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 To prevent confusion please do not quote new EC numbers until they are incorporated into the main list.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 1.8.2.6 S-disulfanyl-L-cysteine oxidoreductase
EC 1.13.12.24 calcium-regulated photoprotein
EC 1.14.11.58 ornithine lipid ester-linked acyl 2-hydroxylase
EC 1.14.11.59 2,4-dihydroxy-1,4-benzoxazin-3-one-glucoside dioxygenase
EC 1.14.13.97 transferred
EC 1.14.14.57 taurochenodeoxycholate 6α-hydroxylase
EC 1.14.14.58 trimethyltridecatetraene synthase
EC 1.14.14.59 dimethylnonatriene synthase
EC 1.14.14.60 ferruginol monooxygenase
EC 1.14.14.61 carnosic acid synthase
EC 1.14.14.62 salviol synthase
EC 1.14.14.63 β-amyrin 16β-monooxygenase
EC 1.14.14.64 β-amyrin 6β-monooxygenase
EC 1.14.14.65 sugiol synthase
EC 1.14.14.66 marmesin synthase
EC 1.14.14.67 11-hydroxysugiol 20-monooxygenase
EC 1.14.14.68 syn-pimaradiene 3-monooxygenase
EC 1.14.14.69 ent-cassadiene hydroxylase
EC 1.14.15.25 p-cymene methyl-monooxygenase
EC 1.14.15.26 toluene methyl-monooxygenase
EC 1.14.19.53 all-trans-retinol 3,4-desaturase
EC 1.14.20.2 transferred
*EC 2.1.1.294 3-O-phospho-polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol 3-phospho-methyltransferase
EC 2.1.1.346 U6 snRNA m6A methyltransferase
EC 2.1.1.347 (+)-O-methylkolavelool synthase
EC 2.1.5 Methylenetransferases
EC 2.1.5.1 sesamin methylene transferase
EC 2.3.1.96 deleted
EC 2.3.1.128 transferred
EC 2.3.1.266 [ribosomal protein S18]-alanine N-acetyltransferase
EC 2.3.1.267 [ribosomal protein S5]-alanine N-acetyltransferase
EC 2.3.1.268 ethanol O-acetyltransferase
EC 2.3.3.20 acyl-CoA:acyl-CoA alkyltransferase
EC 2.4.1.351 rhamnogalacturonan I rhamnosyltransferase
EC 2.4.1.352 glucosylglycerate phosphorylase
*EC 2.5.1.98 Rhizobium leguminosarum exopolysaccharide glucosyl ketal-pyruvate-transferase
EC 2.5.1.99 deleted
EC 2.6.1.114 8-demethyl-8-aminoriboflavin-5′-phosphate synthase
EC 2.7.9.6 rifampicin phosphotransferase
*EC 2.8.1.2 3-mercaptopyruvate sulfurtransferase
EC 3.1.1.103 teichoic acid D-alanine hydrolase
EC 3.2.2.31 adenine glycosylase
EC 3.13.1.7 carbonyl sulfide hydrolase
EC 5.1.3.39 deleted
*EC 5.3.3.8 Δ32-enoyl-CoA isomerase
EC 5.3.3.21 Δ3,52,4-dienoyl-CoA isomerase
EC 6.3.2.52 jasmonoyl—L-amino acid synthetase
*EC 6.3.4.14 biotin carboxylase
*EC 6.3.4.15 biotin—[biotin carboxyl-carrier protein] ligase
*EC 6.4.1.2 acetyl-CoA carboxylase


EC 1.8.2.6 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: S-disulfanyl-L-cysteine oxidoreductase
Reaction: [SoxY protein]-S-disulfanyl-L-cysteine + 6 ferricytochrome c + 3 H2O = [SoxY protein]-S-sulfosulfanyl-L-cysteine + 6 ferrocytochrome c + 6 H+
Other name(s): SoxCD; sulfur dehydrogenase
Systematic name: [SoxY protein]-S-disulfanyl-L-cysteine:cytochrome-c oxidoreductase
Comments: The enzyme is part of the Sox enzyme system, which participates in a bacterial thiosulfate oxidation pathway that produces sulfate. The enzyme from the bacterium Paracoccus pantotrophus contains a molybdoprotein component and a diheme c-type cytochrome component. The enzyme successively oxidizes the outer sulfur atom in [SoxY protein]-S-disulfanyl-L-cysteine, using three water molecules and forming [SoxY protein]-S-sulfosulfanyl-L-cysteine. During the process, six electrons are transferred to the electron chain via cytochrome c.
References:
1.  Friedrich, C.G., Rother, D., Bardischewsky, F., Quentmeier, A. and Fischer, J. Oxidation of reduced inorganic sulfur compounds by bacteria: emergence of a common mechanism. Appl. Environ. Microbiol. 67 (2001) 2873–2882. [PMID: 11425697]
2.  Bardischewsky, F., Quentmeier, A., Rother, D., Hellwig, P., Kostka, S. and Friedrich, C.G. Sulfur dehydrogenase of Paracoccus pantotrophus: the heme-2 domain of the molybdoprotein cytochrome c complex is dispensable for catalytic activity. Biochemistry 44 (2005) 7024–7034. [PMID: 15865447]
3.  Grabarczyk, D.B. and Berks, B.C. Intermediates in the Sox sulfur oxidation pathway are bound to a sulfane conjugate of the carrier protein SoxYZ. PLoS One 12:e0173395 (2017). [PMID: 28257465]
[EC 1.8.2.6 created 2018]
 
 
EC 1.13.12.24 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: calcium-regulated photoprotein
Reaction: [apoaequorin] + coelenterazine + O2 + 3 Ca2+ = [excited state blue fluorescent protein] + CO2 (overall reaction)
(1a) [apoaequorin] + coelenterazine = [apoaequorin containing coelenterazine]
(1b) [apoaequorin containing coelenterazine] + O2 = [aequorin]
(1c) [aequorin] + 3 Ca2+ = [aequorin] 1,2-dioxetan-3-one
(1d) [aequorin] 1,2-dioxetan-3-one = [excited state blue fluorescent protein] + CO2
Glossary: coelenterazine = 8-benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one
coelenteramide = N-[3-benzyl-5-(4-hydroxyphenyl)pyrazin-2-yl]-2-(4-hydroxyphenyl)acetamide
aequorin = the non-covalent complex formed by apoaequorin polypeptide and coelenterazine-2-hydroperoxide.
blue fluorescent protein = the non-covalent complex formed by Ca2+-bound apoaequorin polypeptide and coelenteramide
Other name(s): Ca2+-regulated photoprotein; calcium-activated photoprotein; aequorin; obelin; halistaurin; mitrocomin; phialidin; clytin; mnemiopsin; berovin
Systematic name: coelenterazine:oxygen 2-oxidoreductase (decarboxylating, calcium-dependent)
Comments: Ca2+-regulated photoproteins are found in a variety of bioluminescent marine organisms, mostly coelenterates, and are responsible for their light emission. The best studied enzyme is from the jellyfish Aequorea victoria. The enzyme tightly binds the imidazolopyrazinone derivative coelenterazine, which is then peroxidized by oxygen. The hydroperoxide is stably bound until three Ca2+ ions bind to the protein, inducing a structural change that results in the formation of a 1,2-dioxetan-3-one ring, followed by decarboxylation and generation of a protein-bound coelenteramide in an excited state. The calcium-bound protein-product complex is known as a blue fluorescent protein. In vivo the energy is transferred to a green fluorescent protein (GFP) by Förster resonance energy transfer. In vitro, in the absence of GFP, coelenteramide emits a photon of blue light while returning to its ground state.
References:
1.  Shimomura, O., Johnson, F. H., and Saiga, Y. Purification and properties of aequorin, a bio-(chemi-) luminescent protein from the jellyfish, Aequorea aequorea. Fed. Proc. 21 (1962) 401.
2.  Morise, H., Shimomura, O., Johnson, F.H. and Winant, J. Intermolecular energy transfer in the bioluminescent system of Aequorea. Biochemistry 13 (1974) 2656–2662. [PMID: 4151620]
3.  Inouye, S., Noguchi, M., Sakaki, Y., Takagi, Y., Miyata, T., Iwanaga, S., Miyata, T. and Tsuji, F.I. Cloning and sequence analysis of cDNA for the luminescent protein aequorin. Proc. Natl Acad. Sci. USA 82 (1985) 3154–3158. [PMID: 3858813]
4.  Head, J.F., Inouye, S., Teranishi, K. and Shimomura, O. The crystal structure of the photoprotein aequorin at 2.3 Å resolution. Nature 405 (2000) 372–376. [PMID: 10830969]
5.  Deng, L., Vysotski, E.S., Markova, S.V., Liu, Z.J., Lee, J., Rose, J. and Wang, B.C. All three Ca2+-binding loops of photoproteins bind calcium ions: the crystal structures of calcium-loaded apo-aequorin and apo-obelin. Protein Sci. 14 (2005) 663–675. [PMID: 15689515]
[EC 1.13.12.24 created 2018]
 
 
EC 1.14.11.58 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: ornithine lipid ester-linked acyl 2-hydroxylase
Reaction: an ornithine lipid + 2-oxoglutarate + O2 = a 2-hydroxyornithine lipid + succinate + CO2
Glossary: an ornithine lipid = an Nα-[(3R)-3-(acyloxy)acyl]-L-ornithine
a 2-hydroxyornithine lipid = an Nα-[(3R)-3-(2-hydroxyacyloxy)acyl]-L-ornithine
Other name(s): olsC (gene name)
Systematic name: ornithine lipid,2-oxoglutarate:oxygen oxidoreductase (ester-linked acyl 2-hydroxylase)
Comments: The enzyme, characterized from the bacterium Rhizobium tropici, catalyses the hydroxylation of C-2 of the fatty acyl group that is ester-linked to the 3-hydroxy position of the amide-linked fatty acid.
References:
1.  Rojas-Jimenez, K., Sohlenkamp, C., Geiger, O., Martinez-Romero, E., Werner, D. and Vinuesa, P. A ClC chloride channel homolog and ornithine-containing membrane lipids of Rhizobium tropici CIAT899 are involved in symbiotic efficiency and acid tolerance. Mol Plant Microbe Interact 18 (2005) 1175–1185. [PMID: 16353552]
2.  Vences-Guzman, M.A., Guan, Z., Ormeno-Orrillo, E., Gonzalez-Silva, N., Lopez-Lara, I.M., Martinez-Romero, E., Geiger, O. and Sohlenkamp, C. Hydroxylated ornithine lipids increase stress tolerance in Rhizobium tropici CIAT899. Mol. Microbiol. 79 (2011) 1496–1514. [PMID: 21205018]
[EC 1.14.11.58 created 2018]
 
