The Enzyme Database

Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB)

Proposed Changes to the Enzyme List

The entries below are proposed additions and amendments to the Enzyme Nomenclature list. They were prepared for the NC-IUBMB by Kristian Axelsen, Richard Cammack, Ron Caspi, Masaaki Kotera, Andrew McDonald, Gerry Moss, Dietmar Schomburg, Ida Schomburg and Keith Tipton. Comments and suggestions on these draft entries should be sent to Dr Andrew McDonald (Department of Biochemistry, Trinity College Dublin, Dublin 2, Ireland). The date on which an enzyme will be made official is appended after the EC number. To prevent confusion please do not quote new EC numbers until they are incorporated into the main list.

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


Contents

*EC 1.1.1.203 uronate dehydrogenase
EC 1.1.1.379 (R)-mandelate dehydrogenase
EC 1.1.1.380 L-gulonate 5-dehydrogenase
EC 1.1.1.381 3-hydroxy acid dehydrogenase
EC 1.1.3.47 5-(hydroxymethyl)furfural oxidase
EC 1.1.4.1 transferred
EC 1.1.4.2 transferred
EC 1.2.1.90 glyceraldehyde-3-phosphate dehydrogenase [NAD(P)+]
EC 1.2.1.91 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase
EC 1.2.1.92 3,6-anhydro-α-L-galactose dehydrogenase
EC 1.9.98 With other, known, acceptors
EC 1.9.98.1 iron—cytochrome-c reductase
EC 1.9.99.1 transferred
*EC 1.14.99.42 zeaxanthin 7,8-dioxygenase
EC 1.17.1.7 transferred
EC 1.17.4.4 vitamin-K-epoxide reductase (warfarin-sensitive)
EC 1.17.4.5 vitamin-K-epoxide reductase (warfarin-insensitive)
*EC 1.17.7.1 (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase (ferredoxin)
EC 1.17.7.3 (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase (flavodoxin)
EC 1.17.98 With other, known, acceptors
EC 1.17.98.1 bile-acid 7α-dehydroxylase
EC 1.17.99.5 transferred
EC 1.17.99.6 epoxyqueuosine reductase
*EC 1.19.6.1 nitrogenase (flavodoxin)
EC 1.21.98.1 cyclic dehypoxanthinyl futalosine synthase
EC 1.21.99.2 transferred
*EC 2.1.1.192 23S rRNA (adenine2503-C2)-methyltransferase
*EC 2.1.1.224 23S rRNA (adenine2503-C8)-methyltransferase
EC 2.1.1.308 2-hydroxyethylphosphonate methyltransferase
EC 2.1.1.309 18S rRNA (guanine1575-N7)-methyltransferase
EC 2.1.1.310 25S rRNA (cytosine2870-C5)-methyltransferase
EC 2.1.1.311 25S rRNA (cytosine2278-C5)-methyltransferase
EC 2.1.1.312 25S rRNA (uracil2843-N3)-methyltransferase
EC 2.1.1.313 25S rRNA (uracil2634-N3)-methyltransferase
EC 2.2.1.12 3-acetyloctanal synthase
EC 2.3.1.234 N6-L-threonylcarbamoyladenine synthase
EC 2.3.1.235 tetracenomycin F2 synthase
EC 2.3.1.236 5-methylnaphthoic acid synthase
EC 2.3.1.237 neocarzinostatin naphthoate synthase
EC 2.3.1.238 monacolin J acid methylbutanoate transferase
EC 2.3.1.239 10-deoxymethynolide syntase
EC 2.3.1.240 narbonolide synthase
EC 2.3.1.241 Kdo2-lipid IVA lauroyltransferase
EC 2.3.1.242 Kdo2-lipid IVA palmitoleoyltransferase
EC 2.3.1.243 lauroyl-Kdo2-lipid IVA myristoyltransferase
EC 2.4.1.332 1,2-α-glucosylglycerol phosphorylase
EC 2.4.1.333 1,2-β-oligoglucan phosphorylase
EC 2.4.1.334 1,3-α-oligoglucan phosphorylase
*EC 2.4.2.54 β-ribofuranosylhydroxybenzene 5′-phosphate synthase
*EC 2.5.1.25 tRNA-uridine aminocarboxypropyltransferase
EC 2.5.1.128 N4-bis(aminopropyl)spermidine synthase
EC 2.6.99.4 transferred
*EC 2.7.7.67 CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase
EC 2.7.8.41 cardiolipin synthase (CMP-forming)
*EC 2.8.1.6 biotin synthase
*EC 2.8.1.8 lipoyl synthase
EC 3.1.1.97 diphthine methylesterase
EC 3.1.3.96 pseudouridine 5′-phosphatase
EC 3.5.1.27 deleted
EC 3.5.2.20 isatin hydrolase
*EC 3.5.4.20 pyrithiamine deaminase
EC 3.6.1.67 dihydroneopterin triphosphate diphosphatase
*EC 4.1.99.19 2-iminoacetate synthase
EC 4.2.3.148 cembrene C synthase
EC 4.2.3.149 nephthenol synthase
EC 4.2.3.150 cembrene A synthase
EC 4.2.3.151 pentamethylcyclopentadecatrienol synthase
EC 4.4.1.28 L-cysteine desulfidase
EC 5.5.1.25 3,6-anhydro-α-L-galactonate cycloisomerase
EC 6.3.2.45 UDP-N-acetylmuramate L-alanyl-γ-D-glutamyl-meso-2,6-diaminoheptandioate ligase
*EC 6.3.4.14 biotin carboxylase
EC 6.3.4.24 tyramine—L-glutamate ligase


*EC 1.1.1.203 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: uronate dehydrogenase
Reaction: (1) D-galacturonate + NAD+ = D-galactaro-1,5-lactone + NADH + H+
(2) D-glucuronate + NAD+ = D-glucaro-1,5-lactone + NADH + H+
Other name(s): uronate: NAD-oxidoreductase; uronic acid dehydrogenase
Systematic name: uronate:NAD+ 1-oxidoreductase
Comments: Requires Mg2+. The enzyme, characterized from the bacterium Agrobacterium fabrum, participates in oxidative degradation pathways for galacturonate and glucuronate. The 1,5-lactone product is rather stable at cytosolic pH and does not hydrolyse spontaneously at a substantial rate.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, MetaCyc, CAS registry number: 37250-98-9
References:
1.  Kilgore, W.W. and Starr, M.P. Uronate oxidation by phytopathogenic pseudomonads. Nature (Lond.) 183 (1959) 1412–1413. [PMID: 13657147]
2.  Boer, H., Maaheimo, H., Koivula, A., Penttila, M. and Richard, P. Identification in Agrobacterium tumefaciens of the D-galacturonic acid dehydrogenase gene. Appl. Microbiol. Biotechnol. 86 (2010) 901–909. [PMID: 19921179]
3.  Andberg, M., Maaheimo, H., Boer, H., Penttila, M., Koivula, A. and Richard, P. Characterization of a novel Agrobacterium tumefaciens galactarolactone cycloisomerase enzyme for direct conversion of D-galactarolactone to 3-deoxy-2-keto-L-threo-hexarate. J. Biol. Chem. 287 (2012) 17662–17671. [PMID: 22493433]
[EC 1.1.1.203 created 1972 as EC 1.2.1.35, transferred 1984 to EC 1.1.1.203, modified 2014]
 
 
EC 1.1.1.379 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: (R)-mandelate dehydrogenase
Reaction: (R)-mandelate + NAD+ = phenylglyoxylate + NADH + H+
Glossary: (R)-mandelate = D-mandelate
Other name(s): ManDH2; D-ManDH2
Systematic name: (R)-mandelate:NAD+ 2-oxidoreductase
Comments: The enzyme, found in bacteria and fungi, can also accept a number of substituted mandelate derivatives, such as 3-hydroxymandelate, 4-hydroxymandelate, 2-methoxymandelate, 4-hydroxy-3-methoxymandelate and 3-hydroxy-4-methoxymandelate. The enzyme has no activity with (S)-mandelate (cf. EC 1.1.99.31, (S)-mandelate dehydrogenase) [1,2]. The enzyme transfers the pro-R-hydrogen from NADH [2].
References:
1.  Baker, D.P. and Fewson, C.A. Purification and characterization of D(–)-mandelate dehydrogenase from Rhodotorula graminis. Microbiology 135 (1989) 2035–2044.
2.  Baker, D.P., Kleanthous, C., Keen, J.N., Weinhold, E. and Fewson, C.A. Mechanistic and active-site studies on D(–)-mandelate dehydrogenase from Rhodotorula graminis. Biochem. J. 281 (1992) 211–218. [PMID: 1731758]
3.  Wada, Y., Iwai, S., Tamura, Y., Ando, T., Shinoda, T., Arai, K. and Taguchi, H. A new family of D-2-hydroxyacid dehydrogenases that comprises D-mandelate dehydrogenases and 2-ketopantoate reductases. Biosci. Biotechnol. Biochem. 72 (2008) 1087–1094. [PMID: 18391442]
4.  Miyanaga, A., Fujisawa, S., Furukawa, N., Arai, K., Nakajima, M. and Taguchi, H. The crystal structure of D-mandelate dehydrogenase reveals its distinct substrate and coenzyme recognition mechanisms from those of 2-ketopantoate reductase. Biochem. Biophys. Res. Commun. 439 (2013) 109–114. [PMID: 23954635]
[EC 1.1.1.379 created 2014]
 
 
EC 1.1.1.380 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: L-gulonate 5-dehydrogenase
Reaction: L-gulonate + NAD+ = D-fructuronate + NADH + H+
Glossary: D-fructuronate = D-arabino-hexuronate
Systematic name: L-gulonate:NAD+ 5-oxidoreductase
Comments: The enzyme, characterized from the bacterium Halomonas elongata, participates in a pathway for L-gulonate degradation.
References:
1.  Cooper, R.A. The pathway for L-gulonate catabolism in Escherichia coli K-12 and Salmonella typhimurium LT-2. FEBS Lett 115 (1980) 63–67. [PMID: 6993236]
2.  Wichelecki, D.J., Vendiola, J.A., Jones, A.M., Al-Obaidi, N., Almo, S.C. and Gerlt, J.A. Investigating the physiological roles of low-efficiency D-mannonate and D-gluconate dehydratases in the enolase superfamily: pathways for the catabolism of L-gulonate and L-idonate. Biochemistry 53 (2014) 5692–5699. [PMID: 25145794]
[EC 1.1.1.380 created 2014]
 
 
EC 1.1.1.381 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: 3-hydroxy acid dehydrogenase
Reaction: L-allo-threonine + NADP+ = aminoacetone + CO2 + NADPH + H+ (overall reaction)
(1a) L-allo-threonine + NADP+ = L-2-amino-3-oxobutanoate + NADPH + H+
(1b) L-2-amino-3-oxobutanoate = aminoacetone + CO2 (spontaneous)
Other name(s): ydfG (gene name); YMR226c (gene name)
Systematic name: L-allo-threonine:NADP+ 3-oxidoreductase
Comments: The enzyme, purified from the bacterium Escherichia coli and the yeast Saccharomyces cerevisiae, shows activity with a range of 3- and 4-carbon 3-hydroxy acids. The highest activity is seen with L-allo-threonine, D-threonine, L-serine, D-serine, (S)-3-hydroxy-2-methylpropanoate and (R)-3-hydroxy-2-methylpropanoate. The enzyme has no activity with NAD+ or L-threonine (cf. EC 1.1.1.103, L-threonine 3-dehydrogenase).
References:
1.  Fujisawa, H., Nagata, S. and Misono, H. Characterization of short-chain dehydrogenase/reductase homologues of Escherichia coli (YdfG) and Saccharomyces cerevisiae (YMR226C). Biochim. Biophys. Acta 1645 (2003) 89–94. [PMID: 12535615]
[EC 1.1.1.381 created 2014]
 
 
EC 1.1.3.47 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: 5-(hydroxymethyl)furfural oxidase
Reaction: 5-(hydroxymethyl)furfural + 3 O2 + 2 H2O = furan-2,5-dicarboxylate + 3 H2O2 (overall reaction)
(1a) 5-(hydroxymethyl)furfural + O2 = furan-2,5-dicarbaldehyde + H2O2
(1b) furan-2,5-dicarbaldehyde + H2O = 5-(dihydroxymethyl)furan-2-carbaldehyde (spontaneous)
(1c) 5-(dihydroxymethyl)furan-2-carbaldehyde + O2 = 5-formylfuran-2-carboxylate + H2O2
(1d) 5-formylfuran-2-carboxylate + H2O = 5-(dihydroxymethyl)furan-2-carboxylate (spontaneous)
(1e) 5-(dihydroxymethyl)furan-2-carboxylate + O2 = furan-2,5-dicarboxylate + H2O2
Glossary: 5-(hydroxymethyl)furfural = 5-(hydroxymethyl)furan-2-carbaldehyde
Systematic name: 5-(hydroxymethyl)furfural:oxygen oxidoreductase
Comments: The enzyme, characterized from the bacterium Methylovorus sp. strain MP688, is involved in the degradation and detoxification of 5-(hydroxymethyl)furfural. The enzyme acts only on alcohol groups and requires the spontaneous hydration of aldehyde groups for their oxidation [3]. The enzyme has a broad substrate range that overlaps with EC 1.1.3.7, aryl-alcohol oxidase.
References:
1.  Koopman, F., Wierckx, N., de Winde, J.H. and Ruijssenaars, H.J. Identification and characterization of the furfural and 5-(hydroxymethyl)furfural degradation pathways of Cupriavidus basilensis HMF14. Proc. Natl. Acad. Sci. USA 107 (2010) 4919–4924. [PMID: 20194784]
2.  Dijkman, W.P. and Fraaije, M.W. Discovery and characterization of a 5-hydroxymethylfurfural oxidase from Methylovorus sp. strain MP688. Appl. Environ. Microbiol. 80 (2014) 1082–1090. [PMID: 24271187]
3.  Dijkman, W.P., Groothuis, D.E. and Fraaije, M.W. Enzyme-catalyzed oxidation of 5-hydroxymethylfurfural to furan-2,5-dicarboxylic acid. Angew Chem Int Ed Engl 53 (2014) 6515–6518. [PMID: 24802551]
[EC 1.1.3.47 created 2014]
 
