K.A., Finefield, J.M., Sunderhaus, J.D., McAfoos, T.J., Tsukamoto, S., Williams, R.M. and Sherman, D.H. Genome-based characterization of two prenylation steps in the assembly of the stephacidin and notoamide anticancer agents in a marine-derived Aspergillus sp. J. Am. Chem. Soc. 132 (2010) 12733-12740. [PMID: 20722388]

2. Yin, S., Yu, X., Wang, Q., Liu, X.Q. and Li, S.M. Identification of a brevianamide F reverse prenyltransferase BrePT from Aspergillus versicolor with a broad substrate specificity towards tryptophan-containing cyclic dipeptides. Appl. Microbiol. Biotechnol. 97 (2013) 1649-1660. [PMID: 22660767]

[EC 2.5.1.109 created 2013]

EC 2.5.1.110

Accepted name: 12α,13α-dihydroxyfumitremorgin C prenyltransferase

Reaction: dimethylallyl diphosphate + 12α,13α-dihydroxyfumitremorgin C = diphosphate + fumitremorgin B

For diagram of reaction click here.

Glossary: 12α,13α-dihydroxyfumitremorgin = (5aR,6S,12S,14aS)-5a,6-dihydroxy-9-methoxy-12-(2-methylprop-1-en-1-yl)-1,2,3,5a,6,11,12,14a-octahydro-5H,14H-pyrrolo[1'',2'':4',5']pyrazino[1',2':1,6]pyrido[3,4-b]indole-5,14-dione
fumitremorgin B = (5aR,6S,12S,14aS)-5a,6-dihydroxy-9-methoxy-11-(3-methylbut-2-en-1-yl)-12-(2-methylprop-1-en-1-yl)-1,2,3,5a,6,11,12,14a-octahydro-5H,14H-pyrrolo[1'',2'':4',5']pyrazino[1',2':1,6]pyrido[3,4-b]indole-5,14-dione

Other name(s): ftmH (gene name); FtmPT2

Systematic name: dimethylallyl-diphosphate:12α,13α-dihydroxyfumitremorgin C dimethylallyl-N-1-transferase

Comments: The enzyme from the fungus Aspergillus fumigatus also shows some activity with fumitremorgin C. Involved in the biosynthetic pathways of several indole alkaloids such as fumitremorgins and verruculogen.

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

References:

1. Grundmann, A., Kuznetsova, T., Afiyatullov, S.Sh and Li, S.M. FtmPT2, an N-prenyltransferase from Aspergillus fumigatus, catalyses the last step in the biosynthesis of fumitremorgin B. ChemBioChem. 9 (2008) 2059-2063. [PMID: 18683158]

[EC 2.5.1.110 created 2013]

EC 2.5.1.111

Accepted name: 4-hydroxyphenylpyruvate 3-dimethylallyltransferase

Reaction: dimethylallyl diphosphate + 4-hydroxyphenylpyruvate = diphosphate + 3-dimethylallyl-4-hydroxyphenylpyruvate

For diagram of reaction, click here

Glossary: 3-dimethylallyl-4-hydroxyphenylpyruvate = 3-[4-hydroxy-3-(3-methylbut-2-en-1-yl)phenyl]-2-oxopropanoate

Other name(s): CloQ; 4HPP dimethylallyltransferase; NovQ

Systematic name: dimethylallyl diphosphate:4-hydroxyphenylpyruvate 3-dimethylallyltransferase

Comments: The enzyme is involved in the biosynthesis of the 3-dimethylallyl-4-hydroxyphenylpyruvate moiety of the aminocoumarin antibiotics clorobiocin and novobiocin [1].

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

References:

1. Pojer, F., Wemakor, E., Kammerer, B., Chen, H., Walsh, C.T., Li, S.M. and Heide, L. CloQ, a prenyltransferase involved in clorobiocin biosynthesis. Proc. Natl. Acad. Sci. USA 100 (2003) 2316-2321. [PMID: 12618544]

2. Keller, S., Pojer, F., Heide, L. and Lawson, D.M. Crystallization and preliminary X-ray analysis of the aromatic prenyltransferase CloQ from the clorobiocin biosynthetic cluster of Streptomyces roseochromogenes. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62 (2006) 1153-1155. [PMID: 17077503]

3. Metzger, U., Keller, S., Stevenson, C.E., Heide, L. and Lawson, D.M. Structure and mechanism of the magnesium-independent aromatic prenyltransferase CloQ from the clorobiocin biosynthetic pathway. J. Mol. Biol. 404 (2010) 611-626. [PMID: 20946900]

4. Ozaki, T., Mishima, S., Nishiyama, M. and Kuzuyama, T. NovQ is a prenyltransferase capable of catalyzing the addition of a dimethylallyl group to both phenylpropanoids and flavonoids. J. Antibiot. (Tokyo) 62 (2009) 385-392. [PMID: 19557032]

[EC 2.5.1.111 created 2013]

EC 2.5.1.112

Accepted name: adenylate dimethylallyltransferase (ADP/ATP-dependent)

Reaction: (1) dimethylallyl diphosphate + ADP = diphosphate + N6-(dimethylallyl)adenosine 5′-diphosphate
(2) dimethylallyl diphosphate + ATP = diphosphate + N6-(dimethylallyl)adenosine 5′-triphosphate

For diagram of reaction, click here

Other name(s): cytokinin synthase (ambiguous); isopentenyltransferase (ambiguous); 2-isopentenyl-diphosphate:ADP/ATP Δ2-isopentenyltransferase; adenylate isopentenyltransferase (ambiguous); dimethylallyl diphosphate:ATP/ADP isopentenyltransferase: IPT

Systematic name: dimethylallyl-diphosphate:ADP/ATP dimethylallyltransferase

Comments: Involved in the biosynthesis of cytokinins in plants. The IPT4 isoform from the plant Arabidopsis thaliana is specific for ADP and ATP [1]. Other isoforms, such as IPT1 from Arabidopsis thaliana [1,2] and the enzyme from the common hop, Humulus lupulus [3], also have a lower activity with AMP [cf. EC 2.5.1.27, adenylate dimethylallyltransferase (AMP-dependent)].

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

References:

1. Kakimoto, T. Identification of plant cytokinin biosynthetic enzymes as dimethylallyl diphosphate:ATP/ADP isopentenyltransferases. Plant Cell Physiol 42 (2001) 677-685. [PMID: 11479373]

2. Takei, K., Sakakibara, H. and Sugiyama, T. Identification of genes encoding adenylate isopentenyltransferase, a cytokinin biosynthesis enzyme, in Arabidopsis thaliana. J. Biol. Chem. 276 (2001) 26405-26410. [PMID: 11313355]

3. Sakano, Y., Okada, Y., Matsunaga, A., Suwama, T., Kaneko, T., Ito, K., Noguchi, H. and Abe, I. Molecular cloning, expression, and characterization of adenylate isopentenyltransferase from hop (Humulus lupulus L.). Phytochemistry 65 (2004) 2439-2446. [PMID: 15381407]

[EC 2.5.1.112 created 2013]

EC 2.5.1.113

Accepted name: [CysO sulfur-carrier protein]-thiocarboxylate-dependent cysteine synthase

Reaction: O-phospho-L-serine + [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)SH = [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)-S-L-cysteine + phosphate

Other name(s): CysM

Systematic name: O-phospho-L-serine:thiocarboxylated [CysO sulfur-carrier protein] 2-amino-2-carboxyethyltransferase

Comments: A pyridoxal-phosphate protein. The enzyme participates in an alternative pathway for L-cysteine biosynthesis that involves a protein-bound thiocarboxylate as the sulfide donor. The enzyme from the bacterium Mycobacterium tuberculosis also has very low activity with O3-acetyl-L-serine (cf. EC 2.5.1.65, O-phosphoserine sulfhydrylase).

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

References:

1. O'Leary, S.E., Jurgenson, C.T., Ealick, S.E. and Begley, T.P. O-Phospho-L-serine and the thiocarboxylated sulfur carrier protein CysO-COSH are substrates for CysM, a cysteine synthase from Mycobacterium tuberculosis. Biochemistry 47 (2008) 11606-11615. [PMID: 18842002]

2. Jurgenson, C.T., Burns, K.E., Begley, T.P. and Ealick, S.E. Crystal structure of a sulfur carrier protein complex found in the cysteine biosynthetic pathway of Mycobacterium tuberculosis. Biochemistry 47 (2008) 10354-10364. [PMID: 18771296]

3. Ågren, D., Schnell, R., Oehlmann, W., Singh, M. and Schneider, G. Cysteine synthase (CysM) of Mycobacterium tuberculosis is an O-phosphoserine sulfhydrylase: evidence for an alternative cysteine biosynthesis pathway in mycobacteria. J. Biol. Chem. 283 (2008) 31567-31574. [PMID: 18799456]

4. Ågren, D., Schnell, R. and Schneider, G. The C-terminal of CysM from Mycobacterium tuberculosis protects the aminoacrylate intermediate and is involved in sulfur donor selectivity. FEBS Lett 583 (2009) 330-336. [PMID: 19101553]

[EC 2.5.1.113 created 2013]

EC 2.5.1.114

Accepted name: tRNAPhe (4-demethylwyosine37-C7) aminocarboxypropyltransferase

Reaction: S-adenosyl-L-methionine + 4-demethylwyosine37 in tRNAPhe = S-methyl-5′-thioadenosine + 7-[(3S)-3-amino-3-carboxypropyl]-4-demethylwyosine37 in tRNAPhe

For diagram of reaction, click here

Glossary: 4-demethylwyosine = imG-14 = 6-methyl-3-(β-D-ribofuranosyl)-3,5-dihydro-9H-imidazo[1,2-a]purin-9-one
7-[(3S)-3-amino-3-carboxypropyl]-4-demethylwyosine = yW-89

Other name(s): TYW2; tRNA-yW synthesizing enzyme-2; TRM12 (gene name); taw2 (gene name)

Systematic name: S-adenosyl-L-methionine:tRNAPhe (4-demethylwyosine37-C7)-[(3S)-3-amino-3-carboxypropyl]transferase

Comments: The enzyme, which is found in all eukaryotes and in the majority of Euryarchaeota (but not in the Crenarchaeota), is involved in the hypermodification of the guanine nucleoside at position 37 of tRNA leading to formation of assorted wye bases. This modification is essential for translational reading-frame maintenance. The eukaryotic enzyme is involved in biosynthesis of the tricyclic base wybutosine, which is found only in tRNAPhe.