 
EC 1.14.11.59 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: 2,4-dihydroxy-1,4-benzoxazin-3-one-glucoside dioxygenase
Reaction: (2R)-4-hydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside + 2-oxoglutarate + O2 = (2R)-4,7-dihydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside + succinate + CO2 + H2O
For diagram of benzoxazinone biosynthesis, click here
Glossary: (2R)-4-hydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside = DIBOA β-D-glucoside
(2R)-4,7-dihydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside = TRIBOA β-D-glucoside
Other name(s): BX6 (gene name); DIBOA-Glc dioxygenase
Systematic name: (2R)-4-hydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside:oxygen oxidoreductase (7-hydroxylating)
Comments: The enzyme is involved in the biosynthesis of protective and allelophatic benzoxazinoids in some plants, most commonly from the family of Poaceae (grasses).
References:
1.  Jonczyk, R., Schmidt, H., Osterrieder, A., Fiesselmann, A., Schullehner, K., Haslbeck, M., Sicker, D., Hofmann, D., Yalpani, N., Simmons, C., Frey, M. and Gierl, A. Elucidation of the final reactions of DIMBOA-glucoside biosynthesis in maize: characterization of Bx6 and Bx7. Plant Physiol. 146 (2008) 1053–1063. [PMID: 18192444]
[EC 1.14.11.59 created 2012 as EC 1.14.20.2, transferred 2018 to EC 1.14.11.59]
 
 
EC 1.14.13.97 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Transferred entry: taurochenodeoxycholate 6α-hydroxylase. Now EC 1.14.14.57, taurochenodeoxycholate 6α-hydroxylase
[EC 1.14.13.97 created 2005, deleted 2018]
 
 
EC 1.14.14.57 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: taurochenodeoxycholate 6α-hydroxylase
Reaction: (1) taurochenodeoxycholate + [reduced NADPH—hemoprotein reductase] + O2 = taurohyocholate + [oxidized NADPH—hemoprotein reductase] + H2O
(2) lithocholate + [reduced NADPH—hemoprotein reductase] + O2 = hyodeoxycholate + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of the biosynthesis of cholic-acid conjugates, click here
Glossary: taurochenodeoxycholic acid = N-(3α,7α-dihydroxy-5β-cholan-24-oyl)taurine
taurohyocholic acid = N-(3α,6α,7α-trihydroxy-5β-cholan-24-oyl)taurine
hyodeoxycholate = 3α,6α-dihydroxy-5β-cholan-24-oate
lithocholate = 3α-hydroxy-5β-cholan-24-oate
Other name(s): CYP3A4; CYP4A21; taurochenodeoxycholate 6α-monooxygenase
Systematic name: taurochenodeoxycholate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (6α-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. Requires cytochrome b5 for maximal activity. Acts on taurochenodeoxycholate, taurodeoxycholate and less readily on lithocholate and chenodeoxycholate. In adult pig (Sus scrofa), hyocholic acid replaces cholic acid as a primary bile acid [5].
References:
1.  Araya, Z. and Wikvall, K. 6α-Hydroxylation of taurochenodeoxycholic acid and lithocholic acid by CYP3A4 in human liver microsomes. Biochim. Biophys. Acta 1438 (1999) 47–54. [PMID: 10216279]
2.  Araya, Z., Hellman, U. and Hansson, R. Characterisation of taurochenodeoxycholic acid 6α-hydroxylase from pig liver microsomes. Eur. J. Biochem. 231 (1995) 855–861. [PMID: 7649186]
3.  Kramer, W., Sauber, K., Baringhaus, K.H., Kurz, M., Stengelin, S., Lange, G., Corsiero, D., Girbig, F., Konig, W. and Weyland, C. Identification of the bile acid-binding site of the ileal lipid-binding protein by photoaffinity labeling, matrix-assisted laser desorption ionization-mass spectrometry, and NMR structure. J. Biol. Chem. 276 (2001) 7291–7301. [PMID: 11069906]
4.  Lundell, K., Hansson, R. and Wikvall, K. Cloning and expression of a pig liver taurochenodeoxycholic acid 6α-hydroxylase (CYP4A21): a novel member of the CYP4A subfamily. J. Biol. Chem. 276 (2001) 9606–9612. [PMID: 11113117]
5.  Lundell, K. and Wikvall, K. Gene structure of pig sterol 12α-hydroxylase (CYP8B1) and expression in fetal liver: comparison with expression of taurochenodeoxycholic acid 6α-hydroxylase (CYP4A21). Biochim. Biophys. Acta 1634 (2003) 86–96. [PMID: 14643796]
6.  Russell, D.W. The enzymes, regulation, and genetics of bile acid synthesis. Annu. Rev. Biochem. 72 (2003) 137–174. [PMID: 12543708]
[EC 1.14.14.57 created 2005 asEC 1.14.13.97, transferred 2018 to EC 1.14.14.57]
 
 
EC 1.14.14.58 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: trimethyltridecatetraene synthase
Reaction: (6E,10E)-geranyllinalool + [reduced NADPH—hemoprotein reductase] + O2 = (3E,7E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene + [oxidized NADPH—hemoprotein reductase] + but-3-en-2-one + 2 H2O
Glossary: (6E,10E)-geranyllinalool = (6E,10E)-3,7,11,15-tetramethylhexadeca-1,6,10,14-tetraen-3-ol
Other name(s): CYP82G1; CYP92C5; CYP92C6; DMNT/TMTT homoterpene synthase
Systematic name: (6E,10E)-geranyllinalool,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase
Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the plants Arabidopsis thaliana (thale cress) and Zea mays (maize). It forms this C16 homoterpene in response to herbivore attack. In vitro some variants of the enzyme also convert (3S,6E)-nerolidol to (3E)-4,8-dimethylnona-1,3,7-triene (see EC 1.14.14.59, dimethylnonatriene synthase).
References:
1.  Lee, S., Badieyan, S., Bevan, D.R., Herde, M., Gatz, C. and Tholl, D. Herbivore-induced and floral homoterpene volatiles are biosynthesized by a single P450 enzyme (CYP82G1) in Arabidopsis. Proc. Natl Acad. Sci. USA 107 (2010) 21205–21210. [PMID: 21088219]
2.  Richter, A., Schaff, C., Zhang, Z., Lipka, A.E., Tian, F., Kollner, T.G., Schnee, C., Preiss, S., Irmisch, S., Jander, G., Boland, W., Gershenzon, J., Buckler, E.S. and Degenhardt, J. Characterization of biosynthetic pathways for the production of the volatile homoterpenes DMNT and TMTT in Zea mays. Plant Cell 28 (2016) 2651–2665. [PMID: 27662898]
[EC 1.14.14.58 created 2018]
 
 
EC 1.14.14.59 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: dimethylnonatriene synthase
Reaction: (3S,6E)-nerolidol + [reduced NADPH—hemoprotein reductase] + O2 = (3E)-4,8-dimethylnona-1,3,7-triene + [oxidized NADPH—hemoprotein reductase] + but-3-en-2-one + 2 H2O
Other name(s): CYP82G1; CYP92C5; DMNT/TMTT homoterpene synthase
Systematic name: (3S,6E)-nerolidol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase
Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the plants Arabidopsis thaliana (thale cress) and Zea mays (maize). It forms this C11 homoterpene in response to herbivore attack. In vitro the enzyme also converts (6E,10E)-geranyllinalool to (3E,7E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene (see EC 1.14.14.58, trimethyltridecatetraene synthase).
References:
1.  Lee, S., Badieyan, S., Bevan, D.R., Herde, M., Gatz, C. and Tholl, D. Herbivore-induced and floral homoterpene volatiles are biosynthesized by a single P450 enzyme (CYP82G1) in Arabidopsis. Proc. Natl Acad. Sci. USA 107 (2010) 21205–21210. [PMID: 21088219]
2.  Richter, A., Schaff, C., Zhang, Z., Lipka, A.E., Tian, F., Kollner, T.G., Schnee, C., Preiss, S., Irmisch, S., Jander, G., Boland, W., Gershenzon, J., Buckler, E.S. and Degenhardt, J. Characterization of biosynthetic pathways for the production of the volatile homoterpenes DMNT and TMTT in Zea mays. Plant Cell 28 (2016) 2651–2665. [PMID: 27662898]
[EC 1.14.14.59 created 2018]
 
 
EC 1.14.14.60 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: ferruginol monooxygenase
Reaction: ferruginol + [reduced NADPH—hemoprotein reductase] + O2 = 11-hydroxyferruginol + [oxidized NADPH—hemoprotein reductase] + H2O
Glossary: ferruginol = abieta-8,11,13-trien-12-ol
Other name(s): CYP76AH24; CYP76AH3
Systematic name: ferruginol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (11-hydroxyferruginol forming)
Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the plants Salvia pomifera (apple sage) and Salvia miltiorrhiza (danshen). 11-Hydroxyferruginol is a precursor of carnosic acid, a potent antioxidant.
References:
1.  Ignea, C., Athanasakoglou, A., Ioannou, E., Georgantea, P., Trikka, F.A., Loupassaki, S., Roussis, V., Makris, A.M. and Kampranis, S.C. Carnosic acid biosynthesis elucidated by a synthetic biology platform. Proc. Natl Acad. Sci. USA 113 (2016) 3681–3686. [PMID: 26976595]
2.  Scheler, U., Brandt, W., Porzel, A., Rothe, K., Manzano, D., Bozic, D., Papaefthimiou, D., Balcke, G.U., Henning, A., Lohse, S., Marillonnet, S., Kanellis, A.K., Ferrer, A. and Tissier, A. Elucidation of the biosynthesis of carnosic acid and its reconstitution in yeast. Nat Commun 7:12942 (2016). [PMID: 27703160]
3.  Guo, J., Ma, X., Cai, Y., Ma, Y., Zhan, Z., Zhou, Y.J., Liu, W., Guan, M., Yang, J., Cui, G., Kang, L., Yang, L., Shen, Y., Tang, J., Lin, H., Ma, X., Jin, B., Liu, Z., Peters, R.J., Zhao, Z.K. and Huang, L. Cytochrome P450 promiscuity leads to a bifurcating biosynthetic pathway for tanshinones. New Phytol. 210 (2016) 525–534. [PMID: 26682704]
[EC 1.14.14.60 created 2018]
 
 
EC 1.14.14.61 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: carnosic acid synthase
Reaction: 11-hydroxyferruginol + 3 [reduced NADPH—hemoprotein reductase] + 3 O2 = carnosic acid + 3 [oxidized NADPH—hemoprotein reductase] + 4 H2O
Glossary: carnosic acid = 11,12-dihydroxyabieta-8,11,13-trien-20-oic acid
Other name(s): CYP76AK6; CYP76AK7; CYP76AK8
Systematic name: 11-hydroxyferruginol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase
Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the plants Salvia pomifera (apple sage), S. miltiorrhiza (red sage), S. fruticosa (Greek sage) and Rosmarinus officinalis (Rosemary).
References:
1.  Ignea, C., Athanasakoglou, A., Ioannou, E., Georgantea, P., Trikka, F.A., Loupassaki, S., Roussis, V., Makris, A.M. and Kampranis, S.C. Carnosic acid biosynthesis elucidated by a synthetic biology platform. Proc. Natl Acad. Sci. USA 113 (2016) 3681–3686. [PMID: 26976595]
2.  Scheler, U., Brandt, W., Porzel, A., Rothe, K., Manzano, D., Bozic, D., Papaefthimiou, D., Balcke, G.U., Henning, A., Lohse, S., Marillonnet, S., Kanellis, A.K., Ferrer, A. and Tissier, A. Elucidation of the biosynthesis of carnosic acid and its reconstitution in yeast. Nat Commun 7:12942 (2016). [PMID: 27703160]
[EC 1.14.14.61 created 2018]
 