 
EC 1.1.4.1 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Transferred entry: vitamin-K-epoxide reductase (warfarin-sensitive). Now EC 1.17.4.4, vitamin-K-epoxide reductase (warfarin-sensitive)
[EC 1.1.4.1 created 1989, deleted 2014]
 
 
EC 1.1.4.2 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Transferred entry: vitamin-K-epoxide reductase (warfarin-insensitive). Now EC 1.17.4.5, vitamin-K-epoxide reductase (warfarin-insensitive)
[EC 1.1.4.2 created 1989, deleted 2014]
 
 
EC 1.2.1.90 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: glyceraldehyde-3-phosphate dehydrogenase [NAD(P)+]
Reaction: D-glyceraldehyde 3-phosphate + NAD(P)+ + H2O = 3-phospho-D-glycerate + NAD(P)H + 2 H+
Other name(s): non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase; GAPN
Systematic name: D-glyceraldehyde-3-phosphate:NAD(P)+ oxidoreductase
Comments: The enzyme is part of the modified Embden-Meyerhof-Parnas pathway of the archaeon Thermoproteus tenax. cf. EC 1.2.1.9 [glyceraldehyde-3-phosphate dehydrogenase (NADP+)].
References:
1.  Brunner, N.A., Brinkmann, H., Siebers, B. and Hensel, R. NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase from Thermoproteus tenax. The first identified archaeal member of the aldehyde dehydrogenase superfamily is a glycolytic enzyme with unusual regulatory properties. J. Biol. Chem. 273 (1998) 6149–6156. [PMID: 9497334]
2.  Brunner, N.A., Siebers, B. and Hensel, R. Role of two different glyceraldehyde-3-phosphate dehydrogenases in controlling the reversible Embden-Meyerhof-Parnas pathway in Thermoproteus tenax: regulation on protein and transcript level. Extremophiles 5 (2001) 101–109. [PMID: 11354453]
3.  Pohl, E., Brunner, N., Wilmanns, M. and Hensel, R. The crystal structure of the allosteric non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeum Thermoproteus tenax. J. Biol. Chem. 277 (2002) 19938–19945. [PMID: 11842090]
4.  Lorentzen, E., Hensel, R., Knura, T., Ahmed, H. and Pohl, E. Structural basis of allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase from Thermoproteus tenax. J. Mol. Biol. 341 (2004) 815–828. [PMID: 15288789]
[EC 1.2.1.90 created 2014]
 
 
EC 1.2.1.91 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase
Reaction: 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde + NADP+ + H2O = 3-oxo-5,6-dehydrosuberyl-CoA + NADPH + H+
For diagram of aerobic phenylacetate catabolism, click here
Glossary: 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde = 3,8-dioxooct-5-enoyl-CoA
Other name(s): paaZ (gene name)
Systematic name: 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde:NADP+ oxidoreductase
Comments: The enzyme from Escherichia coli is a bifunctional fusion protein that also catalyses EC 3.3.2.12, oxepin-CoA hydrolase. Combined the two activities result in a two-step conversion of oxepin-CoA to 3-oxo-5,6-dehydrosuberyl-CoA, part of an aerobic phenylacetate degradation pathway.
References:
1.  Ferrandez, A., Minambres, B., Garcia, B., Olivera, E.R., Luengo, J.M., Garcia, J.L. and Diaz, E. Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway. J. Biol. Chem. 273 (1998) 25974–25986. [PMID: 9748275]
2.  Ismail, W., El-Said Mohamed, M., Wanner, B.L., Datsenko, K.A., Eisenreich, W., Rohdich, F., Bacher, A. and Fuchs, G. Functional genomics by NMR spectroscopy. Phenylacetate catabolism in Escherichia coli. Eur. J. Biochem. 270 (2003) 3047–3054. [PMID: 12846838]
3.  Teufel, R., Mascaraque, V., Ismail, W., Voss, M., Perera, J., Eisenreich, W., Haehnel, W. and Fuchs, G. Bacterial phenylalanine and phenylacetate catabolic pathway revealed. Proc. Natl. Acad. Sci. USA 107 (2010) 14390–14395. [PMID: 20660314]
[EC 1.2.1.91 created 2011 as EC 1.17.1.7, transferred 2014 to EC 1.2.1.91]
 
 
EC 1.2.1.92 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: 3,6-anhydro-α-L-galactose dehydrogenase
Reaction: 3,6-anhydro-α-L-galactopyranose + NAD(P)+ + H2O = 3,6-anhydro-α-L-galactonate + NAD(P)H + H+
Systematic name: 3,6-anhydro-α-L-galactopyranose:NAD(P)+ 1-oxidoredutase
Comments: The enzyme, characterized from the marine bacterium Vibrio sp. EJY3, is involved in a degradation pathway for 3,6-anhydro-α-L-galactose, a major component of the polysaccharides produced by red macroalgae, such as agarose and porphyran.
References:
1.  Yun, E.J., Lee, S., Kim, H.T., Pelton, J.G., Kim, S., Ko, H.J., Choi, I.G. and Kim, K.H. The novel catabolic pathway of 3,6-anhydro-L-galactose, the main component of red macroalgae, in a marine bacterium. Environ Microbiol (2014) . [PMID: 25156229]
[EC 1.2.1.92 created 2014]
 
 
EC 1.9.98 With other, known, acceptors
 
EC 1.9.98.1 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: iron—cytochrome-c reductase
Reaction: ferrocytochrome c + Fe3+ = ferricytochrome c + Fe2+
Other name(s): iron-cytochrome c reductase
Systematic name: ferrocytochrome-c:Fe3+ oxidoreductase
Comments: An iron protein.
References:
1.  Yates, M.G. and Nason, A. Electron transport systems of the chemoautotroph Ferrobacillus ferrooxidans. II. Purification and properties of a heat-labile iron-cytochrome c reductase. J. Biol. Chem. 241 (1966) 4872–4880. [PMID: 4288725]
[EC 1.9.98.1 created 1972 as EC 1.9.99.1, transferred 2014 to EC 1.9.98.1]
 
 
EC 1.9.99.1 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Transferred entry: iron—cytochrome-c reductase. Now EC 1.9.98.a, iron—cytochrome-c reductase
[EC 1.9.99.1 created 1972, deleted 2014]
 
 
*EC 1.14.99.42 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: zeaxanthin 7,8-dioxygenase
Reaction: zeaxanthin + 2 O2 = crocetin dialdehyde + 2 (3S)-3-hydroxycyclocitral (overall reaction)
(1a) zeaxanthin + O2 = β-citraurin + (3S)-3-hydroxycyclocitral
(1b) β-citraurin + O2 = crocetin dialdehyde + (3S)-3-hydroxycyclocitral
For diagram of crocin biosynthesis, click here
Glossary: β-citraurin = 3-hydroxy-β-apo-8′-carotenal
Other name(s): zeaxanthin 7,8(7′,8′)-cleavage dioxygenase; CsZCD (incorrect); CCD2 (gene name)
Systematic name: zeaxanthin:oxygen oxidoreductase (7,8-cleaving)
Comments: The enzyme, characterized from the plant Crocus sativus, acts twice on zeaxanthin, cleaving 3-hydroxycyclocitral off each 3-hydroxy end group. It is part of the zeaxanthin degradation pathway in that organism, leading to the different compounds that impart the color, flavor and aroma of the saffron spice.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, MetaCyc
References:
1.  Frusciante, S., Diretto, G., Bruno, M., Ferrante, P., Pietrella, M., Prado-Cabrero, A., Rubio-Moraga, A., Beyer, P., Gomez-Gomez, L., Al-Babili, S. and Giuliano, G. Novel carotenoid cleavage dioxygenase catalyzes the first dedicated step in saffron crocin biosynthesis. Proc. Natl. Acad. Sci. USA 111 (2014) 12246–12251. [PMID: 25097262]
[EC 1.14.99.42 created 2011, modified 2014]
 
 
EC 1.17.1.7 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Transferred entry: 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase. Now EC 1.2.1.91, 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase
[EC 1.17.1.7 created 2011, deleted 2014]
 
 
EC 1.17.4.4 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: vitamin-K-epoxide reductase (warfarin-sensitive)
Reaction: phylloquinone + oxidized dithiothreitol + H2O = 2,3-epoxy-2-methyl-3-phytyl-2,3-dihydro-1,4-naphthoquinone + 1,4-dithiothreitol
Glossary: phylloquinone = 2-methyl-3-phytyl-1,4-naphthoquinone
2,3-epoxy-2-methyl-3-phytyl-2,3-dihydro-1,4-naphthoquinone = vitamin K 2,3-epoxide
Systematic name: phylloquinone:oxidized-dithiothreitol oxidoreductase
Comments: Vitamin K 2,3-epoxide is reduced to vitamin K and possibly to vitamin K hydroquinone by 1,4-dithiothreitol, which is oxidized to a disulfide; some other dithiols and 4-butanethiol can also act. Inhibited strongly by warfarin [cf. EC 1.17.4.5, vitamin-K-epoxide reductase (warfarin-insensitive)].
References:
1.  Lee, J.L. and Fasco, M.J. Metabolism of vitamin K and vitamin K 2,3-epoxide via interaction with a common disulfide. Biochemistry 23 (1984) 2246–2252. [PMID: 6733086]
2.  Mukharji, I. and Silverman, R.B. Purification of a vitamin K epoxide reductase that catalyzes conversion of vitamin K 2,3-epoxide to 3-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone. Proc. Natl. Acad. Sci. USA 82 (1985) 2713–2717. [PMID: 3857611]
3.  Whitlon, D.S., Sadowski, J.A. and Suttie, J.W. Mechanism of coumarin action: significance of vitamin K epoxide reductase inhibition. Biochemistry 17 (1978) 1371–1377. [PMID: 646989]
[EC 1.17.4.4 created 1989 as 1.1.4.1, transferred 2014 to EC 1.17.4.4]
 
 
EC 1.17.4.5 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: vitamin-K-epoxide reductase (warfarin-insensitive)
Reaction: 3-hydroxy-2-methyl-3-phytyl-2,3-dihydro-1,4-naphthoquinone + oxidized dithiothreitol = 2,3-epoxy-2-methyl-3-phytyl-2,3-dihydro-1,4-naphthoquinone + 1,4-dithiothreitol
Glossary: 2,3-epoxy-2-methyl-3-phytyl-2,3-dihydro-1,4-naphthoquinone = vitamin K 2,3-epoxide
Systematic name: 3-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone:oxidized-dithiothreitol oxidoreductase
Comments: Vitamin K 2,3-epoxide is reduced to 3-hydroxy- (and 2-hydroxy-) vitamin K by 1,4-dithiothreitol, which is oxidized to a disulfide. Not inhibited by warfarin [cf. EC 1.17.4.4, vitamin-K-epoxide reductase (warfarin-sensitive)].
References:
1.  Mukharji, I. and Silverman, R.B. Purification of a vitamin K epoxide reductase that catalyzes conversion of vitamin K 2,3-epoxide to 3-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone. Proc. Natl. Acad. Sci. USA 82 (1985) 2713–2717. [PMID: 3857611]
[EC 1.17.4.5 created 1989 as EC 1.1.4.2, transferred 2014 to EC 1.17.4.5]
 
 
*EC 1.17.7.1 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase (ferredoxin)
Reaction: (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H2O + 2 oxidized ferredoxin = 2-C-methyl-D-erythritol 2,4-cyclodiphosphate + 2 reduced ferredoxin
For diagram of Non-Mevalonate terpenoid biosynthesis, click here
Other name(s): 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (ambiguous); (E)-4-hydroxy-3-methylbut-2-en-1-yl-diphosphate:protein-disulfide oxidoreductase (hydrating) (incorrect); (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase (ambiguous); gcpE (gene name); ISPG (gene name); (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase
Systematic name: (E)-4-hydroxy-3-methylbut-2-en-1-yl-diphosphate:oxidized ferredoxin oxidoreductase
Comments: An iron-sulfur protein found in plant chloroplasts and cyanobacteria that contains a [4Fe-4S] cluster [1]. Forms part of an alternative non-mevalonate pathway for isoprenoid biosynthesis [3]. Bacteria have a similar enzyme that uses flavodoxin rather than ferredoxin (cf. EC 1.17.7.3). The enzyme from the plant Arabidopsis thaliana is active with photoreduced 5-deazaflavin but not with flavodoxin [1].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, MetaCyc, PDB
References:
1.  Okada, K. and Hase, T. Cyanobacterial non-mevalonate pathway: (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase interacts with ferredoxin in Thermosynechococcus elongatus BP-1. J. Biol. Chem. 280 (2005) 20672–20679. [PMID: 15792953]
2.  Seemann, M., Wegner, P., Schünemann, V., Tse Sum Bui, B., Wolff, M., Marquet, A., Trautwein, A.X. and Rohmer, M. Isoprenoid biosynthesis in chloroplasts via the methylerythritol phosphate pathway: the (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase (GcpE) from Arabidopsis thaliana is a [4Fe-4S] protein. J. Biol. Inorg. Chem. 10 (2005) 131–137. [PMID: 15650872]
3.  Seemann, M., Tse Sum Bui, B., Wolff, M., Tritsch, D., Campos, N., Boronat, A., Marquet, A. and Rohmer, M. Isoprenoid biosynthesis through the methylerythritol phosphate pathway: the (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase (GcpE) is a [4Fe-4S] protein. Angew. Chem. Int. Ed. Engl. 41 (2002) 4337–4339. [PMID: 12434382]
4.  Seemann, M., Tse Sum Bui, B., Wolff, M., Miginiac-Maslow, M. and Rohmer, M. Isoprenoid biosynthesis in plant chloroplasts via the MEP pathway: direct thylakoid/ferredoxin-dependent photoreduction of GcpE/IspG. FEBS Lett. 580 (2006) 1547–1552. [PMID: 16480720]
[EC 1.17.7.1 created 2003 as EC 1.17.4.3, transferred 2009 to EC 1.17.7.1, modified 2014]
 