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

References:

1. Umitsu, M., Nishimasu, H., Noma, A., Suzuki, T., Ishitani, R. and Nureki, O. Structural basis of AdoMet-dependent aminocarboxypropyl transfer reaction catalyzed by tRNA-wybutosine synthesizing enzyme, TYW2. Proc. Natl. Acad. Sci. USA 106 (2009) 15616-15621. [PMID: 19717466]

2. Rodriguez, V., Vasudevan, S., Noma, A., Carlson, B.A., Green, J.E., Suzuki, T. and Chandrasekharappa, S.C. Structure-function analysis of human TYW2 enzyme required for the biosynthesis of a highly modified Wybutosine (yW) base in phenylalanine-tRNA. PLoS One 7 (2012) e39297. [PMID: 22761755]

3. de Crecy-Lagard, V., Brochier-Armanet, C., Urbonavicius, J., Fernandez, B., Phillips, G., Lyons, B., Noma, A., Alvarez, S., Droogmans, L., Armengaud, J. and Grosjean, H. Biosynthesis of wyosine derivatives in tRNA: an ancient and highly diverse pathway in Archaea. Mol Biol Evol 27 (2010) 2062-2077. [PMID: 20382657]

[EC 2.5.1.114 created 2013]

EC 2.5.1.115

Accepted name: homogentisate phytyltransferase

Reaction: phytyl diphosphate + homogentisate = diphosphate + 2-methyl-6-phytylbenzene-1,4-diol + CO2

For diagram of reaction click here.

Glossary: 2-methyl-6-phytylbenzene-1,4-diol = MPBQ

Other name(s): HPT; VTE2 (gene name)

Systematic name: phytyl diphosphate:homogentisate phytyltransferase

Comments: Requires Mg2+ for activity [3]. Involved in the biosynthesis of the vitamin E tocopherols. While the enzyme from the cyanobacterium Synechocystis PCC 6803 has an appreciable activity with geranylgeranyl diphosphate (EC 2.5.1.116, homogentisate geranylgeranyltransferase), the enzyme from the plant Arabidopsis thaliana has only a low activity with that substrate [1,3,4].

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

References:

1. Collakova, E. and DellaPenna, D. Isolation and functional analysis of homogentisate phytyltransferase from Synechocystis sp. PCC 6803 and Arabidopsis. Plant Physiol. 127 (2001) 1113-1124. [PMID: 11706191]

2. Savidge, B., Weiss, J.D., Wong, Y.H., Lassner, M.W., Mitsky, T.A., Shewmaker, C.K., Post-Beittenmiller, D. and Valentin, H.E. Isolation and characterization of homogentisate phytyltransferase genes from Synechocystis sp. PCC 6803 and Arabidopsis. Plant Physiol. 129 (2002) 321-332. [PMID: 12011362]

3. Sadre, R., Gruber, J. and Frentzen, M. Characterization of homogentisate prenyltransferases involved in plastoquinone-9 and tocochromanol biosynthesis. FEBS Lett 580 (2006) 5357-5362. [PMID: 16989822]

4. Yang, W., Cahoon, R.E., Hunter, S.C., Zhang, C., Han, J., Borgschulte, T. and Cahoon, E.B. Vitamin E biosynthesis: functional characterization of the monocot homogentisate geranylgeranyl transferase. Plant J. 65 (2011) 206-217. [PMID: 21223386]

[EC 2.5.1.115 created 2014]

EC 2.5.1.116

Accepted name: homogentisate geranylgeranyltransferase

Reaction: geranylgeranyl diphosphate + homogentisate = diphosphate + 6-geranylgeranyl-2-methylbenzene-1,4-diol + CO2

For diagram of reaction click here.

Glossary: 6-geranylgeranyl-2-methylbenzene-1,4-diol = MGGBQ

Other name(s): HGGT; slr1736 (gene name)

Systematic name: geranylgeranyl diphosphate:homogentisate geranylgeranyltransferase

Comments: Requires Mg2+ for activity. Involved in the biosynthesis of the vitamin E, tocotrienols. While the enzyme from the bacterium Synechocystis PCC 6803 has higher activity with phytyl diphosphate (EC 2.5.1.115, homogentisate phytyltransferase), the enzymes from barley, rice and wheat have only a low activity with that substrate [2].

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

References:

1. Collakova, E. and DellaPenna, D. Isolation and functional analysis of homogentisate phytyltransferase from Synechocystis sp. PCC 6803 and Arabidopsis. Plant Physiol. 127 (2001) 1113-1124. [PMID: 11706191]

2. Cahoon, E.B., Hall, S.E., Ripp, K.G., Ganzke, T.S., Hitz, W.D. and Coughlan, S.J. Metabolic redesign of vitamin E biosynthesis in plants for tocotrienol production and increased antioxidant content. Nat. Biotechnol. 21 (2003) 1082-1087. [PMID: 12897790]

3. Yang, W., Cahoon, R.E., Hunter, S.C., Zhang, C., Han, J., Borgschulte, T. and Cahoon, E.B. Vitamin E biosynthesis: functional characterization of the monocot homogentisate geranylgeranyl transferase. Plant J. 65 (2011) 206-217. [PMID: 21223386]

[EC 2.5.1.116 created 2014]

EC 2.5.1.117

Accepted name: homogentisate solanesyltransferase

Reaction: all-trans-nonaprenyl diphosphate + homogentisate = diphosphate + 2-methyl-6-all-trans-nonaprenylbenzene-1,4-diol + CO2

For diagram of reaction click here.

Glossary: 2-methyl-6-all-trans-nonaprenylbenzene-1,4-diol = 2-methyl-6-solanesylbenzene-1,4-diol = MSBQ

Other name(s): HST; PDS2 (gene name)

Systematic name: all-trans-nonaprenyl diphosphate:homogentisate nonaprenyltransferase

Comments: Requires Mg2+ for activity. Part of the biosynthesis pathway of plastoquinol-9. The enzymes purified from the plant Arabidopsis thaliana and the alga Chlamydomonas reinhardtii are also active in vitro with unsaturated C10-C20 prenyl diphosphates, producing main products that are not decarboxylated [2].

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

References:

1. Sadre, R., Gruber, J. and Frentzen, M. Characterization of homogentisate prenyltransferases involved in plastoquinone-9 and tocochromanol biosynthesis. FEBS Lett 580 (2006) 5357-5362. [PMID: 16989822]

2. Sadre, R., Frentzen, M., Saeed, M. and Hawkes, T. Catalytic reactions of the homogentisate prenyl transferase involved in plastoquinone-9 biosynthesis. J. Biol. Chem. 285 (2010) 18191-18198. [PMID: 20400515]

[EC 2.5.1.117 created 2014]

EC 2.5.1.118

Accepted name: β-(isoxazolin-5-on-2-yl)-L-alanine synthase

Reaction: O3-acetyl-L-serine + isoxazolin-5-one = 3-(5-oxoisoxazolin-2-yl)-L-alanine + acetate

For diagram of reaction click here.

Systematic name: O3-acetyl-L-serine:isoxazolin-5-one 2-(2-amino-2-carboxyethyl)transferase

Comments: The enzyme from the plants Lathyrus odoratus (sweet pea) and L. sativus (grass pea) also forms 3-(5-oxoisoxazolin-4-yl)-L-alanine in vitro (cf. EC 2.5.1.119). However, only 3-(5-oxoisoxazolin-2-yl)-L-alanine is formed in vivo. 3-(5-oxoisoxazolin-2-yl)-L-alanine is the biosynthetic precursor of the neurotoxin N3-oxalyl-L-2,3-diaminopropanoic acid, the cause of lathyrism. Closely related and possibly identical to EC 2.5.1.47, cysteine synthase, and EC 2.5.1.51, β-pyrazolylalanine synthase.

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

References:

1. Ikegami, F., Kamiya, M., Kuo, Y.H., Lambein, F. and Murakoshi, I. Enzymatic synthesis of two isoxazolylalanine isomers by cysteine synthases in Lathyrus species. Biol. Pharm. Bull. 19 (1996) 1214-1215. [PMID: 8889043]

[EC 2.5.1.118 created 2014]

EC 2.5.1.119

Accepted name: β-(isoxazolin-5-on-4-yl)-L-alanine synthase

Reaction: O3-acetyl-L-serine + isoxazolin-5-one = 3-(5-oxoisoxazolin-4-yl)-L-alanine + acetate

For diagram of reaction click here.