 
EC 1.14.14.62 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: salviol synthase
Reaction: ferruginol + [reduced NADPH—hemoprotein reductase] + O2 = salviol + [oxidized NADPH—hemoprotein reductase] + H2O
Glossary: salviol = abieta-8,11,13-triene-2α,12-diol
Other name(s): CYP71BE52
Systematic name: ferruginol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (salviol forming)
Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the plant Salvia pomifera (apple sage).
References:
1.  Ignea, C., Athanasakoglou, A., Ioannou, E., Georgantea, P., Trikka, F.A., Loupassaki, S., Roussis, V., Makris, A.M. and Kampranis, S.C. Carnosic acid biosynthesis elucidated by a synthetic biology platform. Proc. Natl Acad. Sci. USA 113 (2016) 3681–3686. [PMID: 26976595]
[EC 1.14.14.62 created 2018]
 
 
EC 1.14.14.63 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: β-amyrin 16β-monooxygenase
Reaction: β-amyrin + [reduced NADPH—hemoprotein reductase] + O2 = maniladiol + [oxidized NADPH—hemoprotein reductase] + H2O
Glossary: cochalic acid = 3β,16β-dihydroxyolean-12-en-28-oic acid
maniladiol = 16β-hydroxy-β-amyrin = olean-12-ene-3β,16β-diol
Other name(s): CYP716A141
Systematic name: β-amyrin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (maniladiol forming)
Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the plant Platycodon grandiflorus (baloon flower). The enzyme is also able to oxidize oleanolic acid to cochalic acid.
References:
1.  Tamura, K., Teranishi, Y., Ueda, S., Suzuki, H., Kawano, N., Yoshimatsu, K., Saito, K., Kawahara, N., Muranaka, T. and Seki, H. Cytochrome P450 monooxygenase CYP716A141 is a unique β-amyrin C-16β oxidase Involved in triterpenoid saponin biosynthesis in Platycodon grandiflorus. Plant Cell Physiol 58 (2017) 874–884. [PMID: 28371833]
[EC 1.14.14.63 created 2018]
 
 
EC 1.14.14.64 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: β-amyrin 6β-monooxygenase
Reaction: β-amyrin + [reduced NADPH—hemoprotein reductase] + O2 = daturadiol + [oxidized NADPH—hemoprotein reductase] + H2O
Glossary: daturadiol = 6β-hydroxy-β-amyrin = olean-12-ene-3β,6β-diol
Other name(s): CYP716E26
Systematic name: β-amyrin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (daturadiol forming)
Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the plant Solanum lycopersicum (tomato).
References:
1.  Yasumoto, S., Seki, H., Shimizu, Y., Fukushima, E.O. and Muranaka, T. Functional characterization of CYP716 family P450 enzymes in triterpenoid biosynthesis in tomato. Front. Plant Sci. 8:21 (2017). [PMID: 28194155]
[EC 1.14.14.64 created 2018]
 
 
EC 1.14.14.65 – public review until 19 March 2018 [Last modified: 2018-02-19 16:55:30]
Accepted name: sugiol synthase
Reaction: ferruginol + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = sugiol + 2 [oxidized NADPH—hemoprotein reductase] + 3 H2O
Glossary: ferruginol = abieta-8,11,13-trien-12-ol
sugiol = 12-hydroxyabieta-8,11,13-trien-7-one
Other name(s): CYP76AH3
Systematic name: ferruginol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (sugiol forming)
Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the plant Salvia miltiorrhiza (danshen). The enzyme also oxidizes 11-hydroxyferruginol to 11-hydroxysugiol. It also oxidizes at C-12 of ferruginol (EC 1.14.14.60 ferruginol monooxygenase).
References:
1.  Guo, J., Ma, X., Cai, Y., Ma, Y., Zhan, Z., Zhou, Y.J., Liu, W., Guan, M., Yang, J., Cui, G., Kang, L., Yang, L., Shen, Y., Tang, J., Lin, H., Ma, X., Jin, B., Liu, Z., Peters, R.J., Zhao, Z.K. and Huang, L. Cytochrome P450 promiscuity leads to a bifurcating biosynthetic pathway for tanshinones. New Phytol. 210 (2016) 525–534. [PMID: 26682704]
[EC 1.14.14.65 created 2018]
 
 
EC 1.14.14.66 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: marmesin synthase
Reaction: demethylsuberosin + [reduced NADPH—hemoprotein reductase] + O2 = (+)-marmesin + [oxidized NADPH—hemoprotein reductase] + H2O
Glossary: demethylsuberosin = 7-hydroxy-6-prenyl-1-benzopyran-2-one
(+)-marmesin = (S)-2-(2-hydroxypropan-2-yl)-2,3-dihydro-7H-furo[3,2-g]chromen-7-one
Systematic name: demethylsuberosin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase
Comments: A P-450 monoxygenase involved in psoralen biosynthesis, see EC 1.14.13.102, psoralen synthase.
References:
1.  Hamerski, D. and Matern, U. Elicitor-induced biosynthesis of psoralens in Ammi majus L. suspension cultures. Microsomal conversion of demethylsuberosin into (+)marmesin and psoralen. Eur. J. Biochem. 171 (1988) 369–375. [PMID: 2828055]
[EC 1.14.14.66 created 2018]
 
 
EC 1.14.14.67 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: 11-hydroxysugiol 20-monooxygenase
Reaction: 11-hydroxysugiol + [reduced NADPH—hemoprotein reductase] + O2 = 11,20-dihydroxysugiol + [oxidized NADPH—hemoprotein reductase] + H2O
Glossary: ferruginol = abieta-8,11,13-trien-12-ol
sugiol = 12-hydroxyabieta-8,11,13-trien-7-one
Other name(s): CYP76AK1
Systematic name: 11-hydroxysugiol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (11,20-dihydroxysugiol forming)
Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the plant Salvia miltiorrhiza (danshen). The enzyme also oxidizes 11-hydroxyferruginol to 11,20-dihydroxyferruginol.
References:
1.  Guo, J., Ma, X., Cai, Y., Ma, Y., Zhan, Z., Zhou, Y.J., Liu, W., Guan, M., Yang, J., Cui, G., Kang, L., Yang, L., Shen, Y., Tang, J., Lin, H., Ma, X., Jin, B., Liu, Z., Peters, R.J., Zhao, Z.K. and Huang, L. Cytochrome P450 promiscuity leads to a bifurcating biosynthetic pathway for tanshinones. New Phytol. 210 (2016) 525–534. [PMID: 26682704]
[EC 1.14.14.67 created 2018]
 
 
EC 1.14.14.68 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: syn-pimaradiene 3-monooxygenase
Reaction: 9β-pimara-7,15-diene + [reduced NADPH—hemoprotein reductase] + O2 = 9β-pimara-7,15-diene-3β-ol + [oxidized NADPH—hemoprotein reductase] + H2O
Glossary: syn-pimara-7,15-diene = 9β-pimara-7,15-diene
Other name(s): CYP701A8
Systematic name: 9β-pimara7,15-diene,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (9β-pimara-7,15-diene-3β-ol forming)
Comments: A cytochrome P-450 (heme-thiolate) protein isolated from rice, Oryza sativa.
References:
1.  Kitaoka, N., Wu, Y., Xu, M. and Peters, R.J. Optimization of recombinant expression enables discovery of novel cytochrome P450 activity in rice diterpenoid biosynthesis. Appl. Microbiol. Biotechnol. 99 (2015) 7549–7558. [PMID: 25758958]
[EC 1.14.14.68 created 2018]
 
 
EC 1.14.14.69 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: ent-cassadiene hydroxylase
Reaction: ent-cassa-12,15-diene + 3 [reduced NADPH—hemoprotein reductase] + 3 O2 = ent-3β-hydroxycassa-12,15-dien-2-one + 3 [oxidized NADPH—hemoprotein reductase] + 4 H2O (overall reaction)
(1a) ent-cassa-12,15-diene + [reduced NADPH—hemoprotein reductase] + O2 = ent-cassa-12,15-dien-2β-ol + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) ent-cassa-12,15-dien-2β-ol + [reduced NADPH—hemoprotein reductase] + O2 = ent-cassa-12,15-dien-2-one + [oxidized NADPH—hemoprotein reductase] + 2 H2O
(1b′) ent-cassa-12,15-dien-2β-ol + [reduced NADPH—hemoprotein reductase] + O2 = ent-cassa-12,15-diene-2β,3β-diol + [oxidized NADPH—hemoprotein reductase] + H2O
(1c) ent-cassa-12,15-dien-2-one + [reduced NADPH—hemoprotein reductase] + O2 = ent-3β-hydroxycassa-12,15-dien-2-one + [oxidized NADPH—hemoprotein reductase] + H2O
(1c′) ent-cassa-12,15-diene-2β,3β-diol + [reduced NADPH—hemoprotein reductase] + O2 = ent-3β-hydroxycassa-12,15-dien-2-one + [oxidized NADPH—hemoprotein reductase] + 2 H2O
Other name(s): CYP71Z7
Systematic name: ent-cassa-12,15-diene,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (ent-3β-hydroxycassa-12,15-dien-2-one forming)
Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the plant Oryza sativa (rice) that is involved in phytocassanes biosynthesis. Depending on the order of activities, the enzyme may form either ent-cassa-12,15-dien-2-one or ent-cassa-12,15-diene-2β,3β-diol as an intermediate.
References:
1.  Kitaoka, N., Wu, Y., Xu, M. and Peters, R.J. Optimization of recombinant expression enables discovery of novel cytochrome P450 activity in rice diterpenoid biosynthesis. Appl. Microbiol. Biotechnol. 99 (2015) 7549–7558. [PMID: 25758958]
[EC 1.14.14.69 created 2018]
 