 
EC 1.17.7.3 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase (flavodoxin)
Reaction: (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H2O + oxidized flavodoxin = 2-C-methyl-D-erythritol 2,4-cyclodiphosphate + reduced flavodoxin
For diagram of non-mevalonate terpenoid biosynthesis, click here
Other name(s): 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (ambiguous); (E)-4-hydroxy-3-methylbut-2-en-1-yl-diphosphate:protein-disulfide oxidoreductase (hydrating) (incorrect); (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase (ambiguous); ispG (gene name)
Systematic name: (E)-4-hydroxy-3-methylbut-2-en-1-yl-diphosphate:oxidized flavodoxin oxidoreductase
Comments: A bacterial iron-sulfur protein that contains a [4Fe-4S] cluster. Forms part of an alternative non-mevalonate pathway for isoprenoid biosynthesis that is found in most bacteria. Plants and cyanobacteria have a similar enzyme that utilizes ferredoxin rather than flavodoxin (cf. EC 1.17.7.1).
References:
1.  Hecht, S., Eisenreich, W., Adam, P., Amslinger, S., Kis, K., Bacher, A., Arigoni, D. and Rohdich, F. Studies on the nonmevalonate pathway to terpenes: the role of the GcpE (IspG) protein. Proc. Natl. Acad. Sci. USA 98 (2001) 14837–14842. [PMID: 11752431]
2.  Zepeck, F., Grawert, T., Kaiser, J., Schramek, N., Eisenreich, W., Bacher, A. and Rohdich, F. Biosynthesis of isoprenoids. purification and properties of IspG protein from Escherichia coli. J. Org. Chem. 70 (2005) 9168–9174. [PMID: 16268586]
3.  Puan, K.J., Wang, H., Dairi, T., Kuzuyama, T. and Morita, C.T. fldA is an essential gene required in the 2-C-methyl-D-erythritol 4-phosphate pathway for isoprenoid biosynthesis. FEBS Lett 579 (2005) 3802–3806. [PMID: 15978585]
[EC 1.17.7.3 created 2014]
 
 
EC 1.17.98 With other, known, acceptors
 
EC 1.17.98.1 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: bile-acid 7α-dehydroxylase
Reaction: (1) deoxycholate + FAD + H2O = cholate + FADH2
(2) lithocholate + FAD + H2O = chenodeoxycholate + FADH2
For diagram of reaction, click here and of proposed mechanism, click here
Glossary: cholate = 3α,7α,12α-trihydroxy-5β-cholan-24-oate
deoxycholate = 3α,12α-dihydroxy-5β-cholan-24-oate
lithocholate = 3α-hydroxy-5β-cholan-24-oate
chenodeoxycholate = 3α,7α-dihydroxy-5β-cholan-24-oate
allodeoxycholate = 3α,12α-dihydroxy-5α-cholan-24-oate
Other name(s): cholate 7α-dehydroxylase; 7α-dehydroxylase; bile acid 7-dehydroxylase; deoxycholate:NAD+ oxidoreductase
Systematic name: deoxycholate:FAD oxidoreductase (7α-dehydroxylating)
Comments: Under physiological conditions, the reactions form deoxycholate. This enzyme is highly specific for bile-acid substrates and requires a free C-24 carboxy group and an unhindered 7α-hydroxy group on the B-ring of the steroid nucleus for activity, as found in cholate and chenodeoxycholate. The reaction is stimulated by the presence of NAD+ but is inhibited by excess NADH. This unusual regulation by the NAD+/NADH ratio is most likely the result of the intermediates being linked at C-24 by an anhydride bond to the 5′-diphosphate of 3′-phospho-ADP [2,5,6]. Allodeoxycholate is also formed as a side-product of the 7α-dehydroxylation of cholate [6]. The enzyme is present in intestinal anaerobic bacteria [6], even though its products are important in mammalian physiology.
References:
1.  White, B.A., Cacciapuoti, A.F., Fricke, R.J., Whitehead, T.R., Mosbach, E.H. and Hylemon, P.B. Cofactor requirements for 7α-dehydroxylation of cholic and chenodeoxycholic acid in cell extracts of the intestinal anaerobic bacterium, Eubacterium species V.P.I. 12708. J. Lipid Res. 22 (1981) 891–898. [PMID: 7276750]
2.  White, B.A., Paone, D.A., Cacciapuoti, A.F., Fricke, R.J., Mosbach, E.H. and Hylemon, P.B. Regulation of bile acid 7-dehydroxylase activity by NAD+ and NADH in cell extracts of Eubacterium species V.P.I. 12708. J. Lipid Res. 24 (1983) 20–27. [PMID: 6833878]
3.  Coleman, J.P., White, W.B. and Hylemon, P.B. Molecular cloning of bile acid 7-dehydroxylase from Eubacterium sp. strain VPI 12708. J. Bacteriol. 169 (1987) 1516–1521. [PMID: 3549693]
4.  Russell, D.W. The enzymes, regulation, and genetics of bile acid synthesis. Annu. Rev. Biochem. 72 (2003) 137–174. [PMID: 12543708]
5.  Coleman, J.P., White, W.B., Egestad, B., Sjövall, J. and Hylemon, P.B. Biosynthesis of a novel bile acid nucleotide and mechanism of 7α-dehydroxylation by an intestinal Eubacterium species. J. Biol. Chem. 262 (1987) 4701–4707. [PMID: 3558364]
6.  Hylemon, P.B., Melone, P.D., Franklund, C.V., Lund, E. and Björkhem, I. Mechanism of intestinal 7α-dehydroxylation of cholic acid: evidence that allo-deoxycholic acid is an inducible side-product. J. Lipid Res. 32 (1991) 89–96. [PMID: 2010697]
[EC 1.17.98.1 created 2005 as EC 1.17.1.6, transferred 2006 to EC 1.17.99.5, transferred 2014 to EC 1.17.98.1]
 
 
EC 1.17.99.5 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Transferred entry: bile-acid 7α-dehydroxylase. Now classified as EC 1.17.98.1, bile-acid 7α-dehydroxylase.
[EC 1.17.99.5 created 2005 as EC 1.17.1.6, transferred 2006 to EC 1.17.99.5, deleted 2014]
 
 
EC 1.17.99.6 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: epoxyqueuosine reductase
Reaction: queuosine34 in tRNA + acceptor + H2O = epoxyqueuosine34 in tRNA + reduced acceptor
Glossary: queuine = base Q = 2-amino-5-({[(1S,4S,5R)-4,5-dihydroxycyclopent-2-en-1-yl]amino}methyl)-1,7-dihydropyrrolo[3,2-e]pyrimidin-4-one
epoxyqueine = base oQ
Other name(s): oQ reductase; QueG
Systematic name: queuosine34 in tRNA:acceptor oxidoreductase
Comments: This enzyme catalyses the last step in the bacterial biosynthetic pathway to queuosine, the modified guanosine base in the wobble position in tRNAs specific for Tyr, His, Asp or Asn.
References:
1.  Miles, Z.D., McCarty, R.M., Molnar, G. and Bandarian, V. Discovery of epoxyqueuosine (oQ) reductase reveals parallels between halorespiration and tRNA modification. Proc. Natl. Acad. Sci. USA 108 (2011) 7368–7372. [PMID: 21502530]
[EC 1.17.99.6 created 2014]
 
 
*EC 1.19.6.1 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: nitrogenase (flavodoxin)
Reaction: 4 reduced flavodoxin + N2 + 16 ATP + 16 H2O = 4 oxidized flavodoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
Systematic name: reduced flavodoxin:dinitrogen oxidoreductase (ATP-hydrolysing)
Comments: Requires Mg2+. It is composed of two components, dinitrogen reductase and dinitrogenase, that can be separated but are both required for nitrogenase activity. Dinitrogen reductase is a [4Fe-4S] protein, which, at the expense of ATP, transfers electrons from a dedicated flavodoxin to dinitrogenase. Dinitrogenase is a protein complex that contains either a molybdenum-iron cofactor, a vanadium-iron cofactor, or an iron-iron cofactor, that reduces dinitrogen in three succesive two-electron reductions from nitrogen to diimine to hydrazine to two molecules of ammonia. The reduction is initiated by formation of hydrogen. The enzyme can also reduce acetylene to ethylene (but only very slowly to ethane), azide to nitrogen and ammonia, and cyanide to methane and ammonia. In the absence of a suitable substrate, hydrogen is slowly formed. Some enzymes utilize ferredoxin rather than flavodoxin as the electron donor (see EC 1.18.6.1, nitrogenase).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, MetaCyc, CAS registry number: 9013-04-1
References:
1.  Zumft, W.G. and Mortenson, L.E. The nitrogen-fixing complex of bacteria. Biochim. Biophys. Acta 416 (1975) 1–52. [PMID: 164247]
2.  Eady, R.R., Smith, B.E., Cook, K.A. and Postgate, J.R. Nitrogenase of Klebsiella pneumoniae. Purification and properties of the component proteins. Biochem. J. 128 (1972) 655–675. [PMID: 4344006]
3.  Deistung, J., Cannon, F.C., Cannon, M.C., Hill, S. and Thorneley, R.N. Electron transfer to nitrogenase in Klebsiella pneumoniae. nifF gene cloned and the gene product, a flavodoxin, purified. Biochem. J. 231 (1985) 743–753. [PMID: 3907625]
[EC 1.19.6.1 created 1984, modified 2014]
 
 
EC 1.21.98.1 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: cyclic dehypoxanthinyl futalosine synthase
Reaction: dehypoxanthine futalosine + S-adenosyl-L-methionine = cyclic dehypoxanthinyl futalosine + 5′-deoxyadenosine + L-methionine
For diagram of the futalosine pathway, click here
Glossary: dehypoxanthine futalosine = 3-{3-[(2R,3S,4R)-3,4,5-trihydroxytetrahydrofuran-2-yl]propanoyl}benzoate
cyclic dehypoxanthinyl futalosine = (2R,3S,4R)-3,4,5-trihydroxy-4′-oxo-3′,4,4′,5-tetrahydro-2’H,3H-spiro[furan-2,1′-naphthalene]-6′-carboxylate
Other name(s): MqnC; dehypoxanthinyl futalosine cyclase
Systematic name: dehypoxanthine futalosine:S-adenosyl-L-methionine oxidoreductase (cyclizing)
Comments: This enzyme is a member of the ’AdoMet radical’ (radical SAM) family. The enzyme, found in several bacterial species, is part of the futalosine pathway for menaquinone biosynthesis.
References:
1.  Hiratsuka, T., Furihata, K., Ishikawa, J., Yamashita, H., Itoh, N., Seto, H. and Dairi, T. An alternative menaquinone biosynthetic pathway operating in microorganisms. Science 321 (2008) 1670–1673. [PMID: 18801996]
2.  Cooper, L.E., Fedoseyenko, D., Abdelwahed, S.H., Kim, S.H., Dairi, T. and Begley, T.P. In vitro reconstitution of the radical S-adenosylmethionine enzyme MqnC involved in the biosynthesis of futalosine-derived menaquinone. Biochemistry 52 (2013) 4592–4594. [PMID: 23763543]
[EC 1.21.98.1 created 2014 as EC 1.21.99.2, transferred 2014 to EC 1.21.98.1]
 
 
EC 1.21.99.2 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Transferred entry: EC 1.21.99.2, cyclic dehypoxanthinyl futalosine synthase. Now classified as EC 1.21.98.1, cyclic dehypoxanthinyl futalosine synthase.
[EC 1.21.99.2 created 2014, deleted 2014]
 