Systematic name: O3-acetyl-L-serine:isoxazolin-5-one 4-(2-amino-2-carboxyethyl)transferase

Comments: 3-(5-Oxoisoxazolin-4-yl)-L-alanine is an antifungal antibiotic produced by the bacterium Streptomyces platensis. The enzymes from the plants Lathyrus odoratus (sweet pea) , L. sativus (grass pea) and Citrullus vulgaris (watermelon) that catalyse EC 2.5.1.118 (β-(isoxazolin-5-on-2-yl)-L-alanine synthase) also catalyse this reaction in vitro, but not in vivo. Closely related and possibly identical to EC 2.5.1.47, cysteine synthase, and EC 2.5.1.51, β-pyrazolylalanine synthase.

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

References:

1. Ikegami, F., Kamiya, M., Kuo, Y.H., Lambein, F. and Murakoshi, I. Enzymatic synthesis of two isoxazolylalanine isomers by cysteine synthases in Lathyrus species. Biol. Pharm. Bull. 19 (1996) 1214-1215. [PMID: 8889043]

[EC 2.5.1.119 created 2014]

EC 2.5.1.120

Accepted name: aminodeoxyfutalosine synthase

Reaction: S-adenosyl-L-methionine + 3-[(1-carboxyvinyl)oxy]benzoate + H2O = 6-amino-6-deoxyfutalosine + L-methionine + HCO3-

For diagram of reaction click here.

Glossary: 6-amino-6-deoxyfutalosine = 3-{3-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]propanoyl}benzoate

Other name(s): MqnE; AFL synthase; aminofutalosine synthase

Systematic name: S-adenosyl-L-methionine:3-[(1-carboxyvinyl)-oxy]benzoate adenosyltransferase (HCO3--hydrolysing, 6-amino-6-deoxyfutalosine-forming)

Comments: This enzyme is a member of the ’AdoMet radical’ (radical SAM) family. S-Adenosyl-L-methionine acts as both a radical generator and as the source of the transferred adenosyl group. The enzyme, found in several bacterial species, is part of the futalosine pathway for menaquinone biosynthesis.

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

References:

1. Mahanta, N., Fedoseyenko, D., Dairi, T. and Begley, T.P. Menaquinone biosynthesis: formation of aminofutalosine requires a unique radical SAM enzyme. J. Am. Chem. Soc. 135 (2013) 15318-15321. [PMID: 24083939]

[EC 2.5.1.120 created 2014]

EC 2.5.1.121

Accepted name: 5,10-dihydrophenazine-1-carboxylate 9-dimethylallyltransferase

Reaction: dimethylallyl diphosphate + 5,10-dihydrophenazine-1-carboxylate = diphosphate + 9-(dimethylallyl)-5,10-dihydrophenazine-1-carboxylate

For diagram of reaction click here.

Glossary: 9-(dimethylallyl)-5,10-dihydrophenazine-1-carboxylate = 9-(3-methylbut-2-en-1-yl)-5,10-dihydrophenazine-1-carboxylate

Other name(s): PpzP; dihydrophenazine-1-carboxylate dimethylallyltransferase; 5,10-dihydrophenazine 1-carboxylate dimethylallyltransferase

Systematic name: dimethylallyl diphosphate:5,10-dihydrophenazine-1-carboxylate 9-dimethylallyltransferase

Comments: The enzyme is involved in the biosynthesis of prenylated phenazines by the bacterium Streptomyces anulatus. It is specific for both dimethylallyl diphosphate and 5,10-dihydrophenazine-1-carboxylate.

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

References:

1. Saleh, O., Gust, B., Boll, B., Fiedler, H.P. and Heide, L. Aromatic prenylation in phenazine biosynthesis: dihydrophenazine-1-carboxylate dimethylallyltransferase from Streptomyces anulatus. J. Biol. Chem. 284 (2009) 14439-14447. [PMID: 19339241]

[EC 2.5.1.121 created 2014]

EC 2.5.1.122

Accepted name: 4-O-dimethylallyl-L-tyrosine synthase

Reaction: dimethylallyl diphosphate + L-tyrosine = diphosphate + 4-O-dimethylallyl-L-tyrosine

Other name(s): SirD

Systematic name: dimethylallyl diphosphate:L-tyrosine 4-O-dimethylallyltransferase

Comments: The enzyme is involved in biosynthesis of the phytotoxin sirodesmin PL by the phytopathogenic ascomycete Leptosphaeria maculans.

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

References:

1. Kremer, A. and Li, S.M. A tyrosine O-prenyltransferase catalyses the first pathway-specific step in the biosynthesis of sirodesmin PL. Microbiology 156 (2010) 278-286. [PMID: 19762440]

2. Zou, H.X., Xie, X., Zheng, X.D. and Li, S.M. The tyrosine O-prenyltransferase SirD catalyzes O-, N-, and C-prenylations. Appl. Microbiol. Biotechnol. 89 (2011) 1443-1451. [PMID: 21038099]

[EC 2.5.1.122 created 2014]

EC 2.5.1.123

Accepted name: flaviolin linalyltransferase

Reaction: geranyl diphosphate + flaviolin = 3-linalylflaviolin + diphosphate

For diagram of reaction click here.

Glossary: flaviolin = 2,5,7-trihydroxynaphthalene-1,4-dione
3-linalylflaviolin = 2,5,7-trihydroxy-3-(3,7-dimethylocta-1,6-dien-3-yl)naphthalene-1,4-dione

Other name(s): Fnq26

Systematic name: geranyl-diphosphate:flaviolin 3-linalyltransferase

Comments: Does not require Mg2+ or any other metal ions. Isolated from the bacterium Streptomyces cinnamonensis. In vitro the enzyme also forms traces of 3-geranylflaviolin.

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

References:

1. Haagen, Y., Unsold, I., Westrich, L., Gust, B., Richard, S.B., Noel, J.P. and Heide, L. A soluble, magnesium-independent prenyltransferase catalyzes reverse and regular C-prenylations and O-prenylations of aromatic substrates. FEBS Lett 581 (2007) 2889-2893. [PMID: 17543953]

[EC 2.5.1.123 created 2014]

EC 2.5.1.124

Accepted name: 6-linalyl-2-O,3-dimethylflaviolin synthase

Reaction: geranyl diphosphate + 2-O,3-dimethylflaviolin = diphosphate + 6-linalyl-2-O,3-dimethylflaviolin

Glossary: flaviolin = 2,5,7-trihydroxy-1,4-naphthoquinone
2-O,3-dimethylflaviolin = 5,7-dihydroxy-2-methoxy-3-methylnaphthalene-1,4-dione
6-linalyl-2-O,3-dimethylflaviolin = 6-(3,7-dimethylocta-1,6-dien-3-yl)-5,7-dihydroxy-2-methoxy-3-methylnaphthalene-1,4-dione

Other name(s): Fur7; 6-(3,7-dimethylocta-1,6-dien-3-yl)-5,7-dihydroxy-2-methoxy-3-methylnaphthalene-1,4-dione synthase

Systematic name: geranyl diphosphate:2-O-methyl-3-methylflaviolin geranyltransferase (6-linalyl-2-O,3-dimethylflaviolin-forming)

Comments: The enzyme is involved in biosynthesis of the polyketide-isoprenoid furaquinocin D in the bacterium Streptomyces sp. KO-3988. It catalyses the transfer of a geranyl group to 2-O,3-dimethylflaviolin to yield 6-linalyl-2-O,3-dimethylflaviolin and 7-O-geranyl-2-O,3-dimethylflaviolin (cf. EC 2.5.1.125, 7-geranyloxy-5-hydroxy-2-methoxy-3-methylnaphthalene-1,4-dione synthase) in a 10:1 ratio.

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

References:

1. Kumano, T., Tomita, T., Nishiyama, M. and Kuzuyama, T. Functional characterization of the promiscuous prenyltransferase responsible for furaquinocin biosynthesis: identification of a physiological polyketide substrate and its prenylated reaction products. J. Biol. Chem. 285 (2010) 39663-39671. [PMID: 20937800]

[EC 2.5.1.124 created 2014]

EC 2.5.1.125

Accepted name: 7-geranyloxy-5-hydroxy-2-methoxy-3-methylnaphthalene-1,4-dione synthase

Reaction: geranyl diphosphate + 2-O,3-dimethylflaviolin = diphosphate + 7-O-geranyl-2-O,3-dimethylflaviolin

Glossary: flaviolin = 2,5,7-trihydroxy-1,4-naphthoquinone
2-O,3-dimethylflaviolin = 5,7-dihydroxy-2-methoxy-3-methylnaphthalene-1,4-dione
7-O-geranyl-2-O,3-dimethylflaviolin = 7-{[(2E)-3,7-dimethylocta-2,6-dien-1-yl]oxy}-5-hydroxy-2-methoxy-3-methylnaphthalene-1,4-dione

Other name(s): Fur7

Systematic name: geranyl diphosphate:2-O,3-dimethylflaviolin geranyltransferase (7-O-geranyl-2-O,3-dimethylflaviolin-forming)

Comments: The enzyme is involved in furaquinocin biosynthesis in the bacterium Streptomyces sp. KO-3988. It catalyses the transfer of a geranyl group to 2-O,3-dimethylflaviolin to yield 7-O-geranyl-2-O,3-dimethylflaviolin and 6-linalyl-2-O,3-dimethylflaviolin (cf. EC 2.5.1.124, 6-linalyl-2-O,3-dimethylflaviolin synthase) in a 1:10 ratio.