 
EC 1.14.15.25 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: p-cymene methyl-monooxygenase
Reaction: p-cymene + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ = 4-isopropylbenzyl alcohol + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Glossary: p-cymene = 4-methyl-1-(propan-2-yl)benzene
Other name(s): cymAa (gene name); cymA (gene name); p-cymene methyl hydroxylase
Systematic name: p-cymene,ferredoxin:oxygen oxidoreductase (methyl-hydroxylating)
Comments: The enzyme, characterized from several Pseudomonas strains, initiates p-cymene catabolism through hydroxylation of the methyl group. The enzyme has a distinct preference for substrates containing at least an alkyl or heteroatom substituent at the para-position of toluene. The electrons are provided by a reductase (EC 1.18.1.3, ferredoxin—NAD+ reductase) that transfers electrons from NADH via FAD and an [2Fe-2S] cluster. In Pseudomonas chlororaphis the presence of a third component of unknown function greatly increases the activity. cf. EC 1.14.15.26, toluene methyl-monooxygenase.
References:
1.  Eaton, R.W. p-Cymene catabolic pathway in Pseudomonas putida F1: cloning and characterization of DNA encoding conversion of p-cymene to p-cumate. J. Bacteriol. 179 (1997) 3171–3180. [PMID: 9150211]
2.  Dutta, T.K. and Gunsalus, I.C. Reductase gene sequences and protein structures: p-cymene methyl hydroxylase. Biochem. Biophys. Res. Commun. 233 (1997) 502–506. [PMID: 9144566]
3.  Nishio, T., Patel, A., Wang, Y. and Lau, P.C. Biotransformations catalyzed by cloned p-cymene monooxygenase from Pseudomonas putida F1. Appl. Microbiol. Biotechnol. 55 (2001) 321–325. [PMID: 11341314]
4.  Dutta, T.K., Chakraborty, J., Roy, M., Ghosal, D., Khara, P. and Gunsalus, I.C. Cloning and characterization of a p-cymene monooxygenase from Pseudomonas chlororaphis subsp. aureofaciens. Res. Microbiol. 161 (2010) 876–882. [PMID: 21035544]
[EC 1.14.15.25 created 2018]
 
 
EC 1.14.15.26 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: toluene methyl-monooxygenase
Reaction: (1) toluene + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ = benzyl alcohol + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(2) p-xylene + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ = 4-methylbenzyl alcohol + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(3) m-xylene + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ = 3-methylbenzyl alcohol + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Glossary: toluene = methylbenzene
p-xylene = 1,4-dimethylbenzene
m-xylene = 1,3-dimethylbenzene
Other name(s): xylM (gene names); ntnM (gene names)
Systematic name: methylbenzene,ferredoxin:oxygen oxidoreductase (methyl-hydroxylating)
Comments: The enzyme, characterized from several Pseudomonas strains, catalyses the first step in the degradation of toluenes and xylenes. It has a broad substrate specificity and is also active with substituted compounds, such as chlorotoluenes. The electrons are provided by a reductase (EC 1.18.1.3, ferredoxin—NAD+ reductase) that transfers electrons from NADH via FAD and an [2Fe-2S] cluster. The enzyme can also act on its products, producing gem-diols that spontaneously dehydrate to form aldehydes.
References:
1.  Suzuki, M., Hayakawa, T., Shaw, J.P., Rekik, M. and Harayama, S. Primary structure of xylene monooxygenase: similarities to and differences from the alkane hydroxylation system. J. Bacteriol. 173 (1991) 1690–1695. [PMID: 1999388]
2.  Shaw, J.P. and Harayama, S. Purification and characterisation of the NADH:acceptor reductase component of xylene monooxygenase encoded by the TOL plasmid pWW0 of Pseudomonas putida mt-2. Eur. J. Biochem. 209 (1992) 51–61. [PMID: 1327782]
3.  Brinkmann, U. and Reineke, W. Degradation of chlorotoluenes by in vivo constructed hybrid strains: problems of enzyme specificity, induction and prevention of meta-pathway. FEMS Microbiol. Lett. 75 (1992) 81–87. [PMID: 1526468]
4.  James, K.D. and Williams, P.A. ntn genes determining the early steps in the divergent catabolism of 4-nitrotoluene and toluene in Pseudomonas sp. strain TW3. J. Bacteriol. 180 (1998) 2043–2049. [PMID: 9555884]
[EC 1.14.15.26 created 2018]
 
 
EC 1.14.19.53 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: all-trans-retinol 3,4-desaturase
Reaction: all-trans-retinol + 2 reduced adrenodoxin + 2 H+ + O2 = all-trans-3,4-didehydroretinol + 2 oxidized adrenodoxin + 2 H2O
Other name(s): CYP27C1 (gene name)
Systematic name: all-trans-retinol,reduced adrenodoxin:oxygen 3,4-oxidoreductase
Comments: A cytochrome P-450 (heme thiolate) enzyme found in vertebrates. The enzyme is also active with retinal and retinoic acid.
References:
1.  Enright, J.M., Toomey, M.B., Sato, S.Y., Temple, S.E., Allen, J.R., Fujiwara, R., Kramlinger, V.M., Nagy, L.D., Johnson, K.M., Xiao, Y., How, M.J., Johnson, S.L., Roberts, N.W., Kefalov, V.J., Guengerich, F.P. and Corbo, J.C. Cyp27c1 red-shifts the spectral sensitivity of photoreceptors by converting vitamin A1 into A2. Curr. Biol. 25 (2015) 3048–3057. [PMID: 26549260]
2.  Kramlinger, V.M., Nagy, L.D., Fujiwara, R., Johnson, K.M., Phan, T.T., Xiao, Y., Enright, J.M., Toomey, M.B., Corbo, J.C. and Guengerich, F.P. Human cytochrome P450 27C1 catalyzes 3,4-desaturation of retinoids. FEBS Lett. 590 (2016) 1304–1312. [PMID: 27059013]
[EC 1.14.19.53 created 2018]
 
 
EC 1.14.20.2 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Transferred entry: 2,4-dihydroxy-1,4-benzoxazin-3-one-glucoside dioxygenase. Now EC 1.14.11.59, 2,4-dihydroxy-1,4-benzoxazin-3-one-glucoside dioxygenase
[EC 1.14.20.2 created 2012, deleted 2018]
 
 
*EC 2.1.1.294 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: 3-O-phospho-polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol 3-phospho-methyltransferase
Reaction: S-adenosyl-L-methionine + 3-O-phospho-α-D-Man-(1→2)-α-D-Man-(1→2)-[α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)]n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol = S-adenosyl-L-homocysteine + 3-O-methylphospho-α-D-Man-(1→2)-α-D-Man-(1→2)-[α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)]n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
Other name(s): WbdD; S-adenosyl-L-methionine:3-O-phospho-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Man-(1→3)]n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-α-diphospho-ditrans,octacis-undecaprenol 3-phospho-methyltransferase
Systematic name: S-adenosyl-L-methionine:3-O-phospho-α-D-Man-(1→2)-α-D-Man-(1→2)-[α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)]n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol 3-phospho-methyltransferase
Comments: The enzyme is involved in the biosynthesis of the polymannose O-polysaccharide in the outer leaflet of the membrane of Escherichia coli serotype O9a. O-Polysaccharide structures vary extensively because of differences in the number and type of sugars in the repeat unit. The dual kinase/methylase WbdD also catalyses the preceding phosphorylation of α-D-Man-(1→2)-α-D-Man-(1→2)-[α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)]n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol (cf. EC 2.7.1.181, polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol kinase).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, MetaCyc
References:
1.  Clarke, B.R., Cuthbertson, L. and Whitfield, C. Nonreducing terminal modifications determine the chain length of polymannose O antigens of Escherichia coli and couple chain termination to polymer export via an ATP-binding cassette transporter. J. Biol. Chem. 279 (2004) 35709–35718. [PMID: 15184370]
2.  Clarke, B.R., Greenfield, L.K., Bouwman, C. and Whitfield, C. Coordination of polymerization, chain termination, and export in assembly of the Escherichia coli lipopolysaccharide O9a antigen in an ATP-binding cassette transporter-dependent pathway. J. Biol. Chem. 284 (2009) 30662–30672. [PMID: 19734145]
3.  Clarke, B.R., Richards, M.R., Greenfield, L.K., Hou, D., Lowary, T.L. and Whitfield, C. In vitro reconstruction of the chain termination reaction in biosynthesis of the Escherichia coli O9a O-polysaccharide: the chain-length regulator, WbdD, catalyzes the addition of methyl phosphate to the non-reducing terminus of the growing glycan. J. Biol. Chem. 286 (2011) 41391–41401. [PMID: 21990359]
4.  Liston, S.D., Clarke, B.R., Greenfield, L.K., Richards, M.R., Lowary, T.L. and Whitfield, C. Domain interactions control complex formation and polymerase specificity in the biosynthesis of the Escherichia coli O9a antigen. J. Biol. Chem. 290 (2015) 1075–1085. [PMID: 25422321]
[EC 2.1.1.294 created 2014, modified 2018]
 
 
EC 2.1.1.346 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: U6 snRNA m6A methyltransferase
Reaction: S-adenosyl-L-methionine + adenine in U6 snRNA = S-adenosyl-L-homocysteine + N6-methyladenine in U6 snRNA
Other name(s): METTL16 (gene name)
Systematic name: S-adenosyl-L-methionine:adenine in U6 snRNA methyltransferase
Comments: This enzyme, found in vertebrates, methylates a specific adenine in a hairpin structure of snRNA. The effects of the binding of the methyltransferase to its substrate is important for the regulation of the activity of an isoform of EC 2.5.1.6, methionine adenosyltransferase, that produces S-adenosyl-L-methionine [1,2]. The enzyme also binds (and maybe methylates) the lncRNAs XIST and MALAT1 as well as a number of pre-mRNAs at specific positions often found in the intronic regions [2].
References:
1.  Pendleton, K.E., Chen, B., Liu, K., Hunter, O.V., Xie, Y., Tu, B.P. and Conrad, N.K. The U6 snRNA m6A methyltransferase METTL16 regulates SAM synthetase intron retention. Cell 169 (2017) 824–835.e14. [PMID: 28525753]
2.  Warda, A.S., Kretschmer, J., Hackert, P., Lenz, C., Urlaub, H., Hobartner, C., Sloan, K.E. and Bohnsack, M.T. Human METTL16 is a N6-methyladenosine (m6A) methyltransferase that targets pre-mRNAs and various non-coding RNAs. EMBO Rep. 18 (2017) 2004–2014. [PMID: 29051200]
[EC 2.1.1.346 created 2018]
 
 
EC 2.1.1.347 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: (+)-O-methylkolavelool synthase
Reaction: S-adenosyl-L-methionine + (+)-kolavelool = S-adenosyl-L-homocysteine + (+)-O-methylkolavelool
Other name(s): Haur_2147 (locus name)
Systematic name: S-adenosyl-L-methionine:(+)-kolavelool O-methyltransferase
Comments: Isolated from the bacterium Herpetosiphon aurantiacus.
References:
1.  Nakano, C., Oshima, M., Kurashima, N. and Hoshino, T. Identification of a new diterpene biosynthetic gene cluster that produces O-methylkolavelool in Herpetosiphon aurantiacus. Chembiochem 16 (2015) 772–781. [PMID: 25694050]
[EC 2.1.1.347 created 2018]
 