 
*EC 2.1.1.192 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: 23S rRNA (adenine2503-C2)-methyltransferase
Reaction: (1) 2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine + L-methionine + 5′-deoxyadenosine + 2-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
(2) 2 S-adenosyl-L-methionine + adenine37 in tRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine + L-methionine + 5′-deoxyadenosine + 2-methyladenine37 in tRNA + 2 oxidized [2Fe-2S] ferredoxin
Other name(s): RlmN; YfgB; Cfr
Systematic name: S-adenosyl-L-methionine:23S rRNA (adenine2503-C2)-methyltransferase
Comments: Contains an [4Fe-4S] cluster [2]. 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 appended methyl group. RlmN first transfers an CH2 group to a conserved cysteine (Cys355 in Escherichia coli) [6], the generated radical from a second S-adenosyl-L-methionine then attacks the methyl group, exctracting a hydrogen. The formed radical forms a covalent intermediate with the adenine group of the tRNA [9]. RlmN is an endogenous enzyme used by the cell to refine functions of the ribosome in protein synthesis [2]. The enzyme methylates adenosine by a radical mechanism with CH2 from the S-adenosyl-L-methionine and retention of the hydrogen at C-2 of adenosine2503 of 23S rRNA. It will also methylate 8-methyladenosine2503 of 23S rRNA. cf. EC 2.1.1.224 [23S rRNA (adenine2503-C8)-methyltransferase].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, MetaCyc
References:
1.  Toh, S.M., Xiong, L., Bae, T. and Mankin, A.S. The methyltransferase YfgB/RlmN is responsible for modification of adenosine 2503 in 23S rRNA. RNA 14 (2008) 98–106. [PMID: 18025251]
2.  Yan, F., LaMarre, J.M., Röhrich, R., Wiesner, J., Jomaa, H., Mankin, A.S. and Fujimori, D.G. RlmN and Cfr are radical SAM enzymes involved in methylation of ribosomal RNA. J. Am. Chem. Soc. 132 (2010) 3953–3964. [PMID: 20184321]
3.  Yan, F. and Fujimori, D.G. RNA methylation by radical SAM enzymes RlmN and Cfr proceeds via methylene transfer and hydride shift. Proc. Natl. Acad. Sci. USA 108 (2011) 3930–3934. [PMID: 21368151]
4.  Grove, T.L., Benner, J.S., Radle, M.I., Ahlum, J.H., Landgraf, B.J., Krebs, C. and Booker, S.J. A radically different mechanism for S-adenosylmethionine-dependent methyltransferases. Science 332 (2011) 604–607. [PMID: 21415317]
5.  Boal, A.K., Grove, T.L., McLaughlin, M.I., Yennawar, N.H., Booker, S.J. and Rosenzweig, A.C. Structural basis for methyl transfer by a radical SAM enzyme. Science 332 (2011) 1089–1092. [PMID: 21527678]
6.  Grove, T.L., Radle, M.I., Krebs, C. and Booker, S.J. Cfr and RlmN contain a single [4Fe-4S] cluster, which directs two distinct reactivities for S-adenosylmethionine: methyl transfer by SN2 displacement and radical generation. J. Am. Chem. Soc. 133 (2011) 19586–19589. [PMID: 21916495]
7.  McCusker, K.P., Medzihradszky, K.F., Shiver, A.L., Nichols, R.J., Yan, F., Maltby, D.A., Gross, C.A. and Fujimori, D.G. Covalent intermediate in the catalytic mechanism of the radical S-adenosyl-L-methionine methyl synthase RlmN trapped by mutagenesis. J. Am. Chem. Soc. 134 (2012) 18074–18081. [PMID: 23088750]
8.  Benitez-Paez, A., Villarroya, M. and Armengod, M.E. The Escherichia coli RlmN methyltransferase is a dual-specificity enzyme that modifies both rRNA and tRNA and controls translational accuracy. RNA 18 (2012) 1783–1795. [PMID: 22891362]
9.  Silakov, A., Grove, T.L., Radle, M.I., Bauerle, M.R., Green, M.T., Rosenzweig, A.C., Boal, A.K. and Booker, S.J. Characterization of a cross-linked protein-nucleic acid substrate radical in the reaction catalyzed by RlmN. J. Am. Chem. Soc. 136 (2014) 8221–8228. [PMID: 24806349]
[EC 2.1.1.192 created 2010, modified 2011, modified 2014]
 
 
*EC 2.1.1.224 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: 23S rRNA (adenine2503-C8)-methyltransferase
Reaction: 2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine + L-methionine + 5′-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
Other name(s): Cfr (gene name)
Systematic name: S-adenosyl-L-methionine:23S rRNA (adenine2503-C8)-methyltransferase
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 appended methyl group. It contains an [4Fe-S] cluster [1]. Cfr is an plasmid-acquired methyltransferase that protects cells from the action of antibiotics [1]. The enzyme methylates adenosine at position 2503 of 23S rRNA by a radical mechanism, transferring a CH2 group from S-adenosyl-L-methionine while retaining the hydrogen at the C-8 position of the adenine. RlmN first transfers an CH2 group to a conserved cysteine (Cys338 in Staphylococcus aureus) [7], the generated radical from a second S-adenosyl-L-methionine then attacks the methyl group, exctracting a hydrogen. The formed radical forms a covalent intermediate with the adenine group of the tRNA [8]. The enzyme will also methylate 2-methyladenine produced by the action of EC 2.1.1.192 [23S rRNA (adenine2503-C2)-methyltransferase].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, MetaCyc
References:
1.  Giessing, A.M., Jensen, S.S., Rasmussen, A., Hansen, L.H., Gondela, A., Long, K., Vester, B. and Kirpekar, F. Identification of 8-methyladenosine as the modification catalyzed by the radical SAM methyltransferase Cfr that confers antibiotic resistance in bacteria. RNA 15 (2009) 327–336. [PMID: 19144912]
2.  Kaminska, K.H., Purta, E., Hansen, L.H., Bujnicki, J.M., Vester, B. and Long, K.S. Insights into the structure, function and evolution of the radical-SAM 23S rRNA methyltransferase Cfr that confers antibiotic resistance in bacteria. Nucleic Acids Res. 38 (2010) 1652–1663. [PMID: 20007606]
3.  Yan, F., LaMarre, J.M., Röhrich, R., Wiesner, J., Jomaa, H., Mankin, A.S. and Fujimori, D.G. RlmN and Cfr are radical SAM enzymes involved in methylation of ribosomal RNA. J. Am. Chem. Soc. 132 (2010) 3953–3964. [PMID: 20184321]
4.  Yan, F. and Fujimori, D.G. RNA methylation by radical SAM enzymes RlmN and Cfr proceeds via methylene transfer and hydride shift. Proc. Natl. Acad. Sci. USA 108 (2011) 3930–3934. [PMID: 21368151]
5.  Grove, T.L., Benner, J.S., Radle, M.I., Ahlum, J.H., Landgraf, B.J., Krebs, C. and Booker, S.J. A radically different mechanism for S-adenosylmethionine-dependent methyltransferases. Science 332 (2011) 604–607. [PMID: 21415317]
6.  Boal, A.K., Grove, T.L., McLaughlin, M.I., Yennawar, N.H., Booker, S.J. and Rosenzweig, A.C. Structural basis for methyl transfer by a radical SAM enzyme. Science 332 (2011) 1089–1092. [PMID: 21527678]
7.  Grove, T.L., Radle, M.I., Krebs, C. and Booker, S.J. Cfr and RlmN contain a single [4Fe-4S] cluster, which directs two distinct reactivities for S-adenosylmethionine: methyl transfer by SN2 displacement and radical generation. J. Am. Chem. Soc. 133 (2011) 19586–19589. [PMID: 21916495]
8.  Grove, T.L., Livada, J., Schwalm, E.L., Green, M.T., Booker, S.J. and Silakov, A. A substrate radical intermediate in catalysis by the antibiotic resistance protein Cfr. Nat. Chem. Biol. 9 (2013) 422–427. [PMID: 23644479]
[EC 2.1.1.224 created 2011, modified 2014]
 
 
EC 2.1.1.308 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: 2-hydroxyethylphosphonate methyltransferase
Reaction: S-adenosyl-L-methionine + methylcob(III)alamin + 2-hydroxyethylphosphonate = 5′-deoxyadenosine + L-methionine + cob(III)alamin + (2S)-2-hydroxypropylphosphonate
Other name(s): Fom3
Systematic name: S-adenosyl-L-methionine:methylcob(III)alamin:2-hydroxyethylphosphonate methyltransferase
Comments: Requires cobalamin. The enzyme, isolated from the bacterium Streptomyces wedmorensis, is a member of the ’AdoMet radical’ (radical SAM) family. Involved in fosfomycin biosynthesis.
References:
1.  Woodyer, R.D., Li, G., Zhao, H. and van der Donk, W.A. New insight into the mechanism of methyl transfer during the biosynthesis of fosfomycin. Chem. Commun. (Camb.) (2007) 359–361. [PMID: 17220970]
2.  Allen, K.D. and Wang, S.C. Initial characterization of Fom3 from Streptomyces wedmorensis: The methyltransferase in fosfomycin biosynthesis. Arch. Biochem. Biophys. 543 (2014) 67–73. [PMID: 24370735]
[EC 2.1.1.308 created 2014]
 
 
EC 2.1.1.309 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: 18S rRNA (guanine1575-N7)-methyltransferase
Reaction: S-adenosyl-L-methionine + guanine1575 in 18S rRNA = S-adenosyl-L-homocysteine + N7-methylguanine1575 in 18S rRNA
Other name(s): 18S rRNA methylase Bud23; BUD23 (gene name)
Systematic name: S-adenosyl-L-methionine:18S rRNA (guanine1575-N7)-methyltransferase
Comments: The enzyme, found in eukaryotes, is involved in pre-rRNA processing. The numbering corresponds to the enzyme from the yeast Saccharomyces cerevisiae [1].
References:
1.  White, J., Li, Z., Sardana, R., Bujnicki, J.M., Marcotte, E.M. and Johnson, A.W. Bud23 methylates G1575 of 18S rRNA and is required for efficient nuclear export of pre-40S subunits. Mol. Cell Biol. 28 (2008) 3151–3161. [PMID: 18332120]
[EC 2.1.1.309 created 2014]
 
 
EC 2.1.1.310 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: 25S rRNA (cytosine2870-C5)-methyltransferase
Reaction: S-adenosyl-L-methionine + cytosine2870 in 25S rRNA = S-adenosyl-L-homocysteine + 5-methylcytosine2870 in 25S rRNA
Other name(s): NOP2 (gene name)
Systematic name: S-adenosyl-L-methionine:25S rRNA (cytosine2870-C5)-methyltransferase
Comments: The enzyme, found in eukaryotes, is specific for cytosine2870 of the 25S ribosomal RNA. The numbering corresponds to the enzyme from the yeast Saccharomyces cerevisiae [1].
References:
1.  Sharma, S., Yang, J., Watzinger, P., Kotter, P. and Entian, K.D. Yeast Nop2 and Rcm1 methylate C2870 and C2278 of the 25S rRNA, respectively. Nucleic Acids Res. 41 (2013) 9062–9076. [PMID: 23913415]
[EC 2.1.1.310 created 2014]
 
 
EC 2.1.1.311 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: 25S rRNA (cytosine2278-C5)-methyltransferase
Reaction: S-adenosyl-L-methionine + cytosine2278 in 25S rRNA = S-adenosyl-L-homocysteine + 5-methylcytosine2278 in 25S rRNA
Other name(s): RCM1 (gene name)
Systematic name: S-adenosyl-L-methionine:25S rRNA (cytosine2278-C5)-methyltransferase
Comments: The enzyme, found in eukaryotes, is specific for 25S cytosine2278. The numbering corresponds to the enzyme from the yeast Saccharomyces cerevisiae [1].
References:
1.  Sharma, S., Yang, J., Watzinger, P., Kotter, P. and Entian, K.D. Yeast Nop2 and Rcm1 methylate C2870 and C2278 of the 25S rRNA, respectively. Nucleic Acids Res. 41 (2013) 9062–9076. [PMID: 23913415]
[EC 2.1.1.311 created 2014]
 
 
EC 2.1.1.312 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: 25S rRNA (uracil2843-N3)-methyltransferase
Reaction: S-adenosyl-L-methionine + uracil2843 in 25S rRNA = S-adenosyl-L-homocysteine + N3-methyluracil2843 in 25S rRNA
Other name(s): BMT6
Systematic name: S-adenosyl-L-methionine:tRNA (uracil2843-N3)-methyltransferase
Comments: The enzyme, described from the yeast Saccharomyces cerevisiae, is involved in ribosome biogenesis.
References:
1.  Sharma, S., Yang, J., Duttmann, S., Watzinger, P., Kotter, P. and Entian, K.D. Identification of novel methyltransferases, Bmt5 and Bmt6, responsible for the m3U methylations of 25S rRNA in Saccharomyces cerevisiae. Nucleic Acids Res. 42 (2014) 3246–3260. [PMID: 24335083]
[EC 2.1.1.312 created 2014]
 
 
EC 2.1.1.313 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: 25S rRNA (uracil2634-N3)-methyltransferase
Reaction: S-adenosyl-L-methionine + uracil2634 in 25S rRNA = S-adenosyl-L-homocysteine + N3-methyluracil2634 in 25S rRNA
Other name(s): BMT5
Systematic name: S-adenosyl-L-methionine:tRNA (uracil2634-N3)-methyltransferase
Comments: The enzyme, described from the yeast Saccharomyces cerevisiae, is involved in ribosome biogenesis.
References:
1.  Sharma, S., Yang, J., Duttmann, S., Watzinger, P., Kotter, P. and Entian, K.D. Identification of novel methyltransferases, Bmt5 and Bmt6, responsible for the m3U methylations of 25S rRNA in Saccharomyces cerevisiae. Nucleic Acids Res. 42 (2014) 3246–3260. [PMID: 24335083]
[EC 2.1.1.313 created 2014]
 
 
EC 2.2.1.12 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: 3-acetyloctanal synthase
Reaction: pyruvate + (E)-oct-2-enal = (S)-3-acetyloctanal + CO2
Other name(s): pigD (gene name)
Systematic name: pyruvate:(E)-oct-2-enal acetaldehydetransferase (decarboxylating)
Comments: Requires thiamine diphosphate. The enzyme, characterized from the bacterium Serratia marcescens, participates in the biosynthesis of the antibiotic prodigiosin. The enzyme decarboxylates pyruvate, followed by attack of the resulting two-carbon fragment on (E)-oct-2-enal, resulting in a Stetter reaction. In vitro the enzyme can act on a number of α,β-unsaturated carbonyl compounds, including aldehydes and ketones, and can catalyse both 1-2 and 1-4 carboligations depending on the substrate.
References:
1.  Williamson, N.R., Simonsen, H.T., Ahmed, R.A., Goldet, G., Slater, H., Woodley, L., Leeper, F.J. and Salmond, G.P. Biosynthesis of the red antibiotic, prodigiosin, in Serratia: identification of a novel 2-methyl-3-n-amyl-pyrrole (MAP) assembly pathway, definition of the terminal condensing enzyme, and implications for undecylprodigiosin biosynthesis in Streptomyces. Mol. Microbiol. 56 (2005) 971–989. [PMID: 15853884]
2.  Dresen, C., Richter, M., Pohl, M., Ludeke, S. and Muller, M. The enzymatic asymmetric conjugate umpolung reaction. Angew Chem Int Ed Engl 49 (2010) 6600–6603. [PMID: 20669204]
3.  Kasparyan, E., Richter, M., Dresen, C., Walter, L.S., Fuchs, G., Leeper, F.J., Wacker, T., Andrade, S.L., Kolter, G., Pohl, M. and Muller, M. Asymmetric Stetter reactions catalyzed by thiamine diphosphate-dependent enzymes. Appl. Microbiol. Biotechnol. (2014) . [PMID: 24957249]
[EC 2.2.1.12 created 2014]
 