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

References:

1. Kumano, T., Tomita, T., Nishiyama, M. and Kuzuyama, T. Functional characterization of the promiscuous prenyltransferase responsible for furaquinocin biosynthesis: identification of a physiological polyketide substrate and its prenylated reaction products. J. Biol. Chem. 285 (2010) 39663-39671. [PMID: 20937800]

[EC 2.5.1.125 created 2014]

EC 2.5.1.126

Accepted name: norspermine synthase

Reaction: S-adenosyl 3-(methylsulfanyl)propylamine + norspermidine = S-methyl-5'-thioadenosine + norspermine

Glossary: norspermidine = bis(3-aminopropyl)amine
norspermine = N,N'-bis(3-aminopropyl)-1,3-propanediamine
spermidine = N-(3-aminopropyl)-1,4-butanediamine
thermospermine = N-{3-[(3-aminopropyl)amino]propyl}-1,4-butanediamine

Other name(s): long-chain polyamine synthase (ambiguous); S-adenosyl 3-(methylthio)propylamine:norspermidine 3-aminopropyltransferase

Systematic name: S-adenosyl 3-(methylsulfanyl)propylamine:norspermidine 3-aminopropyltransferase

Comments: The enzyme, characterized from the thermophilic archaeon Pyrobaculum aerophilum, can also synthesize norspermidine from propane-1,3-diamine and thermospermine from spermidine (with lower activity). The long-chain polyamines stabilize double-stranded DNA at high temperatures. In contrast to EC 2.5.1.127, caldopentamine synthase, this enzyme does not accept norspermine as a substrate.

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

References:

1. Knott, J.M. Biosynthesis of long-chain polyamines by crenarchaeal polyamine synthases from Hyperthermus butylicus and Pyrobaculum aerophilum. FEBS Lett 583 (2009) 3519-3524. [PMID: 19822146]

[EC 2.5.1.126 created 2014]

EC 2.5.1.127

Accepted name: caldopentamine synthase

Reaction: S-adenosyl 3-(methylsulfanyl)propylamine + norspermine = S-methyl-5'-thioadenosine + caldopentamine

Glossary: caldopentamine = N-(3-aminopropyl)-N'-{3-[(3-aminopropyl)amino]propyl}-1,3-propanediamine
norspermidine = N-(3-aminopropyl)-1,4-butanediamine
norspermine = N,N'-bis(3-aminopropyl)-1,3-propanediamine
spermidine = N-(3-aminopropyl)-1,4-butanediamine
thermospermine = N-{3-[(3-aminopropyl)amino]propyl}-1,4-butanediamine

Other name(s): long-chain polyamine synthase (ambiguous); S-adenosyl 3-(methylthio)propylamine:norspermine 3-aminopropyltransferase

Systematic name: S-adenosyl 3-(methylsulfanyl)propylamine:norspermine 3-aminopropyltransferase

Comments: The enzyme, characterized from the thermophilic archaeon Hyperthermus butylicus, can also synthesize norspermine from norspermidine and thermospermine from spermidine (with lower activity). The long-chain polyamines stabilize double-stranded DNA at high temperatures. In contrast to EC 2.5.1.23, sym-norspermidine synthase and EC 2.5.1.126, norspermine synthase, this enzyme shows no activity with propane-1,3-diamine.

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

References:

1. Knott, J.M. Biosynthesis of long-chain polyamines by crenarchaeal polyamine synthases from Hyperthermus butylicus and Pyrobaculum aerophilum. FEBS Lett 583 (2009) 3519-3524. [PMID: 19822146]

[EC 2.5.1.127 created 2014]

EC 2.5.1.128

Reaction: 2 S-adenosyl 3-(methylsulfaynyl)propylamine + spermidine = 2 S-methyl-5′-thioadenosine + N4-bis(aminopropyl)spermidine (overall reaction)
(1a) S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = S-methyl-5′-thioadenosine + N4-aminopropylspermidine
(1b) S-adenosyl 3-(methylsulfanyl)propylamine + N4-aminopropylspermidine = S-methyl-5′-thioadenosine + N4-bis(aminopropyl)spermidine

Glossary: spermidine = N-(3-aminopropyl)butane-1,4-diamine
N4-aminopropylspermidine = N,N′-bis(3-aminopropyl)butane-1,4-diamine
N4-bis(aminopropyl)spermidine = N,N,N′-tris(3-aminopropyl)butane-1,4-diamine

Systematic name: S-adenosyl 3-(methylsulfanyl)propylamine:spermidine 3-aminopropyltransferase [N4-bis(aminopropyl)spermidine synthesizing]

Comments: The enzyme, characterized from the thermophilic archaeon Thermococcus kodakarensis, synthesizes the branched-chain polyamine N4-bis(aminopropyl)spermidine, which is required for cell growth at high-temperature. When spermine is used as substrate, the enzyme forms N4-aminopropylspermine.

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

References:

1. Okada, K., Hidese, R., Fukuda, W., Niitsu, M., Takao, K., Horai, Y., Umezawa, N., Higuchi, T., Oshima, T., Yoshikawa, Y., Imanaka, T. and Fujiwara, S. Identification of a novel aminopropyltransferase involved in the synthesis of branched-chain polyamines in hyperthermophiles. J. Bacteriol. 196 (2014) 1866-1876. [PMID: 24610711]

[EC 2.5.1.128 created 2014]

EC 2.5.1.129

Accepted name: flavin prenyltransferase

Reaction: dimethylallyl phosphate + FMNH2 = prenylated FMNH2 + phosphate

For diagram of reaction click here.

Glossary: prenylated FMNH2 = 3,3,4,5-tetramethyl-7-[(2S,3S,4R)-2,3,4-trihydroxy-5-(phosphonatooxy)pentyl]-2,3-dihydro-1H,7H-naphtho[1,8-fg]pteridine-9,11(8H,10H)-dione

Other name(s): ubiX (gene name); PAD1 (gene name)

Systematic name: dimethylallyl-phosphate:FMNH2 prenyltransferase

Comments: The enzyme produces the modified flavin cofactor prenylated FMNH2, which is required by EC 4.1.1.98, 4-hydroxy-3-polyprenylbenzoate decarboxylase, and EC 4.1.1.102, phenacrylate decarboxylase. The enzyme acts as a flavin prenyltransferase, linking a dimethylallyl moiety to the flavin N-5 and C-6 atoms and thus adding a fourth non-aromatic ring to the flavin isoalloxazine group.

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

References:

1. White, M.D., Payne, K.A., Fisher, K., Marshall, S.A., Parker, D., Rattray, N.J., Trivedi, D.K., Goodacre, R., Rigby, S.E., Scrutton, N.S., Hay, S. and Leys, D. UbiX is a flavin prenyltransferase required for bacterial ubiquinone biosynthesis. Nature 522 (2015) 502-506. [PMID: 26083743]

[EC 2.5.1.129 created 2015]

EC 2.5.1.130

Accepted name: 2-carboxy-1,4-naphthoquinone phytyltransferase

Reaction: phytyl diphosphate + 2-carboxy-1,4-naphthoquinone = demethylphylloquinone + diphosphate + CO2

For diagram of reaction click here.

Glossary: 2-carboxy-1,4-naphthoquinone = 1,4-dioxo-2-naphthoic acid

Other name(s): menA (gene name); ABC4 (gene name); 1,4-dioxo-2-naphthoate phytyltransferase; 1,4-diketo-2-naphthoate phytyltransferase

Systematic name: phytyl-diphosphate:2-carboxy-1,4-naphthoquinone phytyltransferase

Comments: This enzyme, found in plants and cyanobacteria, catalyses a step in the synthesis of phylloquinone (vitamin K1), an electron carrier associated with photosystem I. The enzyme catalyses the transfer of the phytyl chain synthesized by EC 1.3.1.83, geranylgeranyl diphosphate reductase, to 2-carboxy-1,4-naphthoquinone.

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

References:

1. Johnson, T.W., Shen, G., Zybailov, B., Kolling, D., Reategui, R., Beauparlant, S., Vassiliev, I.R., Bryant, D.A., Jones, A.D., Golbeck, J.H. and Chitnis, P.R. Recruitment of a foreign quinone into the A(1) site of photosystem I. I. Genetic and physiological characterization of phylloquinone biosynthetic pathway mutants in Synechocystis sp. PCC 6803. J. Biol. Chem. 275 (2000) 8523-8530. [PMID: 10722690]

2. Shimada, H., Ohno, R., Shibata, M., Ikegami, I., Onai, K., Ohto, M.A. and Takamiya, K. Inactivation and deficiency of core proteins of photosystems I and II caused by genetical phylloquinone and plastoquinone deficiency but retained lamellar structure in a T-DNA mutant of Arabidopsis. Plant J. 41 (2005) 627-637. [PMID: 15686525]

[EC 2.5.1.130 created 2015]

EC 2.5.1.131

Accepted name: (4-{4-[2-(γ-L-glutamylamino)ethyl]phenoxymethyl}furan-2-yl)methanamine synthase

Reaction: [5-(aminomethyl)furan-3-yl]methyl diphosphate + γ-L-glutamyltyramine = (4-{4-[2-(γ-L-glutamylamino)ethyl]phenoxymethyl}furan-2-yl)methanamine + diphosphate

For diagram of reaction click here.