 
EC 2.1.5 Methylenetransferases
 
EC 2.1.5.1 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: sesamin methylene transferase
Reaction: (1) (+)-sesamin + tetrahydrofolate = (+)-demethylpiperitol + 5,10-methylenetetrahydrofolate
(2) (+)-demethylpiperitol + tetrahydrofolate = (+)-didemethylpinoresinol + 5,10-methylenetetrahydrofolate
Glossary: (+)-sesamin = 5,5′-[(1S,3aR,4S,6aR)-tetrahydro-1H,3H-furo[3,4-c]furan-1,4-diyl]bis(1,3-benzodioxole)
(+)-demethylpiperitol = 4-[(1S,3aR,4S,6aR)-4-(1,3-benzodioxol-5-yl)tetrahydro-1H,3H-furo[3,4-c]furan-1-yl]benzene-1,2-diol
(+)-didemethylpinoresinol = 4-[(1S,3aR,4S,6aR)-4-(3,4-dihydroxyphenyl)tetrahydro-1H,3H-furo[3,4-c]furan-1-yl]benzene-1,2-diol
Other name(s): sesA (gene name)
Systematic name: (+)-sesamin:tetrahydrofolate N-methylenetransferase
Comments: This enzyme was characterized from the bacterium Sinomonas sp. No.22. It catalyses a cleavage of a methylene bridge, followed by the transfer of the methylene group to tetrahydrofolate. The enzyme is also active with (+)-episesamin, (–)-asarinin, (+)-sesaminol, (+)-sesamolin, and piperine.
References:
1.  Kumano, T., Fujiki, E., Hashimoto, Y. and Kobayashi, M. Discovery of a sesamin-metabolizing microorganism and a new enzyme. Proc. Natl. Acad. Sci. USA 113 (2016) 9087–9092. [PMID: 27444012]
[EC 2.1.5.1 created 2018]
 
 
EC 2.3.1.96 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Deleted entry: glycoprotein N-palmitoyltransferase
[EC 2.3.1.96 created 1989, deleted 2018]
 
 
EC 2.3.1.128 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Transferred entry: ribosomal-protein-alanine N-acetyltransferase, now classified as EC 2.3.1.266, [ribosomal protein S18]-alanine N-acetyltransferase, and EC 2.3.1.267, [ribosomal protein S5]-alanine N-acetyltransferase.
[EC 2.3.1.128 created 1990, deleted 2018]
 
 
EC 2.3.1.266 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: [ribosomal protein S18]-alanine N-acetyltransferase
Reaction: acetyl-CoA + an N-terminal L-alanyl-[S18 protein of 30S ribosome] = CoA + an N-terminal N-acetyl-L-alanyl-[S18 protein of 30S ribosome]
Other name(s): rimI (gene name)
Systematic name: acetyl-CoA:[S18 protein of 30S ribosome]-L-alanine N-acetyltransferase
Comments: The enzyme, characterized from the bacterium Escherichia coli, is specific for protein S18, a component of the 30S ribosomal subunit. cf. EC 2.3.1.267, [ribosomal protein S5]-alanine N-acetyltransferase.
References:
1.  Isono, K. and Isono, S. Ribosomal protein modification in Escherichia coli. II. Studies of a mutant lacking the N-terminal acetylation of protein S18. Mol. Gen. Genet. 177 (1980) 645–651. [PMID: 6991870]
2.  Yoshikawa, A., Isono, S., Sheback, A. and Isono, K. Cloning and nucleotide sequencing of the genes rimI and rimJ which encode enzymes acetylating ribosomal proteins S18 and S5 of Escherichia coli K12. Mol. Gen. Genet. 209 (1987) 481–488. [PMID: 2828880]
[EC 2.3.1.266 created 1990 as EC 2.3.1.128, part transferred 2018 to EC 2.3.1.266]
 
 
EC 2.3.1.267 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: [ribosomal protein S5]-alanine N-acetyltransferase
Reaction: acetyl-CoA + an N-terminal L-alanyl-[S5 protein of 30S ribosome] = CoA + an N-terminal N-acetyl-L-alanyl-[S5 protein of 30S ribosome]
Other name(s): rimJ (gene name)
Systematic name: acetyl-CoA:[S5 protein of 30S ribosome]-L-alanine N-acetyltransferase
Comments: The enzyme, characterized from the bacterium Escherichia coli, is specific for protein S5, a component of the 30S ribosomal subunit. It also plays a role in maturation of the 30S ribosomal subunit. cf. EC 2.3.1.266, [ribosomal protein S18]-alanine N-acetyltransferase.
References:
1.  Yoshikawa, A., Isono, S., Sheback, A. and Isono, K. Cloning and nucleotide sequencing of the genes rimI and rimJ which encode enzymes acetylating ribosomal proteins S18 and S5 of Escherichia coli K12. Mol. Gen. Genet. 209 (1987) 481–488. [PMID: 2828880]
2.  Roy-Chaudhuri, B., Kirthi, N., Kelley, T. and Culver, G.M. Suppression of a cold-sensitive mutation in ribosomal protein S5 reveals a role for RimJ in ribosome biogenesis. Mol. Microbiol. 68 (2008) 1547–1559. [PMID: 18466225]
3.  Roy-Chaudhuri, B., Kirthi, N. and Culver, G.M. Appropriate maturation and folding of 16S rRNA during 30S subunit biogenesis are critical for translational fidelity. Proc. Natl. Acad. Sci. USA 107 (2010) 4567–4572. [PMID: 20176963]
[EC 2.3.1.267 created 1990 as EC 2.3.1.128, part transferred 2018 to EC 2.3.1.267]
 
 
EC 2.3.1.268 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: ethanol O-acetyltransferase
Reaction: ethanol + acetyl-CoA = ethyl acetate + CoA
Other name(s): eat1 (gene name); ethanol acetyltransferase
Systematic name: acetyl-CoA:ethanol O-acetyltransferase
Comments: The enzyme, characterized from the yeast Wickerhamomyces anomalus, is responsible for most ethyl acetate synthesis in known ethyl acetate-producing yeasts. It is only distantly related to enzymes classified as EC 2.3.1.84, alcohol O-acetyltransferase. The enzyme also possesses thioesterase and esterase activities, which are inhibited by high ethanol concentrations.
References:
1.  Kruis, A.J., Levisson, M., Mars, A.E., van der Ploeg, M., Garces Daza, F., Ellena, V., Kengen, S.WM., van der Oost, J. and Weusthuis, R.A. Ethyl acetate production by the elusive alcohol acetyltransferase from yeast. Metab. Eng. 41 (2017) 92–101. [PMID: 28356220]
[EC 2.3.1.268 created 2018]
 
 
EC 2.3.3.20 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: acyl-CoA:acyl-CoA alkyltransferase
Reaction: 2 an acyl-CoA + H2O = a (2R)-2-alkyl-3-oxoalkanoate + 2 CoA
Other name(s): oleA (gene name)
Systematic name: acyl-CoA:acyl-CoA alkyltransferase [(2R)-2-alkyl-3-oxoalkanoate-forming]
Comments: The enzyme, found in certain bacterial species, catalyses a head-to-head non-decarboxylative Claisen condensation of two acyl-CoA molecules, resulting in formation of a 2-alkyl-3-oxoalkanoic acid. It is part of a pathway for the production of olefins.
References:
1.  Sukovich, D.J., Seffernick, J.L., Richman, J.E., Hunt, K.A., Gralnick, J.A. and Wackett, L.P. Structure, function, and insights into the biosynthesis of a head-to-head hydrocarbon in Shewanella oneidensis strain MR-1. Appl. Environ. Microbiol. 76 (2010) 3842–3849. [PMID: 20418444]
2.  Frias, J.A., Richman, J.E., Erickson, J.S. and Wackett, L.P. Purification and characterization of OleA from Xanthomonas campestris and demonstration of a non-decarboxylative Claisen condensation reaction. J. Biol. Chem. 286 (2011) 10930–10938. [PMID: 21266575]
3.  Goblirsch, B.R., Frias, J.A., Wackett, L.P. and Wilmot, C.M. Crystal structures of Xanthomonas campestris OleA reveal features that promote head-to-head condensation of two long-chain fatty acids. Biochemistry 51 (2012) 4138–4146. [PMID: 22524624]
4.  Goblirsch, B.R., Jensen, M.R., Mohamed, F.A., Wackett, L.P. and Wilmot, C.M. Substrate trapping in crystals of the thiolase OleA identifies three channels that enable long chain olefin biosynthesis. J. Biol. Chem. 291 (2016) 26698–26706. [PMID: 27815501]
[EC 2.3.3.20 created 2018]
 
 
EC 2.4.1.351 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: rhamnogalacturonan I rhamnosyltransferase
Reaction: UDP-β-L-rhamnose + α-D-galacturonosyl-[(1→2)-α-L-rhamnosyl-(1→4)-α-D-galacturonosyl]n = UDP + [(1→2)-α-L-rhamnosyl-(1→4)-α-D-galacturonosyl]n+1
Other name(s): RRT; RG I rhamnosyltransferase
Systematic name: UDP-β-L-rhamnose:rhamnogalacturonan I 4-rhamnosyltransferase (configuration-inverting)
Comments: The enzyme, characterized from Vigna angularis (azuki beans), participates in the biosynthesis of rhamnogalacturonan type I. It does not require any metal ions, and prefers substrates with a degree of polymerization larger than 7.
References:
1.  Uehara, Y., Tamura, S., Maki, Y., Yagyu, K., Mizoguchi, T., Tamiaki, H., Imai, T., Ishii, T., Ohashi, T., Fujiyama, K. and Ishimizu, T. Biochemical characterization of rhamnosyltransferase involved in biosynthesis of pectic rhamnogalacturonan I in plant cell wall. Biochem. Biophys. Res. Commun. 486 (2017) 130–136. [PMID: 28283389]
[EC 2.4.1.351 created 2018]
 
 
EC 2.4.1.352 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: glucosylglycerate phosphorylase
Reaction: 2-O-(α-D-glucopyranosyl)-D-glycerate + phosphate = α-D-glucopyranose 1-phosphate + D-glycerate
Systematic name: 2-O-(α-D-glucopyranosyl)-D-glycerate:phosphate α-D-glucosyltransferase (configuration-retaining)
Comments: The enzyme has been characterized from the bacterium Meiothermus silvanus.
References:
1.  Franceus, J., Pinel, D. and Desmet, T. Glucosylglycerate phosphorylase, an enzyme with novel specificity involved in compatible solute metabolism. Appl. Environ. Microbiol. 83 (2017) . [PMID: 28754708]
[EC 2.4.1.352 created 2018]
 