 
EC 2.3.1.234 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: N6-L-threonylcarbamoyladenine synthase
Reaction: L-threonylcarbamoyladenylate + adenine37 in tRNA = AMP + N6-L-threonylcarbamoyladenine37 in tRNA
For diagram of N6-L-threonylcarbamoyladenosine37 modified tRNA biosynthesis, click here
Glossary: N6-L-threonylcarbamoyladenine37 = t6A37
Other name(s): t6A synthase; Kae1; ygjD (gene name); Qri7
Systematic name: L-threonylcarbamoyladenylate:adenine37 in tRNA N6-L-threonylcarbamoyltransferase
Comments: The enzyme is involved in the synthesis of N6-threonylcarbamoyladenosine37 in tRNAs, which is found in tRNAs with the anticodon NNU, i.e. tRNAIle, tRNAThr, tRNAAsn, tRNALys, tRNASer and tRNAArg [3].
References:
1.  Lauhon, C.T. Mechanism of N6-threonylcarbamoyladenonsine (t6A) biosynthesis: isolation and characterization of the intermediate threonylcarbamoyl-AMP. Biochemistry 51 (2012) 8950–8963. [PMID: 23072323]
2.  Deutsch, C., El Yacoubi, B., de Crecy-Lagard, V. and Iwata-Reuyl, D. Biosynthesis of threonylcarbamoyl adenosine (t6A), a universal tRNA nucleoside. J. Biol. Chem. 287 (2012) 13666–13673. [PMID: 22378793]
3.  Perrochia, L., Crozat, E., Hecker, A., Zhang, W., Bareille, J., Collinet, B., van Tilbeurgh, H., Forterre, P. and Basta, T. In vitro biosynthesis of a universal t6A tRNA modification in Archaea and Eukarya. Nucleic Acids Res. 41 (2013) 1953–1964. [PMID: 23258706]
4.  Wan, L.C.K., Mao, D.Y.L., Neculai, D., Strecker, J., Chiovitti, D., Kurinov, I., Poda, G., Thevakumaran, N., Yuan, F., Szilard, R.K., Lissina, E., Nislow, C., Caudy, A.A., Durocher, D. and Sicheri, F. Reconstitution and characterization of eukaryotic N6-threonylcarbamoylation of tRNA using a minimal enzyme system. Nucleic Acids Res. 41 (2013) 6332–6346. [PMID: 23620299]
[EC 2.3.1.234 created 2014 as EC 2.6.99.4, transferred 2014 to EC 2.3.1.234]
 
 
EC 2.3.1.235 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: tetracenomycin F2 synthase
Reaction: 10 malonyl-CoA = tetracenomycin F2 + 10 CoA + 10 CO2 + 2 H2O
Glossary: tetracenomycin F2 = 4-(3-acetyl-4,5,7,10-tetrahydroxyanthracen-2-yl)-3-oxobutanoic acid
Other name(s): TCM PKS
Systematic name: malonyl-CoA:acetate malonyltransferase (tetracenomycin F2 forming)
Comments: A multi-domain polyketide synthase involved in the synthesis of tetracenomycin in the bacterium Streptomyces glaucescens. It involves a ketosynthase complex (TcmKL), an acyl carrier protein (TcmM), a malonyl CoA:ACP acyltransferase (MAT), and a cyclase (TcmN). A malonyl-CoA molecule is initially bound to the acyl carrier protein and decarboxylated to form an acetyl starter unit. Additional two-carbon units are added from nine more malonyl-CoA molecules.
References:
1.  Bao, W., Wendt-Pienkowski, E. and Hutchinson, C.R. Reconstitution of the iterative type II polyketide synthase for tetracenomycin F2 biosynthesis. Biochemistry 37 (1998) 8132–8138. [PMID: 9609708]
[EC 2.3.1.235 created 2014]
 
 
EC 2.3.1.236 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: 5-methylnaphthoic acid synthase
Reaction: acetyl-CoA + 5 malonyl-CoA + 3 NADPH + 3 H+ = 5-methyl-1-naphthoate + 6 CoA + 5 CO2 + 4 H2O + 3 NADP+
Other name(s): AziB
Systematic name: malonyl-CoA:acetyl-CoA malonyltransferase (5-methyl-1-naphthoic acid forming)
Comments: A multi-domain polyketide synthase involved in the synthesis of azinomycin B in the bacterium Streptomyces griseofuscus.
References:
1.  Zhao, Q., He, Q., Ding, W., Tang, M., Kang, Q., Yu, Y., Deng, W., Zhang, Q., Fang, J., Tang, G. and Liu, W. Characterization of the azinomycin B biosynthetic gene cluster revealing a different iterative type I polyketide synthase for naphthoate biosynthesis. Chem. Biol. 15 (2008) 693–705. [PMID: 18635006]
[EC 2.3.1.236 created 2014]
 
 
EC 2.3.1.237 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: neocarzinostatin naphthoate synthase
Reaction: acetyl-CoA + 5 malonyl-CoA + 2 NADPH + 2 H+ = 2-hydroxy-5-methyl-1-naphthoate + 6 CoA + 5 CO2 + 3 H2O + 2 NADP+
Other name(s): naphthoic acid synthase; NNS; ncsB (gene name)
Systematic name: malonyl-CoA:acetyl-CoA malonyltransferase (2-hydroxy-5-methyl-1-naphthoic acid forming)
Comments: A multi-domain polyketide synthase involved in the synthesis of neocarzinostatin in the bacterium Streptomyces carzinostaticus.
References:
1.  Sthapit, B., Oh, T.J., Lamichhane, R., Liou, K., Lee, H.C., Kim, C.G. and Sohng, J.K. Neocarzinostatin naphthoate synthase: an unique iterative type I PKS from neocarzinostatin producer Streptomyces carzinostaticus. FEBS Lett 566 (2004) 201–206. [PMID: 15147895]
[EC 2.3.1.237 created 2014]
 
 
EC 2.3.1.238 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: monacolin J acid methylbutanoate transferase
Reaction: monacolin J acid + (S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase] = lovastatin acid + [2-methylbutanoate polyketide synthase]
Glossary: monacolin J acid = (3R,5R)-7-[(1S,2S,6R,8S,8aR)-8-hydroxy-2,6-dimethyl-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]-3,5-dihydroxyheptanoate
lovastatin acid = (3R,5R)-7-[(1S,2S,6R,8S,8aR)-2,6-dimethyl-8-{[(2S)-2-methylbutanoyl]oxy}-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]-3,5-dihydroxyheptanoate
Other name(s): LovD
Systematic name: monacolin J acid:(S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase] (S)-2-methylbutanoate transferase
Comments: The enzyme catalyses the ultimate reaction in the lovastatin biosynthesis pathway of the filamentous fungus Aspergillus terreus.
References:
1.  Kennedy, J., Auclair, K., Kendrew, S.G., Park, C., Vederas, J.C. and Hutchinson, C.R. Modulation of polyketide synthase activity by accessory proteins during lovastatin biosynthesis. Science 284 (1999) 1368–1372. [PMID: 10334994]
2.  Xie, X., Watanabe, K., Wojcicki, W.A., Wang, C.C. and Tang, Y. Biosynthesis of lovastatin analogs with a broadly specific acyltransferase. Chem. Biol. 13 (2006) 1161–1169. [PMID: 17113998]
3.  Xie, X., Meehan, M.J., Xu, W., Dorrestein, P.C. and Tang, Y. Acyltransferase mediated polyketide release from a fungal megasynthase. J. Am. Chem. Soc. 131 (2009) 8388–8389. [PMID: 19530726]
[EC 2.3.1.238 created 2014]
 
 
EC 2.3.1.239 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: 10-deoxymethynolide syntase
Reaction: malonyl-CoA + 5 (2S)-methylmalonyl-CoA + 5 NADPH + 5 H+ = 10-deoxymethynolide + 6 CoA + 6 CO2 + 5 NADP+ + 2 H2O
Other name(s): pikromycin PKS
Systematic name: (2S)-methylmalonyl-CoA:malonyl-CoA malonyltransferase (10-deoxymethynolide forming)
Comments: The product, 10-deoxymethynolide, contains a 12-membered ring and is an intermediate in the biosynthesis of methymycin in the bacterium Streptomyces venezuelae. The enzyme also produces narbonolide (see EC 2.3.1.240, narbonolide synthase). The enzyme has 29 active sites arranged in four polypeptides (pikAI - pikAIV) with a loading domain, six extension modules and a terminal thioesterase domain. Each extension module contains a ketosynthase (KS), keto reductase (KR), an acyltransferase (AT) and an acyl-carrier protein (ACP). Not all active sites are used in the biosynthesis.
References:
1.  Lu, H., Tsai, S.C., Khosla, C. and Cane, D.E. Expression, site-directed mutagenesis, and steady state kinetic analysis of the terminal thioesterase domain of the methymycin/picromycin polyketide synthase. Biochemistry 41 (2002) 12590–12597. [PMID: 12379101]
2.  Kittendorf, J.D., Beck, B.J., Buchholz, T.J., Seufert, W. and Sherman, D.H. Interrogating the molecular basis for multiple macrolactone ring formation by the pikromycin polyketide synthase. Chem. Biol. 14 (2007) 944–954. [PMID: 17719493]
3.  Yan, J., Gupta, S., Sherman, D.H. and Reynolds, K.A. Functional dissection of a multimodular polypeptide of the pikromycin polyketide synthase into monomodules by using a matched pair of heterologous docking domains. Chembiochem 10 (2009) 1537–1543. [PMID: 19437523]
4.  Whicher, J.R., Dutta, S., Hansen, D.A., Hale, W.A., Chemler, J.A., Dosey, A.M., Narayan, A.R., Hakansson, K., Sherman, D.H., Smith, J.L. and Skiniotis, G. Structural rearrangements of a polyketide synthase module during its catalytic cycle. Nature 510 (2014) 560–564. [PMID: 24965656]
[EC 2.3.1.239 created 2014]
 
 
EC 2.3.1.240 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: narbonolide synthase
Reaction: malonyl-CoA + 6 (2S)-methylmalonyl-CoA + 5 NADPH + 5 H+ = narbonolide + 7 CoA + 7 CO2 + 5 NADP+ + 2 H2O
Other name(s): pikromycin PKS
Systematic name: (2S)-methylmalonyl-CoA:malonyl-CoA malonyltransferase (narbonolide forming)
Comments: The product, narbonolide, contains a 14-membered ring and is an intermediate in the biosynthesis of narbonomycin and pikromycin in the bacterium Streptomyces venezuelae. The enzyme also produces 10-deoxymethynolide (see EC 2.3.1.239, 10-deoxymethynolide synthase). The enzyme has 29 active sites arranged in four polypeptides (pikAI - pikAIV) with a loading domain, six extension modules and a terminal thioesterase domain. Each extension module contains a ketosynthase (KS), keto reductase (KR), an acyltransferase (AT) and an acyl-carrier protein (ACP). Not all active sites are used in the biosynthesis.
References:
1.  Lu, H., Tsai, S.C., Khosla, C. and Cane, D.E. Expression, site-directed mutagenesis, and steady state kinetic analysis of the terminal thioesterase domain of the methymycin/picromycin polyketide synthase. Biochemistry 41 (2002) 12590–12597. [PMID: 12379101]
2.  Kittendorf, J.D., Beck, B.J., Buchholz, T.J., Seufert, W. and Sherman, D.H. Interrogating the molecular basis for multiple macrolactone ring formation by the pikromycin polyketide synthase. Chem. Biol. 14 (2007) 944–954. [PMID: 17719493]
3.  Yan, J., Gupta, S., Sherman, D.H. and Reynolds, K.A. Functional dissection of a multimodular polypeptide of the pikromycin polyketide synthase into monomodules by using a matched pair of heterologous docking domains. Chembiochem 10 (2009) 1537–1543. [PMID: 19437523]
4.  Whicher, J.R., Dutta, S., Hansen, D.A., Hale, W.A., Chemler, J.A., Dosey, A.M., Narayan, A.R., Hakansson, K., Sherman, D.H., Smith, J.L. and Skiniotis, G. Structural rearrangements of a polyketide synthase module during its catalytic cycle. Nature 510 (2014) 560–564. [PMID: 24965656]
[EC 2.3.1.240 created 2014]
 
 
EC 2.3.1.241 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: Kdo2-lipid IVA lauroyltransferase
Reaction: a dodecanoyl-[acyl-carrier protein] + (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-α-D-glucopyranose = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-α-D-glucopyranose + an [acyl-carrier protein]
Glossary: α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-α-D-glucopyranose
Other name(s): LpxL; htrB (gene name); dodecanoyl-[acyl-carrier protein]:α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA O-dodecanoyltransferase; lauroyl-[acyl-carrier protein]:Kdo2-lipid IVA O-lauroyltransferase; (Kdo)2-lipid IVA lauroyltransferase; α-Kdo-(2→4)-α-(2→6)-lipid IVA lauroyltransferase
Systematic name: dodecanoyl-[acyl-carrier protein]:Kdo2-lipid IVA O-dodecanoyltransferase
Comments: The enzyme, characterized from the bacterium Escherichia coli, is involed in the biosynthesis of the phosphorylated outer membrane glycolipid lipid A.
References:
1.  Clementz, T., Bednarski, J.J. and Raetz, C.R. Function of the htrB high temperature requirement gene of Escherichia coli in the acylation of lipid A: HtrB catalyzed incorporation of laurate. J. Biol. Chem. 271 (1996) 12095–12102. [PMID: 8662613]
2.  Six, D.A., Carty, S.M., Guan, Z. and Raetz, C.R. Purification and mutagenesis of LpxL, the lauroyltransferase of Escherichia coli lipid A biosynthesis. Biochemistry 47 (2008) 8623–8637. [PMID: 18656959]
[EC 2.3.1.241 created 2014]
 