Other name(s): MfnF

Systematic name: [5-(aminomethyl)furan-3-yl]methyl-diphosphate:γ-L-glutamyltyramine [5-(aminomethyl)furan-3-yl]methyltransferase

Comments: The enzyme, isolated from the archaeon Methanocaldococcus jannaschii, participates in the biosynthesis of the methanofuran cofactor.

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

References:

1. Wang, Y., Xu, H., Jones, M.K. and White, R.H. Identification of the final two genes functioning in methanofuran biosynthesis in Methanocaldococcus jannaschii. J. Bacteriol. 197 (2015) 2850-2858. [PMID: 26100040]

[EC 2.5.1.131 created 2015]

EC 2.5.1.132

Accepted name: 3-deoxy-D-glycero-D-galacto-nononate 9-phosphate synthase

Reaction: phosphoenolpyruvate + D-mannose 6-phosphate + H2O = 3-deoxy-D-glycero-D-galacto-nononate 9-phosphate + phosphate

Glossary: phosphoenolpyruvate = 2-(phosphonooxy)prop-2-enoate = 2-(phosphooxy)prop-2-enoate
3-deoxy-D-glycero-D-galacto-nononate = KDN

Other name(s): 2-keto-3-deoxy-D-glycero-D-galacto-9-phosphonononic acid synthase; KDN 9-P synthase

Systematic name: phosphoenolpyruvate:D-mannose-6-phosphate 1-(2-carboxy-2-oxoethyl)transferase

Comments: The enzyme participates in the biosynthesis of the sialic acid 3-deoxy-D-glycero-D-galacto-nononate (KDN). The human sialic acid synthase (EC 2.5.1.57) is also able to catalyse the reaction. KDN is abundant in extracellular glycoconjugates of lower vertebrates such as fish and amphibians, but is also found in the capsular polysaccharides of bacteria that belong to the Bacteroides genus.

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

References:

1. Angata, T., Nakata, D., Matsuda, T., Kitajima, K. and Troy, F.A., 2nd. Biosynthesis of KDN (2-keto-3-deoxy-D-glycero-D-galacto-nononic acid). Identification and characterization of a KDN-9-phosphate synthetase activity from trout testis. J. Biol. Chem. 274 (1999) 22949-22956. [PMID: 10438460]

2. Lawrence, S.M., Huddleston, K.A., Pitts, L.R., Nguyen, N., Lee, Y.C., Vann, W.F., Coleman, T.A. and Betenbaugh, M.J. Cloning and expression of the human N-acetylneuraminic acid phosphate synthase gene with 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid biosynthetic ability. J. Biol. Chem. 275 (2000) 17869-17877. [PMID: 10749855]

3. Wang, L., Lu, Z., Allen, K.N., Mariano, P.S. and Dunaway-Mariano, D. Human symbiont Bacteroides thetaiotaomicron synthesizes 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN). Chem. Biol. 15 (2008) 893-897. [PMID: 18804026]

[EC 2.5.1.132 created 2016]

EC 2.5.1.133

Accepted name: bacteriochlorophyll a synthase

Reaction: geranylgeranyl diphosphate + bacteriochlorophyllide a = geranylgeranyl-bacteriochlorophyllide a + diphosphate

For diagram of reaction click here.

Other name(s): bchG (gene name)

Systematic name: geranylgeranyl-diphosphate:bacteriochlorophyllide-a geranylgeranytransferase

Comments: The enzyme catalyses the addition of a geranylgeranyl hydrophobic chain to bacteriochlorophyllide a via an ester bond with the 17-propionate residue. The side chain is later modified to a phytyl chain, resulting in bacteriochlorophyll a.

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

References:

1. Oster, U., Bauer, C.E. and Rüdiger, W. Characterization of chlorophyll a and bacteriochlorophyll a synthases by heterologous expression in Escherichia coli. J. Biol. Chem. 272 (1997) 9671-9676. [PMID: 9092496]

2. Addlesee, H.A., Fiedor, L. and Hunter, C.N. Physical mapping of bchG, orf427, and orf177 in the photosynthesis gene cluster of Rhodobacter sphaeroides: functional assignment of the bacteriochlorophyll synthetase gene. J. Bacteriol. 182 (2000) 3175-3182. [PMID: 10809697]

3. Garcia-Gil, L.J., Gich, F.B. and Fuentes-Garcia, X. A comparative study of bchG from green photosynthetic bacteria. Arch. Microbiol. 179 (2003) 108-115. [PMID: 12560989]

4. Saga, Y., Hirota, K., Harada, J. and Tamiaki, H. In vitro enzymatic activities of bacteriochlorophyll a synthase derived from the green sulfur photosynthetic bacterium Chlorobaculum tepidum. Biochemistry 54 (2015) 4998-5005. [PMID: 26258685]

[EC 2.5.1.133 created 2016]

EC 2.5.1.134

Accepted name: cystathionine β-synthase (O-acetyl-L-serine)

Reaction: O-acetyl-L-serine + L-homocysteine = L-cystathionine + acetate

For diagram of reaction click here.

Other name(s): MccB; O-acetylserine dependent cystathionine β-synthase

Systematic name: O-acetyl-L-serine:L-homocysteine 2-amino-2-carboxyethyltransferase

Comments: A pyridoxal 5'-phosphate protein. The enzyme, purified from the bacterium Bacillus subtilis, also has a low activity with L-serine (cf. EC 4.2.1.22, cystathionine β-synthase).

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

References:

1. Hullo, M.F., Auger, S., Soutourina, O., Barzu, O., Yvon, M., Danchin, A. and Martin-Verstraete, I. Conversion of methionine to cysteine in Bacillus subtilis and its regulation. J. Bacteriol. 189 (2007) 187-197. [PMID: 17056751]

[EC 2.5.1.134 created 2016]

EC 2.5.1.135

Accepted name: validamine 7-phosphate valienyltransferase

Reaction: GDP-valienol + validamine 7-phosphate = validoxylamine A 7'-phosphate + GDP

For diagram of reaction click here

Glossary: valienol = (1S,2S,3S,4R)-5-(hydroxymethyl)cyclohex-5-ene-1,2,3,4-tetrol
validamine = (1R,2S,3S,4S,6R)-4-amino-6-(hydroxymethyl)cyclohexane-1,2,3-triol

Other name(s): vldE (gene name); valL (gene name)

Systematic name: GDP-valienol:validamine 7-phosphate valienyltransferase

Comments: The enzyme, characterized from several Streptomyces strains, is involved in the biosynthesis of the antifungal agent validamycin A.

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

References:

1. Asamizu, S., Yang, J., Almabruk, K.H. and Mahmud, T. Pseudoglycosyltransferase catalyzes nonglycosidic C-N coupling in validamycin a biosynthesis. J. Am. Chem. Soc. 133 (2011) 12124-12135. [PMID: 21766819]

2. Zheng, L., Zhou, X., Zhang, H., Ji, X., Li, L., Huang, L., Bai, L. and Zhang, H. Structural and functional analysis of validoxylamine A 7'-phosphate synthase ValL involved in validamycin A biosynthesis. PLoS One 7 (2012) e32033. [PMID: 22384130]

3. Cavalier, M.C., Yim, Y.S., Asamizu, S., Neau, D., Almabruk, K.H., Mahmud, T. and Lee, Y.H. Mechanistic insights into validoxylamine A 7'-phosphate synthesis by VldE using the structure of the entire product complex. PLoS One 7 (2012) e44934. [PMID: 23028689]

[EC 2.5.1.135 created 2016]

EC 2.5.1.136

Accepted name: 2-acylphloroglucinol 4-prenyltransferase

Reaction: dimethylallyl diphosphate + a 2-acylphloroglucinol = diphosphate + a 2-acyl-4-prenylphloroglucinol

For diagram of reaction click here or click here.

Glossary: naringenin chalcone = 2',4,4',6'-tetrahydroxychalcone = 3-(4-hydroxyphemyl)-1-(2,4,6-trihydroxyphenyl)prop-2-en-1-one
phlorisovalerophenone = 3-methyl-1-(2,4,6-trihydroxyphenyl)butan-1-one

Other name(s): PT-1 (gene name); PT1L (gene name); aromatic prenyltransferase (ambiguous)

Systematic name: dimethylallyl-diphosphate:2-acylphloroglucinol 4-dimethylallyltransferase

Comments: The enzyme, characterized from hop (Humulus lupulus), acts on phlorisovalerophenone, phlormethylbutanophenone, and phlorisobutanophenone during the synthesis of bitter acids. It also acts with much lower activity on naringenin chalcone. Forms a complex with EC 2.5.1.137, 2-acyl-4-prenylphloroglucinol 6-prenyltransferase, which catalyses additional prenylation reactions. Requires Mg2+.