 
*EC 2.5.1.98 – public review until 19 March 2018 [Last modified: 2018-02-19 18:06:10]
Accepted name: Rhizobium leguminosarum exopolysaccharide glucosyl ketal-pyruvate-transferase
Reaction: phosphoenolpyruvate + [β-D-GlcA-(1→4)-2-O-Ac-β-D-GlcA-(1→4)-β-D-Glc-(1→4)-[3-O-(CH3CH(OH)CH2C(O))-4,6-CH3(COO-)C-β-D-Gal-(1→4)-β-D-Glc-(1→4)-β-D-Glc-(1→4)-β-D-Glc-(1→6)]-2(or 3)-O-Ac-α-D-Glc-(1→6)]n = [β-D-GlcA-(1→4)-2-O-Ac-β-D-GlcA-(1→4)-β-D-Glc-(1→4)-[3-O-(CH3CH(OH)CH2C(O))-4,6-CH3(COO-)C-β-D-Gal-(1→3)-4,6-CH3(COO-)C-β-D-Glc-(1→4)-β-D-Glc-(1→4)-β-D-Glc-(1→6)]-2(or 3)-O-Ac-α-D-Glc-(1→6)]n + phosphate
Other name(s): PssM; phosphoenolpyruvate:[D-GlcA-β-(1→4)-2-O-Ac-D-GlcA-β-(1→4)-D-Glc-β-(1→4)-[3-O-CH3-CH2CH(OH)C(O)-D-Gal-β-(1→4)-D-Glc-β-(1→4)-D-Glc-β-(1→4)-D-Glc-β-(1→6)]-2(or 3)-O-Ac-D-Glc-α-(1→6)]n 4,6-O-(1-carboxyethan-1,1-diyl)transferase
Systematic name: phosphoenolpyruvate:[β-D-GlcA-(1→4)-2-O-Ac-β-D-GlcA-(1→4)-β-D-Glc-(1→4)-[3-O-CH3-CH2CH(OH)C(O)-4,6-CH3(COO-)C-β-D-Gal-(1→4)-β-D-Glc-(1→4)-β-D-Glc-(1→4)-β-D-Glc-(1→6)]-2(or 3)-O-Ac-α-D-Glc-(1→6)]n 4,6-O-(1-carboxyethan-1,1-diyl)transferase
Comments: The enzyme is responsible for pyruvylation of the subterminal glucose in the acidic octasaccharide repeating unit of the exopolysaccharide of Rhizobium leguminosarum (bv. viciae strain VF39) which is necessary to establish nitrogen-fixing symbiosis with Pisum sativum, Vicia faba, and Vicia sativa.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, MetaCyc
References:
1.  Ivashina, T.V., Fedorova, E.E., Ashina, N.P., Kalinchuk, N.A., Druzhinina, T.N., Shashkov, A.S., Shibaev, V.N. and Ksenzenko, V.N. Mutation in the pssM gene encoding ketal pyruvate transferase leads to disruption of Rhizobium leguminosarum bv. viciaePisum sativum symbiosis. J. Appl. Microbiol. 109 (2010) 731–742. [PMID: 20233262]
[EC 2.5.1.98 created 2012, modified 2018]
 
 
EC 2.5.1.99 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Deleted entry:  all-trans-phytoene synthase. The activity was an artifact caused by photoisomerization of the product of EC 2.5.1.32, 15-cis-phytoene synthase.
[EC 2.5.1.99 created 2012, deleted 2018]
 
 
EC 2.6.1.114 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: 8-demethyl-8-aminoriboflavin-5′-phosphate synthase
Reaction: L-glutamate + FMN + O2 + H2O + 3 acceptor = 2-oxoglutarate + 8-amino-8-demethylriboflavin 5′-phosphate + CO2 + 3 reduced acceptor (overall reaction)
(1a) FMN + O2 = 8-demethyl-8-formylriboflavin 5′-phosphate + H2O
(1b) 8-demethyl-8-formylriboflavin 5′-phosphate + H2O + acceptor = 8-carboxy-8-demethylriboflavin 5′-phosphate + reduced acceptor
(1c) L-glutamate + 8-carboxy-8-demethylriboflavin 5′-phosphate + H2O + 2 acceptor = 2-oxoglutarate + 8-amino-8-demethylriboflavin 5′-phosphate + CO2 + 2 reduced acceptor
Glossary: roseoflavin = 8-demethyl-8-(dimethylamino)riboflavin
Other name(s): rosB (gene name)
Systematic name: L-glutamate:FMN aminotransferase (oxidizing, decarboxylating)
Comments: The enzyme, characterized from the bacterium Streptomyces davawensis, has the activities of an oxidoreductase, a decarboxylase, and an aminotransferase. Its combined actions result in the replacement of a methyl substituent of one of the aromatic rings of FMN by an amino group, a step in the biosynthetic pathway of roseoflavin. The reaction requires thiamine for completion.
References:
1.  Schwarz, J., Konjik, V., Jankowitsch, F., Sandhoff, R. and Mack, M. Identification of the key enzyme of roseoflavin biosynthesis. Angew Chem Int Ed Engl 55 (2016) 6103–6106. [PMID: 27062037]
2.  Jhulki, I., Chanani, P.K., Abdelwahed, S.H. and Begley, T.P. A remarkable oxidative cascade that replaces the riboflavin C8 methyl with an amino group during roseoflavin biosynthesis. J. Am. Chem. Soc. 138 (2016) 8324–8327. [PMID: 27331868]
3.  Konjik, V., Brunle, S., Demmer, U., Vanselow, A., Sandhoff, R., Ermler, U. and Mack, M. The crystal structure of RosB: insights into the reaction mechanism of the first member of a family of flavodoxin-like enzymes. Angew Chem Int Ed Engl 56 (2017) 1146–1151. [PMID: 27981706]
[EC 2.6.1.114 created 2018]
 
 
EC 2.7.9.6 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: rifampicin phosphotransferase
Reaction: ATP + rifampicin + H2O = AMP + 21-phosphorifampicin + phosphate
Glossary: rifampicin = rifampin = 3-[(4-methylpiperazin-1-yl)iminomethyl]rifamycin
Other name(s): rifampin phosphotransferase; RPH
Systematic name: ATP:rifampicin, water 21-O-phosphotransferase
Comments: The enzyme, characterized from a diverse collection of Gram-positive bacteria, inactivates the antibiotic rifampicin by phosphorylating it at position 21. The enzyme comprises three domains: two substrate-binding domains (ATP-grasp and rifampicin-binding domains) and a smaller phosphate-carrying L-histidine swivel domain that transits between the spatially distinct substrate-binding sites during catalysis.
References:
1.  Spanogiannopoulos, P., Waglechner, N., Koteva, K. and Wright, G.D. A rifamycin inactivating phosphotransferase family shared by environmental and pathogenic bacteria. Proc. Natl Acad. Sci. USA 111 (2014) 7102–7107. [PMID: 24778229]
2.  Stogios, P.J., Cox, G., Spanogiannopoulos, P., Pillon, M.C., Waglechner, N., Skarina, T., Koteva, K., Guarne, A., Savchenko, A. and Wright, G.D. Rifampin phosphotransferase is an unusual antibiotic resistance kinase. Nat Commun 7:11343 (2016). [PMID: 27103605]
[EC 2.7.9.6 created 2018]
 
 
*EC 2.8.1.2 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: 3-mercaptopyruvate sulfurtransferase
Reaction: 3-mercaptopyruvate + reduced thioredoxin = pyruvate + hydrogen sulfide + oxidized thioredoxin (overall reaction)
(1a) 3-mercaptopyruvate + [3-mercaptopyruvate sulfurtransferase]-L-cysteine = pyruvate + [3-mercaptopyruvate sulfurtransferase]-S-sulfanyl-L-cysteine
(1b) [3-mercaptopyruvate sulfurtransferase]-S-sulfanyl-L-cysteine + reduced thioredoxin = hydrogen sulfide + [3-mercaptopyruvate sulfurtransferase]-L-cysteine + oxidized thioredoxin
Glossary: mercaptopyruvate = 2-oxo-3-sulfanylpropanoate
Other name(s): β-mercaptopyruvate sulfurtransferase; TUM1 (gene name); MPST (gene name); 3-mercaptopyruvate:cyanide sulfurtransferase
Systematic name: 3-mercaptopyruvate:sulfide sulfurtransferase
Comments: The enzyme catalyses a transsulfuration reaction from 3-mercaptopyruvate to an internal cysteine residue. In the presence of a dithiol such as reduced thioredoxin or dihydrolipoate, the sulfanyl sulfur is released as hydrogen sulfide. The enzyme participates in a sulfur relay process that leads to the 2-thiolation of some tRNAs and to protein urmylation by transferring sulfur between the NFS1 cysteine desulfurase (EC 2.8.1.7) and the MOCS3 sulfurtransferase (EC 2.8.1.11).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, MetaCyc, PDB, CAS registry number: 9026-05-5
References:
1.  Fiedler, H. and Wood, J.L. Specificity studies on the β-mercaptopyruvate-cyanide transsulfuration system. J. Biol. Chem. 222 (1956) 387–397. [PMID: 13367011]
2.  Sörbo, B.H. Enzymic transfer of sulfur from mercaptopyruvate to sulfite or sulfinates. Biochem. Biophys. Acta 24 (1957) 324–329. [PMID: 13436433]
3.  Hylin, J.W. and Wood, J.L. Enzymatic formation of polysulfides from mercaptopyruvate. J. Biol. Chem. 234 (1959) 2141–2144. [PMID: 13673028]
4.  van den Hamer, C.J.A., Morell, A.G. and Scheinberg, H.I. A study of the copper content of β-mercaptopyruvate trans-sulfurase. J. Biol. Chem. 242 (1967) 2514–2516. [PMID: 6026243]
5.  Vachek, H. and Wood, J.L. Purification and properties of mercaptopyruvate sulfur transferase of Escherichia coli. Biochim. Biophys. Acta 258 (1972) 133–146. [PMID: 4550801]
6.  Nagahara, N. and Katayama, A. Post-translational regulation of mercaptopyruvate sulfurtransferase via a low redox potential cysteine-sulfenate in the maintenance of redox homeostasis. J. Biol. Chem. 280 (2005) 34569–34576. [PMID: 16107337]
7.  Shibuya, N., Tanaka, M., Yoshida, M., Ogasawara, Y., Togawa, T., Ishii, K. and Kimura, H. 3-Mercaptopyruvate sulfurtransferase produces hydrogen sulfide and bound sulfane sulfur in the brain. Antioxid Redox Signal 11 (2009) 703–714. [PMID: 18855522]
8.  Mikami, Y., Shibuya, N., Kimura, Y., Nagahara, N., Ogasawara, Y. and Kimura, H. Thioredoxin and dihydrolipoic acid are required for 3-mercaptopyruvate sulfurtransferase to produce hydrogen sulfide. Biochem. J. 439 (2011) 479–485. [PMID: 21732914]
[EC 2.8.1.2 created 1961, modified 2018]
 