 
EC 2.3.1.242 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: Kdo2-lipid IVA palmitoleoyltransferase
Reaction: a palmitoleoyl-[acyl-carrier protein] + (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-α-D-glucopyranose = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-[[(3R)-3-((9Z)-hexadec-9-enoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-α-D-glucopyranose + an [acyl-carrier protein]
Glossary: α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-α-D-glucopyranose
Other name(s): LpxP; palmitoleoyl-acyl carrier protein-dependent acyltransferase; cold-induced palmitoleoyl transferase; palmitoleoyl-[acyl-carrier protein]:Kdo2-lipid IVA O-palmitoleoyltransferase; (Kdo)2-lipid IVA palmitoleoyltransferase; α-Kdo-(2→4)-α-(2→6)-lipid IVA palmitoleoyltransferase
Systematic name: palmitoleoyl-[acyl-carrier protein]:α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA O-palmitoleoyltransferase
Comments: The enzyme, characterized from the bacterium Escherichia coli, is induced upon cold shock and is involved in the formation of a cold-adapted variant of the outer membrane glycolipid lipid A.
References:
1.  Carty, S.M., Sreekumar, K.R. and Raetz, C.R. Effect of cold shock on lipid A biosynthesis in Escherichia coli. Induction At 12 degrees C of an acyltransferase specific for palmitoleoyl-acyl carrier protein. J. Biol. Chem. 274 (1999) 9677–9685. [PMID: 10092655]
2.  Vorachek-Warren, M.K., Carty, S.M., Lin, S., Cotter, R.J. and Raetz, C.R. An Escherichia coli mutant lacking the cold shock-induced palmitoleoyltransferase of lipid A biosynthesis: absence of unsaturated acyl chains and antibiotic hypersensitivity at 12 degrees C. J. Biol. Chem. 277 (2002) 14186–14193. [PMID: 11830594]
[EC 2.3.1.242 created 2014]
 
 
EC 2.3.1.243 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: lauroyl-Kdo2-lipid IVA myristoyltransferase
Reaction: a tetradecanoyl-[acyl-carrier protein] + (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-[[(3R)-3-dodecanoyloxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-α-D-glucopyranose = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-α-D-glucopyranose + an [acyl-carrier protein]
Glossary: α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-α-D-glucopyranose

α-Kdo-(2→4)-α-Kdo-(2→6)-lipid A = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(16)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-α-D-glucopyranose

Kdo = 3-deoxy-D-manno-octulosonic acid
Other name(s): MsbB acyltransferase; lpxM (gene name); myristoyl-[acyl-carrier protein]:α-Kdo-(2→4)-α-Kdo-(2→6)-(dodecanoyl)-lipid IVA O-myristoyltransferase
Systematic name: tetradecanoyl-[acyl-carrier protein]:dodecanoyl-Kdo2-lipid IVA O-tetradecanoyltransferase
Comments: The enzyme, characterized from the bacterium Escherichia coli, is involed in the biosynthesis of the phosphorylated outer membrane glycolipid lipid A.
References:
1.  Clementz, T., Zhou, Z. and Raetz, C.R. Function of the Escherichia coli msbB gene, a multicopy suppressor of htrB knockouts, in the acylation of lipid A. Acylation by MsbB follows laurate incorporation by HtrB. J. Biol. Chem. 272 (1997) 10353–10360. [PMID: 9099672]
[EC 2.3.1.243 created 2014]
 
 
EC 2.4.1.332 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: 1,2-α-glucosylglycerol phosphorylase
Reaction: 2-O-α-D-glucopyranosyl-sn-glycerol + phosphate = β-D-glucose 1-phosphate + glycerol
Other name(s): 2-O-α-D-glucopyranosylglycerol phosphorylase
Systematic name: 2-O-α-D-glucopyranosyl-sn-glycerol:phosphate β-D-glucosyltransferase
Comments: The enzyme has been isolated from the bacterium Bacillus selenitireducens. In the absence of glycerol the enzyme produces α-D-glucopyranose and phosphate from β-D-glucopyranose 1-phosphate. In this reaction the glucosyl residue is transferred to a water molecule with an inversion of the anomeric conformation.
References:
1.  Nihira, T., Saito, Y., Ohtsubo, K., Nakai, H. and Kitaoka, M. 2-O-α-D-glucosylglycerol phosphorylase from Bacillus selenitireducens MLS10 possessing hydrolytic activity on β-D-glucose 1-phosphate. PLoS One 9:e86548 (2014). [PMID: 24466148]
2.  Touhara, K.K., Nihira, T., Kitaoka, M., Nakai, H. and Fushinobu, S. Structural basis for reversible phosphorolysis and hydrolysis reactions of 2-O-α-glucosylglycerol phosphorylase. J. Biol. Chem. 289 (2014) 18067–18075. [PMID: 24828502]
[EC 2.4.1.332 created 2014]
 
 
EC 2.4.1.333 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: 1,2-β-oligoglucan phosphorylase
Reaction: [(1→2)-β-D-glucosyl]n + phosphate = [(1→2)-β-D-glucosyl]n-1 + α-D-glucose 1-phosphate
Systematic name: 1,2-β-D-glucan:phosphate α-D-glucosyltransferase
Comments: The enzyme has been isolated from the bacterium Listeria innocua. It catalyses the reversible phosphorolysis of β-(1→2)-D-glucans. The minimum length of the substrate for the phosphorolytic reaction is 3 D-glucose units. In the synthetic reaction starting from sophorose and α-D-glucose 1-phosphate the average polymerisation degree is 39.
References:
1.  Nakajima, M., Toyoizumi, H., Abe, K., Nakai, H., Taguchi, H. and Kitaoka, M. 1,2-β-Oligoglucan phosphorylase from Listeria innocua. PLoS One 9:e92353 (2014). [PMID: 24647662]
[EC 2.4.1.333 created 2014]
 
 
EC 2.4.1.334 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: 1,3-α-oligoglucan phosphorylase
Reaction: [(1→3)-α-D-glucosyl]n + phosphate = [(1→3)-α-D-glucosyl]n-1 + β-D-glucose 1-phosphate
Systematic name: 1,3-α-D-glucan:phosphate β-D-glucosyltransferase
Comments: The enzyme, isolated from the bacterium Clostridium phytofermentans, catalyses a reversible reaction. Substrates for the phosphorolytic reaction are α-1,3-linked oligoglucans with a polymerisation degree of 3 or more. Nigerose (i.e. 3-O-α-D-glucopyranosyl-D-glucopyranose) is not phosphorylyzed but can serve as substrate in the reverse direction (cf. EC 2.4.1.279, nigerose phosphorylase).
References:
1.  Nihira, T., Nishimoto, M., Nakai, H., Ohtsubo, K., and Kitaoka, M. Characterization of two phosphorylases for α-1,3-oligoglucans from Clostridium phytofermentans. J. Appl. Glycosci. 61 (2014) 59–66.
[EC 2.4.1.334 created 2014]
 
 
*EC 2.4.2.54 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: β-ribofuranosylhydroxybenzene 5′-phosphate synthase
Reaction: 5-phospho-α-D-ribose 1-diphosphate + 4-hydroxybenzoate = 4-(β-D-ribofuranosyl)hydroxybenzene 5′-phosphate + diphosphate
For diagram of methanopterin biosynthesis (part 2), click here
Other name(s): β-RFAP synthase (incorrect); β-RFA-P synthase (incorrect); AF2089 (gene name); MJ1427 (gene name); 4-(β-D-ribofuranosyl)aminobenzene 5′-phosphate synthase (incorrect); β-ribofuranosylaminobenzene 5′-phosphate synthase (incorrect)
Systematic name: 5-phospho-α-D-ribose 1-diphosphate:4-aminobenzoate 5-phospho-β-D-ribofuranosyltransferase (decarboxylating)
Comments: The enzyme is involved in biosynthesis of tetrahydromethanopterin in archaea. It was initially thought to use 4-aminobenzoate as a substrate, but was later shown to utilize 4-hydroxybenzoate [4]. The activity is dependent on Mg2+ or Mn2+ [1].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, MetaCyc
References:
1.  Rasche, M.E. and White, R.H. Mechanism for the enzymatic formation of 4-(β-D-ribofuranosyl)aminobenzene 5′-phosphate during the biosynthesis of methanopterin. Biochemistry 37 (1998) 11343–11351. [PMID: 9698382]
2.  Scott, J.W. and Rasche, M.E. Purification, overproduction, and partial characterization of β-RFAP synthase, a key enzyme in the methanopterin biosynthesis pathway. J. Bacteriol. 184 (2002) 4442–4448. [PMID: 12142414]
3.  Dumitru, R.V. and Ragsdale, S.W. Mechanism of 4-(β-D-ribofuranosyl)aminobenzene 5′-phosphate synthase, a key enzyme in the methanopterin biosynthetic pathway. J. Biol. Chem. 279 (2004) 39389–39395. [PMID: 15262968]
4.  White, R.H. The conversion of a phenol to an aniline occurs in the biochemical formation of the 1-(4-aminophenyl)-1-deoxy-D-ribitol moiety in methanopterin. Biochemistry 50 (2011) 6041–6052. [PMID: 21634403]
[EC 2.4.2.54 created 2013, modified 2014]
 
 
*EC 2.5.1.25 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: tRNA-uridine aminocarboxypropyltransferase
Reaction: S-adenosyl-L-methionine + uridine47 tRNAPhe = S-methyl-5′-thioadenosine + 3-[(3S)-3-amino-3-carboxypropyl]-uridine47 in tRNAPhe
Other name(s): S-adenosyl-L-methionine:tRNA-uridine 3-(3-amino-3-carboxypropyl)transferase
Systematic name: S-adenosyl-L-methionine:uridine47 in tRNAPhe 3-[(3S)-3-amino-3-carboxypropyl]transferase
Comments: The enzyme was studied in the bacterium Escherichia coli. The modification is found in the variable loop of the tRNA.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, MetaCyc
References:
1.  Nishimura, S., Taya, Y., Kuchino, Y. and Ohashi, Z. Enzymatic synthesis of 3-(3-amino-3-carboxypropyl)uridine in Escherichia coli phenylalanine transfer RNA: transfer of the 3-amino-acid-3-carboxypropyl group from S-adenosylmethionine. Biochem. Biophys. Res. Commun. 57 (1974) 702–708. [PMID: 4597321]
[EC 2.5.1.25 created 1984, modified 2014]
 
 
EC 2.5.1.128 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: N4-bis(aminopropyl)spermidine synthase
Reaction: 2 S-adenosyl 3-(methylthio)propylamine + spermidine = 2 S-methyl-5′-thioadenosine + N4-bis(aminopropyl)spermidine (overall reaction)
(1a) S-adenosyl 3-(methylthio)propylamine + spermidine = S-methyl-5′-thioadenosine + N4-aminopropylspermidine
(1b) S-adenosyl 3-(methylthio)propylamine + N4-aminopropylspermidine = S-methyl-5′-thioadenosine + N4-bis(aminopropyl)spermidine
Glossary: spermidine = N-(3-aminopropyl)-1,4-butanediamine
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-(methylthio)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.
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 2.6.99.4 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Transferred entry: N6-L-threonylcarbamoyladenine synthase. Now EC 2.3.1.234, N6-L-threonylcarbamoyladenine synthase.
[EC 2.6.99.4 created 2014, deleted 2014]
 
 
*EC 2.7.7.67 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase
Reaction: CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate = diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
For diagram of archaetidylserine biosynthesis, click here and for diagram of archaetidylserine biosynthesis, click here
Glossary: 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate = 2,3-bis-(O-geranylgeranyl)-glycerophosphate ether = unsaturated archaetidic acid
CDP-unsaturated archaeol = CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
Other name(s): CDP-2,3-di-O-geranylgeranyl-sn-glycerol synthase; CTP:2,3-GG-GP ether cytidylyltransferase; CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase; CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol synthase; CTP:2,3-bis-O-(geranylgeranyl)-sn-glycero-1-phosphate cytidylyltransferase; CDP-unsaturated archaeol synthase; CDP-archaeol synthase (incorrect)
Systematic name: CTP:2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate cytidylyltransferase
Comments: This enzyme catalyses one of the steps in the biosynthesis of polar lipids in archaea, which are characterized by having an sn-glycerol 1-phosphate backbone rather than an sn-glycerol 3-phosphate backbone as is found in bacteria and eukaryotes [1]. The enzyme requires Mg2+ and K+ for maximal activity [1].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, MetaCyc, PDB, CAS registry number: 329791-09-5
References:
1.  Morii, H., Nishihara, M. and Koga, Y. CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase in the methanogenic archaeon Methanothermobacter thermoautotrophicus. J. Biol. Chem. 275 (2000) 36568–36574. [PMID: 10960477]
2.  Morii, H. and Koga, Y. CDP-2,3-di-O-geranylgeranyl-sn-glycerol:L-serine O-archaetidyltransferase (archaetidylserine synthase) in the methanogenic archaeon Methanothermobacter thermautotrophicus. J. Bacteriol. 185 (2003) 1181–1189. [PMID: 12562787]
[EC 2.7.7.67 created 2009, modified 2014]
 