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

References:

1. Tsurumaru, Y., Sasaki, K., Miyawaki, T., Uto, Y., Momma, T., Umemoto, N., Momose, M. and Yazaki, K. HlPT-1, a membrane-bound prenyltransferase responsible for the biosynthesis of bitter acids in hops. Biochem. Biophys. Res. Commun. 417 (2012) 393-398. [PMID: 22166201]

2. Li, H., Ban, Z., Qin, H., Ma, L., King, A.J. and Wang, G. A heteromeric membrane-bound prenyltransferase complex from hop catalyzes three sequential aromatic prenylations in the bitter acid pathway. Plant Physiol. 167 (2015) 650-659. [PMID: 25564559]

[EC 2.5.1.136 created 2017]

EC 2.5.1.137

Accepted name: 2-acyl-4-prenylphloroglucinol 6-prenyltransferase

Reaction: (1) dimethylallyl diphosphate + a 2-acyl-4-prenylphloroglucinol = diphosphate + a 2-acyl-4,6-bisprenylphloroglucinol
(2) dimethylallyl diphosphate + a 2-acyl-4,6-bisprenylphloroglucinol = diphosphate + a a 2-acyl-4,6,6-trisprenylcyclohexa-2,4-dien-1-one

For diagram of reaction click here.

Glossary: a 2-acyl-4,6,6-triprenylphloroglucinol = a β bitter acid

Other name(s): PT2 (gene name); aromatic prenyltransferase (ambiguous)

Systematic name: dimethylallyl-diphosphate:2-acyl-4-prenylphloroglucinol 6-dimethylallyltransferase

Comments: The enzyme, characterized from hop (Humulus lupulus), catalyses two successive prenylations of a 2-acyl-4-prenylphloroglucinol during the synthesis of bitter acids. Forms a complex with EC 2.5.1.136, 2-acylphloroglucinol 4-prenyltransferase, which catalyses the initial prenylation of the substrates. Requires Mg2+.

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

References:

1. Li, H., Ban, Z., Qin, H., Ma, L., King, A.J. and Wang, G. A heteromeric membrane-bound prenyltransferase complex from hop catalyzes three sequential aromatic prenylations in the bitter acid pathway. Plant Physiol. 167 (2015) 650-659. [PMID: 25564559]

[EC 2.5.1.137 created 2017]

EC 2.5.1.138

Accepted name: coumarin 8-geranyltransferase

Reaction: (1) geranyl diphosphate + umbelliferone = diphosphate + 8-geranylumbelliferone
(2) geranyl diphosphate + esculetin = diphosphate + 8-geranylesculetin

Glossary: esculetin = 6,7-dihydroxy-1-benzopyran-2-one
umbelliferone = 7-hydroxy-1-benzopyran-2-one

Other name(s): ClPT1

Systematic name: geranyl-diphosphate:umbelliferone 8-geranyltransferase

Comments: The enzyme, characterized from the plant Citrus limon, is specific for geranyl diphosphate as a prenyl donor. It also has low activity with the coumarins 5,7-dihydroxycoumarin and 5-methoxy-7-hydroxycoumarin.

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

References:

1. Munakata, R., Inoue, T., Koeduka, T., Karamat, F., Olry, A., Sugiyama, A., Takanashi, K., Dugrand, A., Froelicher, Y., Tanaka, R., Uto, Y., Hori, H., Azuma, J., Hehn, A., Bourgaud, F. and Yazaki, K. Molecular cloning and characterization of a geranyl diphosphate-specific aromatic prenyltransferase from lemon. Plant Physiol. 166 (2014) 80-90. [PMID: 25077796]

[EC 2.5.1.138 created 2017]

EC 2.5.1.139

Accepted name: umbelliferone 6-dimethylallyltransferase

Reaction: dimethylallyl diphosphate + umbelliferone = diphosphate + demethylsuberosin

For diagram of reaction click here.

Glossary: demethylsuberosin = 7-hydroxy-6-prenyl-1-benzopyran-2-one
osthenol = 7-hydroxy-8-prenyl-1-benzopyran-2-one

Other name(s): PcPT

Systematic name: dimethylallyl-diphosphate:umbelliferone 6-dimethylallyltransferase

Comments: The enzyme from parsley (Petroselinum crispum) is specific for umbelliferone and dimethylallyl diphosphate. A minor product is osthenol, which is produced by transfer of the dimethylallyl group to C-8 of umbelliferone.

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

References:

1. Hamerski, D., Schmitt, D. and Matern, U. Induction of two prenyltransferases for the accumulation of coumarin phytoalexins in elicitor-treated Ammi majus cell suspension cultures. Phytochemistry 29 (1990) 1131-1135. [PMID: 1366425]

2. Karamat, F., Olry, A., Munakata, R., Koeduka, T., Sugiyama, A., Paris, C., Hehn, A., Bourgaud, F. and Yazaki, K. A coumarin-specific prenyltransferase catalyzes the crucial biosynthetic reaction for furanocoumarin formation in parsley. Plant J. 77 (2014) 627-638. [PMID: 24354545]

[EC 2.5.1.139 created 2017]

EC 2.5.1.140

Accepted name: N-(2-amino-2-carboxyethyl)-L-glutamate synthase

Reaction: O-phospho-L-serine + L-glutamate = N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate + phosphate

Other name(s): SbnA; ACEGA synthase

Systematic name: O-phospho-L-serine:L-glutamate N-(2S)-2-amino-2-carboxyethyltransferase

Comments: The enzyme, characterized from the bacterium Staphylococcus aureus, is involved in the biosynthesis of the siderophore staphyloferrin B.

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

References:

1. Beasley, F.C., Cheung, J. and Heinrichs, D.E. Mutation of L-2,3-diaminopropionic acid synthase genes blocks staphyloferrin B synthesis in Staphylococcus aureus. BMC Microbiol. 11 (2011) 199. [PMID: 21906287]

2. Kobylarz, M.J., Grigg, J.C., Takayama, S.J., Rai, D.K., Heinrichs, D.E. and Murphy, M.E. Synthesis of L-2,3-diaminopropionic acid, a siderophore and antibiotic precursor. Chem. Biol. 21 (2014) 379-388. [PMID: 24485762]

[EC 2.5.1.140 created 2017]

EC 2.5.1.141

Accepted name: heme o synthase

Reaction: (2E,6E)-farnesyl diphosphate + protoheme IX + H2O = diphosphate + ferroheme o

For diagram of reaction click here

Other name(s): ctaB (gene name); COX10 (gene name)

Systematic name: (2E,6E)-farnesyl-diphosphate:protoheme IX farnesyltranstransferase

Comments: The enzyme, found in many archaea, bacteria, and eukaryotes, produces heme o, which in many cases is further modified into heme a. In organisms that produce heme a, the enzyme forms a complex with heme a synthase. In some archaeal species the enzyme transfers a geranylgeranyl group instead of a farnesyl group

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

References:

1. Saiki, K., Mogi, T. and Anraku, Y. Heme O biosynthesis in Escherichia coli: the cyoE gene in the cytochrome bo operon encodes a protoheme IX farnesyltransferase. Biochem. Biophys. Res. Commun. 189 (1992) 1491-1497. [PMID: 1336371]

2. Svensson, B., Lubben, M. and Hederstedt, L. Bacillus subtilis CtaA and CtaB function in haem A biosynthesis. Mol. Microbiol. 10 (1993) 193-201. [PMID: 7968515]

3. Glerum, D.M. and Tzagoloff, A. Isolation of a human cDNA for heme A:farnesyltransferase by functional complementation of a yeast cox10 mutant. Proc. Natl. Acad. Sci. USA 91 (1994) 8452-8456. [PMID: 8078902]

4. Lubben, M. and Morand, K. Novel prenylated hemes as cofactors of cytochrome oxidases. Archaea have modified hemes A and O. J. Biol. Chem 269 (1994) 21473-21479. [PMID: 8063781]

5. Brown, B.M., Wang, Z., Brown, K.R., Cricco, J.A. and Hegg, E.L. Heme O synthase and heme A synthase from Bacillus subtilis and Rhodobacter sphaeroides interact in Escherichia coli. Biochemistry 43 (2004) 13541-13548. [PMID: 15491161]

6. Mogi, T. Over-expression and characterization of Bacillus subtilis heme O synthase. J. Biochem. 145 (2009) 669-675. [PMID: 19204012]

[EC 2.5.1.141 created 2017]

EC 2.5.1.142

Accepted name: nerylneryl diphosphate synthase

Reaction: dimethylallyl diphosphate + 3 isopentenyl diphosphate = 3 diphosphate + nerylneryl diphosphate

For diagram of reaction click here

Glossary: nerylneryl diphosphate = all-cis-tetraprenyl diphosphate

Other name(s): CPT2

Systematic name: dimethylallyl-diphosphate:isopentenyl-diphosphate cistransferase (adding 3 isopentenyl units)

Comments: Isolated from the plant Solanum lycopersicum (tomato).

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

References:

1. Akhtar, T.A., Matsuba, Y., Schauvinhold, I., Yu, G., Lees, H.A., Klein, S.E. and Pichersky, E. The tomato cis-prenyltransferase gene family. Plant J. 73 (2013) 640-652. [PMID: 23134568]

2. Matsuba, Y., Zi, J., Jones, A.D., Peters, R.J. and Pichersky, E. Biosynthesis of the diterpenoid lycosantalonol via nerylneryl diphosphate in Solanum lycopersicum. PLoS One 10 (2015) e0119302. [PMID: 25786135]

[EC 2.5.1.142 created 2017]

EC 2.5.1.143

Accepted name: pyridinium-3,5-biscarboxylic acid mononucleotide synthase

Reaction: deamido-NAD+ + hydrogencarbonate = AMP + pyridinium-3,5-biscarboxylate mononucleotide

Other name(s): LarB; P2CMN synthase; nicotinic acid adenine dinucleotide carboxylase/hydrolase; NaAD carboxylase/hydrolase

Systematic name: deamido-NAD+:hydrogencarbonate nicotinate-β-D-ribonucleotidyltransferase

Comments: This enzyme, found in the bacterium Lactobacillus plantarum, is involved in the biosynthesis of a nickel-pincer cofactor. It carboxylates the pyridinium ring of deamido-NAD+ and cleaves the phosphoanhydride bond to release AMP and generate pyridinium-3,5-biscarboxylic acid mononucleotide (P2CMN).