 
EC 3.1.1.103 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: teichoic acid D-alanine hydrolase
Reaction: [(4-D-Ala)-(2-GlcNAc)-Rib-ol-P]n-[Gro-P]m-ManNAc-GlcNAc-PP-peptidoglycan + n H2O = [(2-GlcNAc)-Rib-ol-P]n-[Gro-P]m-ManNAc-GlcNAc-PP-peptidoglycan + n D-alanine
Glossary: Rib-ol = ribitol
Other name(s): fmtA (gene name)
Systematic name: teichoic acid D-alanylhydrolase
Comments: The enzyme, characterized from the bacterium Staphylococcus aureus, removes D-alanine groups from the teichoic acid produced by this organism, thus modulating the electrical charge of the bacterial surface. The activity greatly increases methicillin resistance in MRSA strains.
References:
1.  Komatsuzawa, H., Sugai, M., Ohta, K., Fujiwara, T., Nakashima, S., Suzuki, J., Lee, C.Y. and Suginaka, H. Cloning and characterization of the fmt gene which affects the methicillin resistance level and autolysis in the presence of triton X-100 in methicillin-resistant Staphylococcus aureus. Antimicrob. Agents Chemother. 41 (1997) 2355–2361. [PMID: 9371333]
2.  Qamar, A. and Golemi-Kotra, D. Dual roles of FmtA in Staphylococcus aureus cell wall biosynthesis and autolysis. Antimicrob. Agents Chemother. 56 (2012) 3797–3805. [PMID: 22564846]
3.  Rahman, M.M., Hunter, H.N., Prova, S., Verma, V., Qamar, A. and Golemi-Kotra, D. The Staphylococcus aureus methicillin resistance factor FmtA is a D-amino esterase that acts on teichoic acids. MBio 7 (2016) e02070. [PMID: 26861022]
[EC 3.1.1.103 created 2018]
 
 
EC 3.2.2.31 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: adenine glycosylase
Reaction: Hydrolyses free adenine bases from 7,8-dihydro-8-oxoguanine:adenine mismatched double-stranded DNA, leaving an apurinic site.
Other name(s): mutY (gene name); A/G-specific adenine glycosylase
Systematic name: adenine-DNA deoxyribohydrolase (adenine-releasing)
Comments: The enzyme serves as a mismatch repair enzyme that works to correct 7,8-dihydro-8-oxoguanine:adenine mispairs that arise in DNA when error-prone synthesis occurs past 7,8-dihydro-8-oxoguanine (GO) lesions in DNA. The enzyme excises the adenine of the mispair, producing an apurinic site sensitive to AP endonuclease activity. After removing the undamaged adenine the enzyme remains bound to the site to prevent EC 3.2.2.23 (MutM) from removing the GO lesion, which could lead to a double strand break. In vitro the enzyme is also active with adenine:guanine, adenine:cytosine, and adenine:7,8-dihydro-8-oxoadenine (AO) mispairs, removing the adenine in all cases.
References:
1.  Au, K.G., Clark, S., Miller, J.H. and Modrich, P. Escherichia coli mutY gene encodes an adenine glycosylase active on G-A mispairs. Proc. Natl. Acad. Sci. USA 86 (1989) 8877–8881. [PMID: 2682664]
2.  Michaels, M.L., Tchou, J., Grollman, A.P. and Miller, J.H. A repair system for 8-oxo-7,8-dihydrodeoxyguanine. Biochemistry 31 (1992) 10964–10968. [PMID: 1445834]
[EC 3.2.2.31 created 2018]
 
 
EC 3.13.1.7 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: carbonyl sulfide hydrolase
Reaction: carbonyl sulfide + H2O = hydrogen sulfide + CO2
Other name(s): COSase; COS hydrolase; cos (gene name)
Systematic name: carbonyl sulfide hydrogen-sulfide-lyase (decarboxylating)
Comments: The enzyme, characterized from the bacterium Thiobacillus thioparus, catalyses a step in the degradation pathway of thiocyanate. This activity is also catalysed by the archaeal EC 3.13.1.5, carbon disulfide lyase.
References:
1.  Ogawa, T., Noguchi, K., Saito, M., Nagahata, Y., Kato, H., Ohtaki, A., Nakayama, H., Dohmae, N., Matsushita, Y., Odaka, M., Yohda, M., Nyunoya, H. and Katayama, Y. Carbonyl sulfide hydrolase from Thiobacillus thioparus strain THI115 is one of the β-carbonic anhydrase family enzymes. J. Am. Chem. Soc. 135 (2013) 3818–3825. [PMID: 23406161]
[EC 3.13.1.7 created 2018]
 
 
EC 5.1.3.39 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Deleted entry: L-erythrulose 4-phosphate epimerase. The activity has been shown not to take place.
[EC 5.1.3.39 created 2016, deleted 2018]
 
 
*EC 5.3.3.8 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: Δ32-enoyl-CoA isomerase
Reaction: (1) a (3Z)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-CoA
(2) a (3E)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-CoA
For diagram of Benzoyl-CoA catabolism, click here
Other name(s): ECI (gene name); dodecenoyl-CoA isomerase; dodecenoyl-CoA Δ-isomerase; Δ3-cis2-trans-enoyl-CoA isomerase; acetylene-allene isomerase; dodecenoyl-CoA Δ3-cis2-trans-isomerase; dodecenoyl-CoA (3Z)-(2E)-isomerase
Systematic name: (3Z/3E)-alk-3-enoyl-CoA (2E)-isomerase
Comments: The enzyme participates in the β-oxidation of fatty acids with double bonds at an odd position. Processing of these substrates via the β-oxidation system results in intermediates with a cis- or trans-double bond at position C3, which cannot be processed further by the regular enzymes of the β-oxidation system. This enzyme isomerizes the bond to a trans bond at position C2, which can be processed further. The reaction rate is ten times higher for the (3Z) isomers than for (3E) isomers. The enzyme can also catalyse the isomerization of 3-acetylenic fatty acyl thioesters to 2,3-dienoyl fatty acyl thioesters.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, MetaCyc, PDB, CAS registry number: 62213-29-0
References:
1.  Stoffel, W., Ditzer, R. and Caesar, H. Der Stoffwechsel der ungesättigten Fettsäuren. III. Zur β-Oxydation der Mono- und Polyenfettsäuren. Der Mechanismus der enzymatischen Reaktionen an Δ3cis-Enoyl-CoA-Verbindungen. Hoppe-Seyler's Z. Physiol. Chem. 339 (1964) 167–181. [PMID: 5830064]
2.  Stoffel, W. and Ecker, W. Δ3-cis,-Δ2-trans-Enoyl-CoA isomerase from rat liver mitochondria. Methods Enzymol. 14 (1969) 99–105.
3.  Stoffel, W. and Grol, M. Purification and properties of 3-cis-2-trans-enoyl-CoA isomerase (dodecenoyl-CoA Δ-isomerase) from rat liver mitochondria. Hoppe-Seyler's Z. Physiol. Chem. 359 (1978) 1777–1782. [PMID: 738702]
4.  Miesowicz, F.M. and Bloch, K. Purification of hog liver isomerase. Mechanism of isomerization of 3-alkenyl and 3-alkynyl thioesters. J. Biol. Chem. 254 (1979) 5868–5877. [PMID: 376522]
5.  Engeland, K. and Kindl, H. Purification and characterization of a plant peroxisomal δ 2, δ 3-enoyl-CoA isomerase acting on 3-cis-enoyl-CoA and 3-trans-enoyl-CoA. Eur. J. Biochem. 196 (1991) 699–705. [PMID: 2013292]
6.  Geisbrecht, B.V., Zhang, D., Schulz, H. and Gould, S.J. Characterization of PECI, a novel monofunctional Δ3, Δ2-enoyl-CoA isomerase of mammalian peroxisomes. J. Biol. Chem. 274 (1999) 21797–21803. [PMID: 10419495]
7.  Zhang, D., Yu, W., Geisbrecht, B.V., Gould, S.J., Sprecher, H. and Schulz, H. Functional characterization of Δ32-enoyl-CoA isomerases from rat liver. J. Biol. Chem. 277 (2002) 9127–9132. [PMID: 11781327]
8.  Goepfert, S., Vidoudez, C., Tellgren-Roth, C., Delessert, S., Hiltunen, J.K. and Poirier, Y. Peroxisomal Δ32-enoyl CoA isomerases and evolution of cytosolic paralogues in embryophytes. Plant J. 56 (2008) 728–742. [PMID: 18657232]
[EC 5.3.3.8 created 1978, modified 1980, modified 2018]
 
 
EC 5.3.3.21 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: Δ3,52,4-dienoyl-CoA isomerase
Reaction: a (3E,5Z)-alka-3,5-dienoyl-CoA = a (2E,4E)-alka-2,4-dienoyl-CoA
Other name(s): 3,5-tetradecadienoyl-CoA isomerase; DCI1 (gene name)
Systematic name: (3E,5Z)-alka-3,5-dienoyl-CoA Δ3,52,4 isomerase
Comments: The enzyme participates in an alternative degradation route of fatty acids with cis-double bonds on odd-number carbons such as oleate and linoleate. The main physiological substrate is (3E,5Z)-tetradeca-3,5-dienoyl-CoA, but other (3E,5Z)-dienoyl-CoAs with varying carbon chain lengths are also substrates.
References:
1.  Filppula, S.A., Yagi, A.I., Kilpelainen, S.H., Novikov, D., FitzPatrick, D.R., Vihinen, M., Valle, D. and Hiltunen, J.K. Δ3,52,4-dienoyl-CoA isomerase from rat liver. Molecular characterization. J. Biol. Chem. 273 (1998) 349–355. [PMID: 9417087]
2.  Modis, Y., Filppula, S.A., Novikov, D.K., Norledge, B., Hiltunen, J.K. and Wierenga, R.K. The crystal structure of dienoyl-CoA isomerase at 1.5 Å resolution reveals the importance of aspartate and glutamate sidechains for catalysis. Structure 6 (1998) 957–970. [PMID: 9739087]
3.  Geisbrecht, B.V., Schulz, K., Nau, K., Geraghty, M.T., Schulz, H., Erdmann, R. and Gould, S.J. Preliminary characterization of Yor180Cp: identification of a novel peroxisomal protein of saccharomyces cerevisiae involved in fatty acid metabolism. Biochem. Biophys. Res. Commun. 260 (1999) 28–34. [PMID: 10381339]
4.  Gurvitz, A., Mursula, A.M., Yagi, A.I., Hartig, A., Ruis, H., Rottensteiner, H. and Hiltunen, J.K. Alternatives to the isomerase-dependent pathway for the β-oxidation of oleic acid are dispensable in Saccharomyces cerevisiae. Identification of YOR180c/DCI1 encoding peroxisomal Δ(3,5)-Δ(2,4)-dienoyl-CoA isomerase. J. Biol. Chem. 274 (1999) 24514–24521. [PMID: 10455114]
5.  Zhang, D., Liang, X., He, X.Y., Alipui, O.D., Yang, S.Y. and Schulz, H. Δ3,52,4-dienoyl-CoA isomerase is a multifunctional isomerase. A structural and mechanistic study. J. Biol. Chem. 276 (2001) 13622–13627. [PMID: 11278886]
6.  Goepfert, S., Vidoudez, C., Rezzonico, E., Hiltunen, J.K. and Poirier, Y. Molecular identification and characterization of the Arabidopsis Δ3,52,4-dienoyl-coenzyme A isomerase, a peroxisomal enzyme participating in the β-oxidation cycle of unsaturated fatty acids. Plant Physiol. 138 (2005) 1947–1956. [PMID: 16040662]
[EC 5.3.3.21 created 2018]
 