 
EC 2.7.8.41 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: cardiolipin synthase (CMP-forming)
Reaction: a CDP-diacylglycerol + a phosphatidylglycerol = a cardiolipin + CMP
Systematic name: CDP-diacylglycerol:phosphatidylglycerol diacylglycerolphosphotransferase (CMP-forming)
Comments: The eukaryotic enzyme is involved in the biosynthesis of the mitochondrial phospholipid cardiolipin. It requires divalent cations for activity.
References:
1.  Schlame, M. and Hostetler, K.Y. Solubilization, purification, and characterization of cardiolipin synthase from rat liver mitochondria. Demonstration of its phospholipid requirement. J. Biol. Chem. 266 (1991) 22398–22403. [PMID: 1657995]
2.  Nowicki, M., Muller, F. and Frentzen, M. Cardiolipin synthase of Arabidopsis thaliana. FEBS Lett 579 (2005) 2161–2165. [PMID: 15811335]
3.  Houtkooper, R.H., Akbari, H., van Lenthe, H., Kulik, W., Wanders, R.J., Frentzen, M. and Vaz, F.M. Identification and characterization of human cardiolipin synthase. FEBS Lett 580 (2006) 3059–3064. [PMID: 16678169]
4.  Sandoval-Calderon, M., Geiger, O., Guan, Z., Barona-Gomez, F. and Sohlenkamp, C. A eukaryote-like cardiolipin synthase is present in Streptomyces coelicolor and in most actinobacteria. J. Biol. Chem. 284 (2009) 17383–17390. [PMID: 19439403]
5.  Sarma, P.V., Srikanth, L., Venkatesh, K., Murthy, P.S. and Sarma, P.U. Isolation, purification and characterization of cardiolipin synthase from Mycobacterium phlei. Bioinformation 9 (2013) 690–695. [PMID: 23930021]
[EC 2.7.8.41 created 2014]
 
 
*EC 2.8.1.6 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: biotin synthase
Reaction: dethiobiotin + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = biotin + (sulfur carrier) + 2 L-methionine + 2 5′-deoxyadenosine + 2 oxidized [2Fe-2S] ferredoxin
Other name(s): dethiobiotin:sulfur sulfurtransferase
Systematic name: dethiobiotin:sulfur-(sulfur carrier) sulfurtransferase
Comments: The enzyme binds a [4Fe-4S] and a [2Fe-2S] cluster. In every reaction cycle, the enzyme consumes two molecules of AdoMet, each producing 5′-deoxyadenosine and a putative dethiobiotinyl carbon radical. Reaction with another equivalent of AdoMet results in abstraction of the C6 methylene pro-S hydrogen atom from 9-mercaptodethiobiotin, and the resulting carbon radical is quenched via formation of an intramolecular C-S bond, thus closing the biotin thiophane ring. The sulfur donor is believed to be the [2Fe-2S] cluster, which is sacrificed in the process, so that in vitro the reaction is a single turnover. In vivo, the [2Fe-2S] cluster can be reassembled by the Isc or Suf iron-sulfur cluster assembly systems, to allow further catalysis.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, MetaCyc, PDB, CAS registry number: 80146-93-6
References:
1.  Trainor, D.A., Parry, R.J. and Gitterman, A. Biotin biosynthesis. 2. Stereochemistry of sulfur introduction at C-4 of dethiobiotin. J. Am. Chem. Soc. 102 (1980) 1467–1468.
2.  Shiuan, D. and Campbell, A. Transcriptional regulation and gene arrangement of Escherichia coli, Citrobacter freundii and Salmonella typhimurium biotin operons. Gene 67 (1988) 203–211. [PMID: 2971595]
3.  Zhang, S., Sanyal, I., Bulboaca, G.H., Rich, A. and Flint, D.H. The gene for biotin synthase from Saccharomyces cerevisiae: cloning, sequencing, and complementation of Escherichia coli strains lacking biotin synthase. Arch. Biochem. Biophys. 309 (1994) 29–35. [PMID: 8117110]
4.  Ugulava, N.B., Gibney, B.R. and Jarrett, J.T. Biotin synthase contains two distinct iron-sulfur cluster binding sites: chemical and spectroelectrochemical analysis of iron-sulfur cluster interconversions. Biochemistry 40 (2001) 8343–8351. [PMID: 11444981]
5.  Berkovitch, F., Nicolet, Y., Wan, J.T., Jarrett, J.T. and Drennan, C.L. Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme. Science 303 (2004) 76–79. [PMID: 14704425]
6.  Lotierzo, M., Tse Sum Bui, B., Florentin, D., Escalettes, F. and Marquet, A. Biotin synthase mechanism: an overview. Biochem. Soc. Trans. 33 (2005) 820–823. [PMID: 16042606]
7.  Taylor, A.M., Farrar, C.E. and Jarrett, J.T. 9-Mercaptodethiobiotin is formed as a competent catalytic intermediate by Escherichia coli biotin synthase. Biochemistry 47 (2008) 9309–9317. [PMID: 18690713]
8.  Reyda, M.R., Fugate, C.J. and Jarrett, J.T. A complex between biotin synthase and the iron-sulfur cluster assembly chaperone HscA that enhances in vivo cluster assembly. Biochemistry 48 (2009) 10782–10792. [PMID: 19821612]
[EC 2.8.1.6 created 1999, modified 2006, modified 2011, modified 2014]
 
 
*EC 2.8.1.8 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: lipoyl synthase
Reaction: protein N6-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = protein N6-(lipoyl)lysine + 2 (sulfur carrier) + 2 L-methionine + 2 5′-deoxyadenosine + 2 oxidized [2Fe-2S] ferredoxin
Other name(s): LS; LipA; lipoate synthase; protein 6-N-(octanoyl)lysine:sulfur sulfurtransferase; protein N6-(octanoyl)lysine:sulfur sulfurtransferase
Systematic name: protein N6-(octanoyl)lysine:sulfur-(sulfur carrier) sulfurtransferase
Comments: This enzyme is a member of the ’AdoMet radical’ (radical SAM) family, all members of which produce the 5′-deoxyadenosin-5′-yl radical and methionine from AdoMet [i.e. S-adenosylmethionine, or S-(5′-deoxyadenosin-5′-yl)methionine], by the addition of an electron from an iron-sulfur centre. The radical is converted into 5′-deoxyadenosine when it abstracts a hydrogen atom from C-6 and C-8, leaving reactive radicals at these positions so that they can add sulfur, with inversion of configuration [4]. This enzyme catalyses the final step in the de-novo biosynthesis of the lipoyl cofactor, with the other enzyme involved being EC 2.3.1.181, lipoyl(octanoyl) transferase. Lipoylation is essential for the function of several key enzymes involved in oxidative metabolism, as it converts apoprotein into the biologically active holoprotein. Examples of such lipoylated proteins include pyruvate dehydrogenase (E2 domain), 2-oxoglutarate dehydrogenase (E2 domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein) [2,5]. An alternative lipoylation pathway involves EC 2.7.7.63, lipoate—protein ligase, which can lipoylate apoproteins using exogenous lipoic acid (or its analogues) [7].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, MetaCyc, CAS registry number: 189398-80-9
References:
1.  Cicchillo, R.M. and Booker, S.J. Mechanistic investigations of lipoic acid biosynthesis in Escherichia coli: both sulfur atoms in lipoic acid are contributed by the same lipoyl synthase polypeptide. J. Am. Chem. Soc. 127 (2005) 2860–2861. [PMID: 15740115]
2.  Vanden Boom, T.J., Reed, K.E. and Cronan, J.E., Jr. Lipoic acid metabolism in Escherichia coli: isolation of null mutants defective in lipoic acid biosynthesis, molecular cloning and characterization of the E. coli lip locus, and identification of the lipoylated protein of the glycine cleavage system. J. Bacteriol. 173 (1991) 6411–6420. [PMID: 1655709]
3.  Zhao, X., Miller, J.R., Jiang, Y., Marletta, M.A. and Cronan, J.E. Assembly of the covalent linkage between lipoic acid and its cognate enzymes. Chem. Biol. 10 (2003) 1293–1302. [PMID: 14700636]
4.  Cicchillo, R.M., Iwig, D.F., Jones, A.D., Nesbitt, N.M., Baleanu-Gogonea, C., Souder, M.G., Tu, L. and Booker, S.J. Lipoyl synthase requires two equivalents of S-adenosyl-L-methionine to synthesize one equivalent of lipoic acid. Biochemistry 43 (2004) 6378–6386. [PMID: 15157071]
5.  Jordan, S.W. and Cronan, J.E., Jr. A new metabolic link. The acyl carrier protein of lipid synthesis donates lipoic acid to the pyruvate dehydrogenase complex in Escherichia coli and mitochondria. J. Biol. Chem. 272 (1997) 17903–17906. [PMID: 9218413]
6.  Miller, J.R., Busby, R.W., Jordan, S.W., Cheek, J., Henshaw, T.F., Ashley, G.W., Broderick, J.B., Cronan, J.E., Jr. and Marletta, M.A. Escherichia coli LipA is a lipoyl synthase: in vitro biosynthesis of lipoylated pyruvate dehydrogenase complex from octanoyl-acyl carrier protein. Biochemistry 39 (2000) 15166–15178. [PMID: 11106496]
7.  Perham, R.N. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu. Rev. Biochem. 69 (2000) 961–1004. [PMID: 10966480]
[EC 2.8.1.8 created 2006, modified 2014]
 
 
EC 3.1.1.97 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: diphthine methylesterase
Reaction: diphthine methyl ester-[translation elongation factor 2] + H2O = diphthine-[translation elongation factor 2] + methanol
Glossary: diphthine methyl ester = 2-[(3S)-3-carboxy methyl ester-3-(trimethylammonio)propyl]-L-histidine
diphthine = 2-[(3S)-3-carboxy-3-(trimethylammonio)propyl]-L-histidine
Other name(s): Dph7
Systematic name: diphthine methyl ester acylhydrolase
Comments: The protein is only present in eukaryotes.
References:
1.  Lin, Z., Su, X., Chen, W., Ci, B., Zhang, S. and Lin, H. Dph7 catalyzes a previously unknown demethylation step in diphthamide biosynthesis. J. Am. Chem. Soc. 136 (2014) 6179–6182. [PMID: 24739148]
[EC 3.1.1.97 created 2014]
 
 
EC 3.1.3.96 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: pseudouridine 5′-phosphatase
Reaction: pseudouridine 5′-phosphate + H2O = pseudouridine + phosphate
Other name(s): pseudouridine 5′-monophosphatase; 5′-PsiMPase; HDHD1
Systematic name: pseudouridine 5′-phosphohydrolase
Comments: Requires Mg2+ for activity.
References:
1.  Preumont, A., Rzem, R., Vertommen, D. and Van Schaftingen, E. HDHD1, which is often deleted in X-linked ichthyosis, encodes a pseudouridine-5′-phosphatase. Biochem. J. 431 (2010) 237–244. [PMID: 20722631]
[EC 3.1.3.96 created 2014]
 
 
EC 3.5.1.27 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Deleted entry: N-formylmethionylaminoacyl-tRNA deformylase. The activity is covered by EC 3.5.1.88, peptide deformylase
[EC 3.5.1.27 created 1972, deleted 2014]
 
 
EC 3.5.2.20 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: isatin hydrolase
Reaction: isatin + H2O = isatinate
Glossary: isatin = 1H-indole-2,3-dione
isatinate = 2-(2-aminophenyl)-2-oxoacetate
Systematic name: isatin amidohydrolase
Comments: Requires Mn2+. This enzyme, found in several bacterial species, is involved in the degradation of indole-3-acetic acid.
References:
1.  Sommer, M.R. and Jochimsen, B. Identification of enzymes involved in indole-3-acetic acid degradation. Plant Soil 186 (1996) 143–149.
2.  Bjerregaard-Andersen, K., Sommer, T., Jensen, J.K., Jochimsen, B., Etzerodt, M. and Morth, J.P. A proton wire and water channel revealed in the crystal structure of isatin hydrolase. J. Biol. Chem. 289 (2014) 21351–21359. [PMID: 24917679]
[EC 3.5.2.20 created 2014]
 
 
*EC 3.5.4.20 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: pyrithiamine deaminase
Reaction: 1-(4-amino-2-methylpyrimid-5-ylmethyl)-3-(β-hydroxyethyl)-2-methylpyridinium + H2O = 1-(4-hydroxy-2-methylpyrimid-5-ylmethyl)-3-(β-hydroxyethyl)-2-methylpyridinium + NH3
Systematic name: 1-(4-amino-2-methylpyrimid-5-ylmethyl)-3-(β-hydroxyethyl)-2-methylpyridinium aminohydrolase
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, MetaCyc, CAS registry number: 37289-23-9
References:
1.  Sinha, A.K. and Chatterjee, G.C. Metabolism of pyrithiamine by the pyrithiamine-requiring mutant of Staphylococcus aureus. Biochem. J. 107 (1968) 165–169. [PMID: 5641872]
[EC 3.5.4.20 created 1972, modified 2014]
 
 
EC 3.6.1.67 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: dihydroneopterin triphosphate diphosphatase
Reaction: 7,8-dihydroneopterin 3′-triphosphate + H2O = 7,8-dihydroneopterin 3′-phosphate + diphosphate
Other name(s): folQ (gene name); nudB (gene name); NUDT1 (gene name); dihydroneopterin triphosphate pyrophosphohydrolase
Systematic name: 7,8-dihydroneopterin 3′-triphosphate diphosphohydrolase
Comments: The enzyme participates in a folate biosynthesis pathway, which is found in bacteria, fungi, and plants. Requires Mg2+.
References:
1.  Suzuki, Y. and Brown, G.M. The biosynthesis of folic acid. XII. Purification and properties of dihydroneopterin triphosphate pyrophosphohydrolase. J. Biol. Chem. 249 (1974) 2405–2410. [PMID: 4362677]
2.  O'Handley, S.F., Frick, D.N., Bullions, L.C., Mildvan, A.S. and Bessman, M.J. Escherichia coli orf17 codes for a nucleoside triphosphate pyrophosphohydrolase member of the MutT family of proteins. Cloning, purification, and characterization of the enzyme. J. Biol. Chem. 271 (1996) 24649–24654. [PMID: 8798731]
3.  Klaus, S.M., Wegkamp, A., Sybesma, W., Hugenholtz, J., Gregory, J.F., 3rd and Hanson, A.D. A nudix enzyme removes pyrophosphate from dihydroneopterin triphosphate in the folate synthesis pathway of bacteria and plants. J. Biol. Chem. 280 (2005) 5274–5280. [PMID: 15611104]
4.  Gabelli, S.B., Bianchet, M.A., Xu, W., Dunn, C.A., Niu, Z.D., Amzel, L.M. and Bessman, M.J. Structure and function of the E. coli dihydroneopterin triphosphate pyrophosphatase: a Nudix enzyme involved in folate biosynthesis. Structure 15 (2007) 1014–1022. [PMID: 17698004]
[EC 3.6.1.67 created 2014]
 