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

References:

1. Desguin, B., Soumillion, P., Hols, P. and Hausinger, R.P. Nickel-pincer cofactor biosynthesis involves LarB-catalyzed pyridinium carboxylation and LarE-dependent sacrificial sulfur insertion. Proc. Natl Acad. Sci. USA 113 (2016) 5598-5603. [PMID: 27114550]

[EC 2.5.1.143 created 2018]

EC 2.5.1.144

Accepted name: S-sulfo-L-cysteine synthase (O-acetyl-L-serine-dependent)

Reaction: O-acetyl-L-serine + thiosulfate = S-sulfo-L-cysteine + acetate

For diagram of reaction click here.

Glossary: O-acetyl-L-serine = (2S)-3-acetyloxy-2-aminopropanoic acid

Other name(s): cysteine synthase B; cysM (gene name); CS26 (gene name)

Systematic name: O-acetyl-L-serine:thiosulfate 2-amino-2-carboxyethyltransferase

Comments: In plants, the activity is catalysed by a chloroplastic enzyme that plays an important role in chloroplast function and is essential for light-dependent redox regulation within the chloroplast. The bacterial enzyme also catalyses the activity of EC 2.5.1.47, cysteine synthase. cf. EC 2.8.5.1, S-sulfo-L-cysteine synthase (3-phospho-L-serine-dependent).

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

References:

1. Hensel, G. and Truper, H.G. O-Acetylserine sulfhydrylase and S-sulfocysteine synthase activities of Rhodospirillum tenue. Arch. Microbiol. 134 (1983) 227-232. [PMID: 6615127]

2. Nakamura, T., Iwahashi, H. and Eguchi, Y. Enzymatic proof for the identity of the S-sulfocysteine synthase and cysteine synthase B of Salmonella typhimurium. J. Bacteriol. 158 (1984) 1122-1127. [PMID: 6373737]

3. Bermudez, M.A., Paez-Ochoa, M.A., Gotor, C. and Romero, L.C. Arabidopsis S-sulfocysteine synthase activity is essential for chloroplast function and long-day light-dependent redox control. Plant Cell 22 (2010) 403-416. [PMID: 20179139]

4. Bermudez, M.A., Galmes, J., Moreno, I., Mullineaux, P.M., Gotor, C. and Romero, L.C. Photosynthetic adaptation to length of day is dependent on S-sulfocysteine synthase activity in the thylakoid lumen. Plant Physiol. 160 (2012) 274-288. [PMID: 22829322]

5. Gotor, C. and Romero, L.C. S-sulfocysteine synthase function in sensing chloroplast redox status. Plant Signal Behav 8 (2013) e23313. [PMID: 23333972]

[EC 2.5.1.144 created 2018]

EC 2.5.1.145

Accepted name: phosphatidylglycerol—prolipoprotein diacylglyceryl transferase

Reaction: L-1-phosphatidyl-sn-glycerol + a [prolipoprotein]-L-cysteine = sn-glycerol 1-phosphate + an [prolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine

Other name(s): lgt (gene name)

Systematic name: L-1-phosphatidyl-sn-glycerol:[prolipoprotein]-L-cysteine diacyl-sn-glyceryltransferase

Comments: This bacterial enzyme, which is associated with the membrane, catalyses the transfer of an sn-1,2-diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the prospective N-terminal cysteine of a prolipoprotein, the first step in the formation of mature triacylated lipoproteins.

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

References:

1. Sankaran, K. and Wu, H.C. Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl moiety from phosphatidylglycerol. J. Biol. Chem. 269 (1994) 19701-19706. [PMID: 8051048]

2. Qi, H.Y., Sankaran, K., Gan, K. and Wu, H.C. Structure-function relationship of bacterial prolipoprotein diacylglyceryl transferase: functionally significant conserved regions. J. Bacteriol. 177 (1995) 6820-6824. [PMID: 7592473]

3. Gan, K., Sankaran, K., Williams, M.G., Aldea, M., Rudd, K.E., Kushner, S.R. and Wu, H.C. The umpA gene of Escherichia coli encodes phosphatidylglycerol:prolipoprotein diacylglyceryl transferase (lgt) and regulates thymidylate synthase levels through translational coupling. J. Bacteriol. 177 (1995) 1879-1882. [PMID: 7896715]

4. Sankaran, K., Gan, K., Rash, B., Qi, H.Y., Wu, H.C. and Rick, P.D. Roles of histidine-103 and tyrosine-235 in the function of the prolipoprotein diacylglyceryl transferase of Escherichia coli. J. Bacteriol. 179 (1997) 2944-2948. [PMID: 9139912]

5. Pailler, J., Aucher, W., Pires, M. and Buddelmeijer, N. Phosphatidylglycerol::prolipoprotein diacylglyceryl transferase (Lgt) of Escherichia coli has seven transmembrane segments, and its essential residues are embedded in the membrane. J. Bacteriol. 194 (2012) 2142-2151. [PMID: 22287519]

[EC 2.5.1.145 created 2018]

EC 2.5.1.146

Accepted name: 3-geranyl-3-[(Z)-2-isocyanoethenyl]indole synthase

Reaction: geranyl diphosphate + 3-[(Z)-2-isocyanoethenyl]-1H-indole = 3-geranyl-3-[(Z)-2-isocyanoethenyl]-1H-indole + diphosphate

Other name(s): famD2 (gene name)

Systematic name: geranyl-diphosphate:3-[(Z)-2-isocyanoethenyl]-1H-indole geranyltransferase

Comments: The enzyme, characterized from the cyanobacterium Fischerella ambigua UTEX 1903, participates in the biosynthesis of hapalindole-type alkaloids.

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

References:

1. Li, S., Lowell, A.N., Yu, F., Raveh, A., Newmister, S.A., Bair, N., Schaub, J.M., Williams, R.M. and Sherman, D.H. Hapalindole/ambiguine biogenesis Is mediated by a Cope rearrangement, C-C bond-forming cascade. J. Am. Chem. Soc. 137 (2015) 15366-15369. [PMID: 26629885]

[EC 2.5.1.146 created 2018]

EC 2.5.1.147

Accepted name: 5-amino-6-(D-ribitylamino)uracil—L-tyrosine 4-hydroxyphenyl transferase

Reaction: 5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine = 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + 2-iminoacetate + L-methionine + 5'-deoxyadenosine

For diagram of reaction click here.

Glossary: 5-amino-6-(D-ribitylamino)uracil = 5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione

Other name(s): cofH (gene name); cbiF (gene name) (ambiguous)

Systematic name: 5-amino-6-(D-ribitylamino)uracil:L-tyrosine, 4-hydroxyphenyl transferase

Comments: The enzyme is involved in the production of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (Fo), the precursor of the redox cofactor coenzyme F420, which is found in methanogens and in various actinobacteria. Fo is also produced by some cyanobacteria and eukaryotes. The enzyme, which forms a complex with EC 4.3.1.32, 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, is a radical SAM enzyme that uses the 5'-deoxyadenosyl radical to initiate the reaction.

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

References:

1. Decamps, L., Philmus, B., Benjdia, A., White, R., Begley, T.P. and Berteau, O. Biosynthesis of F0, precursor of the F420 cofactor, requires a unique two radical-SAM domain enzyme and tyrosine as substrate. J. Am. Chem. Soc. 134 (2012) 18173-18176. [PMID: 23072415]

2. Philmus, B., Decamps, L., Berteau, O. and Begley, T.P. Biosynthetic versatility and coordinated action of 5'-deoxyadenosyl radicals in deazaflavin biosynthesis. J. Am. Chem. Soc. 137 (2015) 5406-5413. [PMID: 25781338]

[EC 2.5.1.147 created 2010 as EC 2.5.1.77, part transferred 2018 to EC 2.5.1.147]

EC 2.5.1.148

Accepted name: lycopaoctaene synthase

Reaction: 2 geranylgeranyl diphosphate + NADPH + H+ = lycopaoctaene + 2 diphosphate + NADP+ (overall reaction)
(1a) 2 geranylgeranyl diphosphate = diphosphate + prephytoene diphosphate
(1b) prephytoene diphosphate + NADPH + H+ = lycopaoctaene + diphosphate + NADP+

For diagram of reaction click here

Glossary: lycopaoctaene = 15,15'-dihydrophytoene = (6E,10E,14E,18E,22E,26E)-2,6,10,14,19,23,27,31-octamethyldotriaconta-2,6,10,14,18,22,26,30-octaene

Other name(s): LOS (gene name)

Systematic name: geranylgeranyl diphosphate:geranylgeranyl diphosphate geranylgeranyltransferase

Comments: The enzyme, characterized from the green microalga Botryococcus braunii race L, in involved in biosynthesis of (14E,18E)-lycopadiene. In vitro, the enzyme can accept (2E,6E)-farnesyl diphosphate and phytyl diphosphate as substrates, and is also able to catalyse the condensation of two different substrate molecules, forming chimeric products. However, the use of these alternative substrates is not significant in vivo.