 
EC 6.3.2.52 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: jasmonoyl—L-amino acid synthetase
Reaction: ATP + jasmonate + an L-amino acid = AMP + diphosphate + a jasmonoyl-L-amino acid
Other name(s): JAR1 (gene name); JAR4 (gene name); JAR6 (gene name)
Systematic name: jasmonate:L-amino acid ligase
Comments: Two jasmonoyl-L-amino acid synthetases have been described from Nicotiana attenuata [3] and one from Arabidopsis thaliana [1]. The N. attenuata enzymes generate jasmonoyl-L-isoleucine, jasmonoyl-L-leucine, and jasmonoyl-L-valine. The enzyme from A. thaliana could catalyse the addition of many different amino acids to jasmonate in vitro [1,4,5]. While the abundant form of jasmonate in plants is (–)-jasmonate, the active form of jasmonoyl-L-isoleucine is (+)-7-iso-jasmonoyl-L-isoleucine.
References:
1.  Staswick, P.E. and Tiryaki, I. The oxylipin signal jasmonic acid is activated by an enzyme that conjugates it to isoleucine in Arabidopsis. Plant Cell 16 (2004) 2117–2127. [PMID: 15258265]
2.  Kang, J.H., Wang, L., Giri, A. and Baldwin, I.T. Silencing threonine deaminase and JAR4 in Nicotiana attenuata impairs jasmonic acid-isoleucine-mediated defenses against Manduca sexta. Plant Cell 18 (2006) 3303–3320. [PMID: 17085687]
3.  Wang, L., Halitschke, R., Kang, J.H., Berg, A., Harnisch, F. and Baldwin, I.T. Independently silencing two JAR family members impairs levels of trypsin proteinase inhibitors but not nicotine. Planta 226 (2007) 159–167. [PMID: 17273867]
4.  Guranowski, A., Miersch, O., Staswick, P.E., Suza, W. and Wasternack, C. Substrate specificity and products of side-reactions catalyzed by jasmonate:amino acid synthetase (JAR1). FEBS Lett. 581 (2007) 815–820. [PMID: 17291501]
5.  Suza, W.P. and Staswick, P.E. The role of JAR1 in jasmonoyl-L-isoleucine production during Arabidopsis wound response. Planta 227 (2008) 1221–1232. [PMID: 18247047]
[EC 6.3.2.52 created 2018]
 
 
*EC 6.3.4.14 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: biotin carboxylase
Reaction: ATP + [biotin carboxyl-carrier protein]-biotin-N6-L-lysine + hydrogencarbonate- = ADP + phosphate + [biotin carboxyl-carrier protein]-carboxybiotin-N6-L-lysine
Other name(s): accC (gene name); biotin-carboxyl-carrier-protein:carbon-dioxide ligase (ADP-forming)
Systematic name: [biotin carboxyl-carrier protein]-biotin-N6-L-lysine:hydrogencarbonate ligase (ADP-forming)
Comments: This enzyme, part of an acetyl-CoA carboxylase complex, acts on a biotin carboxyl-carrier protein (BCCP) that has been biotinylated by EC 6.3.4.15, biotin—[biotin carboxyl-carrier protein] ligase. In some organisms the enzyme is part of a multi-domain polypeptide that also includes the carrier protein (e.g. mycobacteria). Yet in other organisms (e.g. mammals) this activity is included in a single polypeptide that also catalyses the transfer of the carboxyl group from biotin to acetyl-CoA (see EC 6.4.1.2, acetyl-CoA carboxylase).
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]
2.  Norman, E., De Smet, K.A., Stoker, N.G., Ratledge, C., Wheeler, P.R. and Dale, J.W. Lipid synthesis in mycobacteria: characterization of the biotin carboxyl carrier protein genes from Mycobacterium leprae and M. tuberculosis. J. Bacteriol. 176 (1994) 2525–2531. [PMID: 7909542]
3.  Janiyani, K., Bordelon, T., Waldrop, G.L. and Cronan, J.E., Jr. Function of Escherichia coli biotin carboxylase requires catalytic activity of both subunits of the homodimer. J. Biol. Chem. 276 (2001) 29864–29870. [PMID: 11390406]
4.  Chou, C.Y., Yu, L.P. and Tong, L. Crystal structure of biotin carboxylase in complex with substrates and implications for its catalytic mechanism. J. Biol. Chem. 284 (2009) 11690–11697. [PMID: 19213731]
5.  Broussard, T.C., Pakhomova, S., Neau, D.B., Bonnot, R. and Waldrop, G.L. Structural analysis of substrate, reaction intermediate, and product binding in Haemophilus influenzae biotin carboxylase. Biochemistry 54 (2015) 3860–3870. [PMID: 26020841]
[EC 6.3.4.14 created 1976, modified 2014, modified 2018]
 
 
*EC 6.3.4.15 – public review until 19 March 2018 [Last modified: 2018-02-19 08:58:20]
Accepted name: biotin—[biotin carboxyl-carrier protein] ligase
Reaction: ATP + biotin + [biotin carboxyl-carrier protein]-L-lysine = AMP + diphosphate + [biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine
Other name(s): birA (gene name); HLCS (gene name); HCS1 (gene name); biotin-[acetyl-CoA carboxylase] synthetase; biotin-[acetyl coenzyme A carboxylase] synthetase; acetyl coenzyme A holocarboxylase synthetase; acetyl CoA holocarboxylase synthetase; biotin:apocarboxylase ligase; Biotin holoenzyme synthetase; biotin:apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] ligase (AMP-forming); biotin—[acetyl-CoA-carboxylase] ligase
Systematic name: biotin:apo-[carboxyl-carrier protein] ligase (AMP-forming)
Comments: The enzyme biotinylates a biotin carboxyl-carrier protein that is part of an acetyl-CoA carboxylase complex, enabling its subsequent carboxylation by EC 6.3.4.14, biotin carboxylase. The carboxyl group is eventually transferred to acetyl-CoA by EC 2.1.3.15, acetyl-CoA carboxytransferase. In some organisms the carrier protein is part of EC 6.4.1.2, acetyl-CoA carboxylase.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, MetaCyc, PDB, CAS registry number: 37340-95-7
References:
1.  Landman, A.D. and Dakshinamurti, K. Acetyl-Coenzyme A carboxylase. Role of the prosthetic group in enzyme polymerization. Biochem. J. 145 (1975) 545–548. [PMID: 239688]
2.  Wilson, K.P., Shewchuk, L.M., Brennan, R.G., Otsuka, A.J. and Matthews, B.W. Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains. Proc. Natl. Acad. Sci. USA 89 (1992) 9257–9261. [PMID: 1409631]
3.  Nenortas, E. and Beckett, D. Purification and characterization of intact and truncated forms of the Escherichia coli biotin carboxyl carrier subunit of acetyl-CoA carboxylase. J. Biol. Chem. 271 (1996) 7559–7567. [PMID: 8631788]
[EC 6.3.4.15 created 1978, modified 2018]
 
 
*EC 6.4.1.2 – public review until 19 March 2018 [Last modified: 2018-02-20 11:24:21]
Accepted name: acetyl-CoA carboxylase
Reaction: ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA
For diagram of the 3-hydroxypropanoate cycle, click here and for diagram of the 3-hydroxypropanoate/4-hydroxybutanoate cycle and dicarboxylate/4-hydroxybutanoate cycle in archaea, click here
Other name(s): HFA1 (gene name); ACC1 (gene name); acetyl coenzyme A carboxylase; acetyl-CoA:carbon-dioxide ligase (ADP-forming)
Systematic name: acetyl-CoA:hydrogencarbonate ligase (ADP-forming)
Comments: This enzyme is a multi-domain polypeptide that catalyses three different activities - a biotin carboxyl-carrier protein (BCCP), a biotin carboxylase that catalyses the transfer of a carboxyl group from hydrogencarbonate to the biotin molecule carried by the carrier protein, and the transfer of the carboxyl group from biotin to acetyl-CoA, forming malonyl-CoA. In some organisms these activities are catalysed by separate enzymes (see EC 6.3.4.14, biotin carboxylase, and EC 2.1.3.15, acetyl-CoA carboxytransferase). The carboxylation of the carrier protein requires ATP, while the transfer of the carboxyl group to acetyl-CoA does not.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, MetaCyc, PDB, CAS registry number: 9023-93-2
References:
1.  Wakil, S.J. A malonic acid derivative as an intermediate in fatty acid synthesis. J. Am. Chem. Soc. 80 (1958) 6465.
2.  Hatch, M.D. and Stumpf, P.K. Fat metabolism in higher plants. XVI. Acetyl coenzyme A carboxylase and acyl coenzyme A-malonyl coenzyme A transcarboxylase from wheat germ. J. Biol. Chem. 236 (1961) 2879–2885. [PMID: 13905314]
3.  Matsuhashi, M., Matsuhashi, S., Numa, S. and Lynen, F. [On the biosynthesis of fatty acids. IV. Acetyl-CoA carboxylase from yeast.] Biochem. Z. 340 (1964) 243–262. [PMID: 14317957] (in German)
4.  Matsuhashi, M., Matsuhashi, S. and Lynen, F. [On the biosynthesis of fatty acids. V. Acetyl-CoA carboxylase from rat liver and its activation by citric acid.] Biochem. Z. 340 (1964) 263–289. [PMID: 14317958] (in German)
5.  Vagelos, P. Regulation of fatty acid biosynthesis. Curr. Top. Cell. Regul. 4 (1971) 119–166.
6.  Trumble, G.E., Smith, M.A. and Winder, W.W. Purification and characterization of rat skeletal muscle acetyl-CoA carboxylase. Eur. J. Biochem. 231 (1995) 192–198. [PMID: 7628470]
7.  Cheng, D., Chu, C.H., Chen, L., Feder, J.N., Mintier, G.A., Wu, Y., Cook, J.W., Harpel, M.R., Locke, G.A., An, Y. and Tamura, J.K. Expression, purification, and characterization of human and rat acetyl coenzyme A carboxylase (ACC) isozymes. Protein Expr. Purif. 51 (2007) 11–21. [PMID: 16854592]
8.  Kim, K.W., Yamane, H., Zondlo, J., Busby, J. and Wang, M. Expression, purification, and characterization of human acetyl-CoA carboxylase 2. Protein Expr. Purif. 53 (2007) 16–23. [PMID: 17223360]
[EC 6.4.1.2 created 1961, modified 2018]
 
 


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