 
*EC 4.1.99.19 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: 2-iminoacetate synthase
Reaction: L-tyrosine + S-adenosyl-L-methionine + NADPH = 2-iminoacetate + 4-methylphenol + 5′-deoxyadenosine + L-methionine + NADP+ + H+
For diagram of thiamine diphosphate biosynthesis, click here
Glossary: 4-methylphenol = 4-cresol = p-cresol
Other name(s): thiH (gene name)
Systematic name: L-tyrosine 4-methylphenol-lyase (2-iminoacetate-forming)
Comments: Binds a [4Fe-4S] cluster that is coordinated by 3 cysteines and an exchangeable S-adenosyl-L-methionine molecule. The first stage of catalysis is reduction of the S-adenosyl-L-methionine to produce methionine and a 5-deoxyadenosin-5-yl radical that is crucial for the conversion of the substrate. The reductant is assumed to be NADPH, which is provided by a flavoprotein:NADPH oxidoreductase system [4]. Part of the pathway for thiamine biosynthesis.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, MetaCyc
References:
1.  Leonardi, R., Fairhurst, S.A., Kriek, M., Lowe, D.J. and Roach, P.L. Thiamine biosynthesis in Escherichia coli: isolation and initial characterisation of the ThiGH complex. FEBS Lett. 539 (2003) 95–99. [PMID: 12650933]
2.  Kriek, M., Martins, F., Challand, M.R., Croft, A. and Roach, P.L. Thiamine biosynthesis in Escherichia coli: identification of the intermediate and by-product derived from tyrosine. Angew. Chem. Int. Ed. Engl. 46 (2007) 9223–9226. [PMID: 17969213]
3.  Kriek, M., Martins, F., Leonardi, R., Fairhurst, S.A., Lowe, D.J. and Roach, P.L. Thiazole synthase from Escherichia coli: an investigation of the substrates and purified proteins required for activity in vitro. J. Biol. Chem. 282 (2007) 17413–17423. [PMID: 17403671]
4.  Challand, M.R., Martins, F.T. and Roach, P.L. Catalytic activity of the anaerobic tyrosine lyase required for thiamine biosynthesis in Escherichia coli. J. Biol. Chem. 285 (2010) 5240–5248. [PMID: 19923213]
[EC 4.1.99.19 created 2011, modified 2014]
 
 
EC 4.2.3.148 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: cembrene C synthase
Reaction: geranylgeranyl diphosphate = cembrene C + diphosphate
Glossary: cembrene C = (1E,5E,9E)-1,5,9-trimethyl-12-(propan-2-ylidene)cyclotetradeca-1,5,9-triene
Other name(s): DtcycA (gene name)
Systematic name: geranylgeranyl-diphosphate diphosphate-lyase (cembrene-C-forming)
Comments: Requires Mg2+. Isolated from the bacterium Streptomyces sp. SANK 60404. This bifunctional enzyme also produces (R)-nephthenol. See EC 4.2.3.149, nephthenol synthase.
References:
1.  Meguro, A., Tomita, T., Nishiyama, M. and Kuzuyama, T. Identification and characterization of bacterial diterpene cyclases that synthesize the cembrane skeleton. Chembiochem 14 (2013) 316–321. [PMID: 23386483]
[EC 4.2.3.148 created 2014]
 
 
EC 4.2.3.149 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: nephthenol synthase
Reaction: geranylgeranyl diphosphate + H2O = (R)-nephthenol + diphosphate
Glossary: (R)-nephthenol = 2-[(1R,3E,7E,11E)-4,8,12-trimethyltetradeca-3,7,11-trien-1-yl]propan-2-ol
Other name(s): DtcycA (gene name); DtcycB (gene name)
Systematic name: geranylgeranyl-diphosphate diphosphate-lyase [(R)-nephthenol-forming]
Comments: Requires Mg2+. Two isozymes with this activity were isolated from the bacterium Streptomyces sp. SANK 60404. The enzyme encoded by the DtcycA gene also produces cembrene C (see EC 4.2.3.148, cembrene C synthase), while the enzyme encoded by the DtcycB gene also produces (R)-cembrene A and (1S,4E,8E,12E)-2,2,5,9,13-pentamethylcyclopentadeca-4,8,12-trien-1-ol (see EC 4.2.3.150, cembrene A synthase, and EC 4.2.3.151, pentamethylcyclopentadecatrienol synthase).
References:
1.  Meguro, A., Tomita, T., Nishiyama, M. and Kuzuyama, T. Identification and characterization of bacterial diterpene cyclases that synthesize the cembrane skeleton. Chembiochem 14 (2013) 316–321. [PMID: 23386483]
[EC 4.2.3.149 created 2014]
 
 
EC 4.2.3.150 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: cembrene A synthase
Reaction: geranylgeranyl diphosphate = (R)-cembrene A + diphosphate
Glossary: cembrene A = (1E,5E,9E,12R)-1,5,9-trimethyl-12-(propan-2-en-2-yl)cyclotetradeca-1,5,9-triene
Other name(s): DtcycB (gene name)
Systematic name: geranylgeranyl-diphosphate diphosphate-lyase [(R)-cembrene-A-forming]
Comments: Requires Mg2+. Isolated from the bacterium Streptomyces sp. SANK 60404. This trifunctional enzyme, which contains a [4Fe-4S] cluster, also produces (R)-nephthenol and (1S,4E,8E,12E)-2,2,5,9,13-pentamethylcyclopentadeca-4,8,12-trien-1-ol. See EC 4.2.3.149, nephthenol synthase and EC 4.2.3.151, pentamethylcyclopentadecatrienol synthase.
References:
1.  Meguro, A., Tomita, T., Nishiyama, M. and Kuzuyama, T. Identification and characterization of bacterial diterpene cyclases that synthesize the cembrane skeleton. Chembiochem 14 (2013) 316–321. [PMID: 23386483]
[EC 4.2.3.150 created 2014]
 
 
EC 4.2.3.151 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: pentamethylcyclopentadecatrienol synthase
Reaction: geranylgeranyl diphosphate + H2O = (1S,4E,8E,12E)-2,2,5,9,13-pentamethylcyclopentadeca-4,8,12-trien-1-ol + diphosphate
Other name(s): DtcycB (gene name)
Systematic name: geranylgeranyl-diphosphate diphosphate-lyase [(1S,4E,8E,12E)-2,2,5,9,13-pentamethylcyclopentadeca-4,8,12-trien-1-ol-forming]
Comments: Requires Mg2+. Isolated from the bacterium Streptomyces sp. SANK 60404. This trifunctional enzyme, which contains a [4Fe-4S] cluster, also produces (R)-nephthenol and (R)-cembrene A. See EC 4.2.3.150, cembrene A synthase and EC 4.2.3.149, nephthenol synthase.
References:
1.  Meguro, A., Tomita, T., Nishiyama, M. and Kuzuyama, T. Identification and characterization of bacterial diterpene cyclases that synthesize the cembrane skeleton. Chembiochem 14 (2013) 316–321. [PMID: 23386483]
[EC 4.2.3.151 created 2014]
 
 
EC 4.4.1.28 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: L-cysteine desulfidase
Reaction: L-cysteine + H2O = sulfide + NH3 + pyruvate (overall reaction)
(1a) L-cysteine = 2-aminoprop-2-enoate + sulfide
(1b) 2-aminoprop-2-enoate = 2-iminopropanoate (spontaneous)
(1c) 2-iminopropanoate + H2O = pyruvate + NH3 (spontaneous)
Other name(s): L-cysteine desulfhydrase
Systematic name: L-cysteine sulfide-lyase (deaminating; pyruvate-forming)
Comments: The enzyme from the archaeon Methanocaldococcus jannaschii contains a [4Fe-4S] cluster and is specific for L-cysteine (cf. EC 4.4.1.1, cystathionine γ-lyase). It cleaves a carbon-sulfur bound releasing sulfide and the unstable enamine product 2-aminoprop-2-enoate that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. The same reaction can also be catalysed by some pyridoxal-phosphate proteins (cf. EC 4.4.1.1, cystathionine γ-lyase).
References:
1.  Tchong, S.I., Xu, H. and White, R.H. L-cysteine desulfidase: an [4Fe-4S] enzyme isolated from Methanocaldococcus jannaschii that catalyzes the breakdown of L-cysteine into pyruvate, ammonia, and sulfide. Biochemistry 44 (2005) 1659–1670. [PMID: 15683250]
[EC 4.4.1.28 created 2014]
 
 
EC 5.5.1.25 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: 3,6-anhydro-α-L-galactonate cycloisomerase
Reaction: 3,6-anhydro-α-L-galactonate = 2-dehydro-3-deoxy-D-galactonate
Systematic name: 3,6-anhydro-α-L-galactonate lyase (ring-opening)
Comments: The enzyme, characterized from the marine bacterium Vibrio sp. EJY3, is involved in a degradation pathway for 3,6-anhydro-α-L-galactopyranose, a major component of the polysaccharides of red macroalgae.
References:
1.  Yun, E.J., Lee, S., Kim, H.T., Pelton, J.G., Kim, S., Ko, H.J., Choi, I.G. and Kim, K.H. The novel catabolic pathway of 3,6-anhydro-L-galactose, the main component of red macroalgae, in a marine bacterium. Environ Microbiol (2014) . [PMID: 25156229]
[EC 5.5.1.25 created 2014]
 
 
EC 6.3.2.45 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: UDP-N-acetylmuramate L-alanyl-γ-D-glutamyl-meso-2,6-diaminoheptandioate ligase
Reaction: ATP + UDP-N-acetyl-α-D-muramate + L-alanyl-γ-D-glutamyl-meso-2,6-diaminoheptanedioate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-γ-D-glutamyl-meso-2,6-diaminoheptanedioate
Glossary: meso-2,6-diaminoheptanedioate = meso-2,6-diaminopimelate
Other name(s): murein peptide ligase; Mpl; yjfG (gene name); UDP-MurNAc:L-Ala-γ-D-Glu-meso-A2pm ligase; UDP-N-acetylmuramate:L-alanyl-γ-D-glutamyl-meso-diaminopimelate ligase
Systematic name: UDP-N-acetylmuramate:L-alanyl-γ-D-glutamyl-meso-2,6-diaminoheptandioate ligase
Comments: The enzyme catalyses the reincorporation into peptidoglycan of the tripeptide L-alanyl-γ-D-glutamyl-2,6-meso-diaminoheptanedioate released during the maturation and constant remodeling of this bacterial cell wall polymer that occur during cell growth and division. The enzyme can also use the tetrapeptide L-alanyl-γ-D-glutamyl-meso-2,6-diaminoheptanedioyl-D-alanine or the pentapeptide L-alanyl-γ-D-glutamyl-meso-2,6-diaminoheptandioyl-D-alanyl-D-alanine in vivo and in vitro. Requires Mg2+.
References:
1.  Mengin-Lecreulx, D., van Heijenoort, J. and Park, J.T. Identification of the mpl gene encoding UDP-N-acetylmuramate: L-alanyl-γ-D-glutamyl-meso-diaminopimelate ligase in Escherichia coli and its role in recycling of cell wall peptidoglycan. J. Bacteriol. 178 (1996) 5347–5352. [PMID: 8808921]
2.  Herve, M., Boniface, A., Gobec, S., Blanot, D. and Mengin-Lecreulx, D. Biochemical characterization and physiological properties of Escherichia coli UDP-N-acetylmuramate:L-alanyl-γ-D-glutamyl-meso-diaminopimelate ligase. J. Bacteriol. 189 (2007) 3987–3995. [PMID: 17384195]
[EC 6.3.2.45 created 2014]
 
 
*EC 6.3.4.14 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: biotin carboxylase
Reaction: ATP + biotin-carboxyl-carrier protein + hydrogen carbonate = ADP + phosphate + carboxybiotin-carboxyl-carrier protein
Other name(s): biotin carboxylase (component of acetyl CoA carboxylase)
Systematic name: biotin-carboxyl-carrier-protein:carbon-dioxide ligase (ADP-forming)
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, MetaCyc, PDB, CAS registry number: 9075-71-2
References:
1.  Dimroth, P., Guchhait, R.B., Stoll, E. and Lane, M.D. Enzymatic carboxylation of biotin: molecular and catalytic properties of a component enzyme of acetyl CoA carboxylase. Proc. Natl. Acad. Sci. USA 67 (1970) 1353–1360. [PMID: 4922289]
[EC 6.3.4.14 created 1976, modified 2014]
 
 
EC 6.3.4.24 – public review until 15 January 2015 [Last modified: 2014-12-18 07:02:46]
Accepted name: tyramine—L-glutamate ligase
Reaction: ATP + tyramine + L-glutamate = ADP + phosphate + γ-glutamyltyramine
Other name(s): mfnD (gene name)
Systematic name: tyramine:L-glutamate γ-ligase (ADP-forming)
Comments: The enzyme, which has been characterized from the archaebacterium Methanocaldococcus fervens, participates in the biosynthesis of the cofactor methanofuran. Requires a divalent cation for activity, with Mn2+ giving the highest activity, followed by Mg2+, Co2+, Zn2+, and Fe2+.
References:
1.  Wang, Y., Xu, H., Harich, K.C. and White, R.H. Identification and characterization of a tyramine-glutamate ligase (MfnD) Involved in methanofuran biosynthesis. Biochemistry 53 (2014) 6220–6230. [PMID: 25211225]
[EC 6.3.4.24 created 2014]
 
 


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