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

References:

1. Thapa, H.R., Naik, M.T., Okada, S., Takada, K., Molnar, I., Xu, Y. and Devarenne, T.P. A squalene synthase-like enzyme initiates production of tetraterpenoid hydrocarbons in Botryococcus braunii Race L. Nat Commun 7 (2016) 11198. [PMID: 27050299]

2. Thapa, H.R., Tang, S., Sacchettini, J.C. and Devarenne, T.P. Tetraterpene synthase substrate and product specificity in the green microalga Botryococcus braunii Race L. ACS Chem. Biol. 12 (2017) 2408-2416. [PMID: 28813599]

[EC 2.5.1.148 created 2018]

EC 2.5.1.149

Accepted name: lycopene elongase/hydratase (flavuxanthin-forming)

Reaction: (1) dimethylallyl diphosphate + all-trans-lycopene + acceptor + H2O = nonaflavuxanthin + reduced electron acceptor + diphosphate
(2) dimethylallyl diphosphate + nonaflavuxanthin + acceptor + H2O = flavuxanthin + reduced electron acceptor + diphosphate

For diagram of reaction click here

Glossary: flavuxanthin = 2,2'-bis-(4-hydroxy-3-methylbut-2-enyl)-1,16,1',16'-tetradehydro-1,2,1',2'-tetrahydro-ψ,ψ-carotene = (2E,8E,10E,12E,14E,16E,18E,20E,22E,24E,26E,28E,34E)-5,32-diisopropenyl-2,8,12,16,21,25,29,35-octamethylhexatriaconta-2,8,10,12,14,16,18,20,22,24,26,28,34-tridecaene-1,36-diol

Other name(s): crtEb (gene name)

Systematic name: dimethylallyl-diphosphate:all-trans-lycopene dimethylallyltransferase (hydrating, flavuxanthin-forming)

Comments: The enzyme, characterized from the bacterium Corynebacterium glutamicum, is bifunctional. It catalyses the elongation of the C40 carotenoid all-trans-lycopene by attaching an isoprene unit at C-2, as well as the hydroxylation of the new isoprene unit. The enzyme acts at both ends of the substrate, forming the C50 carotenoid flavuxanthin via the C45 intermediate nonaflavuxanthin. cf. EC 2.5.1.150, lycopene elongase/hydratase (dihydrobisanhydrobacterioruberin-forming).

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

References:

1. Krubasik, P., Kobayashi, M. and Sandmann, G. Expression and functional analysis of a gene cluster involved in the synthesis of decaprenoxanthin reveals the mechanisms for C50 carotenoid formation. Eur. J. Biochem. 268 (2001) 3702-3708. [PMID: 11432736]

2. Heider, S.A., Peters-Wendisch, P. and Wendisch, V.F. Carotenoid biosynthesis and overproduction in Corynebacterium glutamicum. BMC Microbiol. 12 (2012) 198. [PMID: 22963379]

[EC 2.5.1.149 created 2018]

EC 2.5.1.150

Accepted name: lycopene elongase/hydratase (dihydrobisanhydrobacterioruberin-forming)

Reaction: (1) dimethylallyl diphosphate + all-trans-lycopene + H2O = dihydroisopentenyldehydrorhodopin + diphosphate
(2) dimethylallyl diphosphate + isopentenyldehydrorhodopin + H2O = dihydrobisanhydrobacterioruberin + diphosphate

For diagram of reaction click here

Glossary: dihydrobisanhydrobacterioruberin = (2S,2S')-2,2'-bis(3-methylbut-2-en-1-yl)-3,3',4,4'-tetradehydro-1,1',2,2'-tetrahydro-ψ,ψ-carotene-1,1'-diol = (3S,4E,6E,8E,10E,12E,14E,16E,18E,20E,22E,24E,26E,30R)-2,6,10,14,19,23,27,31-octamethyl-3,30-bis(3-methylbut-2-en-1-yl)dotriaconta-4,6,8,10,12,14,16,18,20,22,24,26-dodecaene-2,31-diol

Other name(s): lbtA (gene name); lyeJ (gene name)

Systematic name: dimethylallyl-diphosphate:all-trans-lycopene dimethylallyltransferase (hydrating, dihydrobisanhydrobacterioruberin-forming)

Comments: The enzyme, characterized from the bacterium Dietzia sp. CQ4 and the halophilic archaea Halobacterium salinarum and Haloarcula japonica, is bifunctional. It catalyses the elongation of the C40 carotenoid all-trans-lycopene by attaching an isoprene unit at C-2 as well as the hydroxylation of the previous end of the molecule. The enzyme acts at both ends of the substrate, and combined with the action of EC 1.3.99.37, 1-hydroxy-2-isopentenylcarotenoid 3,4-desaturase, it forms the C50 carotenoid dihydrobisanhydrobacterioruberin. cf. EC 2.5.1.149, lycopene elongase/hydratase (flavuxanthin-forming).

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

References:

1. Tao, L., Yao, H. and Cheng, Q. Genes from a Dietzia sp. for synthesis of C40 and C50 β-cyclic carotenoids. Gene 386 (2007) 90-97. [PMID: 17008032]

2. Dummer, A.M., Bonsall, J.C., Cihla, J.B., Lawry, S.M., Johnson, G.C. and Peck, R.F. Bacterioopsin-mediated regulation of bacterioruberin biosynthesis in Halobacterium salinarum. J. Bacteriol. 193 (2011) 5658-5667. [PMID: 21840984]

3. Yang, Y., Yatsunami, R., Ando, A., Miyoko, N., Fukui, T., Takaichi, S. and Nakamura, S. Complete biosynthetic pathway of the C50 carotenoid bacterioruberin from lycopene in the extremely halophilic archaeon Haloarcula japonica. J. Bacteriol. 197 (2015) 1614-1623. [PMID: 25712483]

[EC 2.5.1.150 created 2018]

EC 2.5.1.151

Accepted name: alkylcobalamin dealkylase

Reaction: an alkylcobalamin + [alkylcobalamin reductase] + glutathione = cob(I)alamin-[alkylcobalamin reductase] + an S-alkylglutathione

Other name(s): MMACHC (gene name)

Systematic name: alkylcobalamin:glutathione S-alkyltransferase

Comments: This mammalian enzyme, which is cytosolic, can bind internalized alkylcobalamins and process them to cob(I)alamin using the thiolate of glutathione for nucleophilic displacement. The product remains bound to the protein, and, following its oxidation to cob(II)alamin, is transferred by the enzyme, together with its interacting partner MMADHC, directly to downstream enzymes involved in adenosylcobalamin and methylcobalamin. In addition to its dealkylase function, the enzyme also catalyse an entirely different decyanase reaction with cyanocobalamin [cf. EC 1.16.1.6, cyanocobalamin reductase (cyanide-eliminating)].

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

References:

1. Hannibal, L., Kim, J., Brasch, N.E., Wang, S., Rosenblatt, D.S., Banerjee, R. and Jacobsen, D.W. Processing of alkylcobalamins in mammalian cells: A role for the MMACHC (cblC) gene product. Mol Genet Metab 97 (2009) 260-266. [PMID: 19447654]

2. Kim, J., Hannibal, L., Gherasim, C., Jacobsen, D.W. and Banerjee, R. A human vitamin B12 trafficking protein uses glutathione transferase activity for processing alkylcobalamins. J. Biol. Chem. 284 (2009) 33418-33424. [PMID: 19801555]

3. Koutmos, M., Gherasim, C., Smith, J.L. and Banerjee, R. Structural basis of multifunctionality in a vitamin B12-processing enzyme. J. Biol. Chem. 286 (2011) 29780-29787. [PMID: 21697092]

[EC 2.5.1.151 created 2018]

EC 2.5.1.152

Accepted name: D-histidine 2-aminobutanoyltransferase

Reaction: S-adenosyl-L-methionine + D-histidine = N-[(3S)-3-amino-3-carboxypropyl]-D-histidine + S-methyl-5'-thioadenosine

For diagram of reaction click here.

Glossary: staphylopine = N-[(3S)-3-{[(1S)-1-carboxyethyl]amino}-3-carboxypropyl]-D-histidine

Other name(s): cntL (gene name)

Systematic name: S-adenosyl-L-methionine:D-histidine N-[(3S)-3-amino-3-carboxypropyl]-transferase

Comments: The enzyme, characterized from the bacterium Staphylococcus aureus, participates in the biosynthesis of the metallophore staphylopine, which is involved in the acquisition of nickel, copper, and cobalt.

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

References:

1. Ghssein, G., Brutesco, C., Ouerdane, L., Fojcik, C., Izaute, A., Wang, S., Hajjar, C., Lobinski, R., Lemaire, D., Richaud, P., Voulhoux, R., Espaillat, A., Cava, F., Pignol, D., Borezee-Durant, E. and Arnoux, P. Biosynthesis of a broad-spectrum nicotianamine-like metallophore in Staphylococcus aureus. Science 352 (2016) 1105-1109. [PMID: 27230378]

[EC 2.5.1.152 created 2019]


Continued with EC 2.6.1.1 to EC 2.6.1.50
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