The Enzyme Database

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EC 1.3.1.9     Relevance: 100%
Accepted name: enoyl-[acyl-carrier-protein] reductase (NADH)
Reaction: an acyl-[acyl-carrier protein] + NAD+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH + H+
Other name(s): enoyl-[acyl carrier protein] reductase; enoyl-ACP reductase; NADH-enoyl acyl carrier protein reductase; NADH-specific enoyl-ACP reductase; acyl-[acyl-carrier-protein]:NAD+ oxidoreductase; fabI (gene name)
Systematic name: acyl-[acyl-carrier protein]:NAD+ oxidoreductase
Comments: The enzyme catalyses an essential step in fatty acid biosynthesis, the reduction of the 2,3-double bond in enoyl-acyl-[acyl-carrier-protein] derivatives of the elongating fatty acid moiety. The enzyme from the bacterium Escherichia coli accepts substrates with carbon chain length from 4 to 18 [3]. The FAS-I enzyme from the bacterium Mycobacterium tuberculosis prefers substrates with carbon chain length from 12 to 24 carbons.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37251-08-4
References:
1.  Shimakata, T. and Stumpf, P.K. Purification and characterizations of β-ketoacyl-[acyl-carrier-protein] reductase, β-hydroxyacyl-[acylcarrier-protein] dehydrase, and enoyl-[acyl-carrier-protein] reductase from Spinacia oleracea leaves. Arch. Biochem. Biophys. 218 (1982) 77–91. [DOI] [PMID: 6756317]
2.  Weeks, G. and Wakil, S.J. Studies on the mechanism of fatty acid synthesis. 18. Preparation and general properties of the enoyl acyl carrier protein reductases from Escherichia coli. J. Biol. Chem. 243 (1968) 1180–1189. [PMID: 4384650]
3.  Yu, X., Liu, T., Zhu, F. and Khosla, C. In vitro reconstitution and steady-state analysis of the fatty acid synthase from Escherichia coli. Proc. Natl. Acad. Sci. USA 108 (2011) 18643–18648. [DOI] [PMID: 22042840]
[EC 1.3.1.9 created 1972, modified 2013]
 
 
EC 1.14.19.24     Relevance: 99.9%
Accepted name: acyl-CoA 11-(E)-desaturase
Reaction: an acyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = an (11E)-enoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Systematic name: acyl-CoA,ferrocytochrome b5:oxygen oxidoreductase (11,12 trans-dehydrogenating)
Comments: Involved in sex pheromone synthesis in the Lepidoptera (moths). The enzyme from the moth Spodoptera littoralis prefers 13:0 and 14:0 substrates. The product is formed by the stereospecific removal of the pro-R H at C-11 and the pro-S H at C-12. cf. EC 1.14.19.5, acyl-CoA 11-(Z)-desaturase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 199543-17-4
References:
1.  Foster, S. P. and Roelofs, W. L. Biosynthesis of a monoene and a conjugated diene sex pheromone component of the lightbrown apple moth by 11 desaturation. Experientia 46 (1990) 269–273.
2.  Martinez, T., Fabrias, G. and Camps, F. Sex pheromone biosynthetic pathway in Spodoptera littoralis and its activation by a neurohormone. J. Biol. Chem. 265 (1990) 1381–1387. [PMID: 2295634]
3.  Navarro, I., Font, I., Fabrias, G. and Camps, F. Stereospecificity of the (E)- and (Z)-11 myristoyl desaturases in the biosynthesis of Spodoptera littoralis sex pheromone. J. Am. Chem. Soc. 119 (1997) 11335–11336.
4.  Pinilla, A., Camps, F. and Fabrias, G. Cryptoregiochemistry of the Δ11-myristoyl-CoA desaturase involved in the biosynthesis of Spodoptera littoralis sex pheromone. Biochemistry 38 (1999) 15272–15277. [DOI] [PMID: 10563812]
[EC 1.14.19.24 created 2000 as EC 1.14.99.31, transferred 2015 to EC 1.14.19.24]
 
 
EC 3.5.1.82     Relevance: 99.8%
Accepted name: N-acyl-D-glutamate deacylase
Reaction: N-acyl-D-glutamate + H2O = a carboxylate + D-glutamate
Systematic name: N-acyl-D-glutamate amidohydrolase
Comments: The enzyme from Alcaligenes xylosoxydans subsp. xylosoxydans and Pseudomonas sp. is specific for N-acyl-D-glutamate. Requires zinc.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 82249-69-2
References:
1.  Wakayama, M., Ashika, T., Miyamoto, Y., Yoshikawa, T., Sonoda, Y., Sakai, K. and Moriguchi, M. Primary structure of N-acyl-D-glutamate amidohydrolase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6. J. Biochem. (Tokyo) 118 (1995) 204–209. [PMID: 8537313]
2.  Wakayama, M., Miura, Y., Oshima, K., Sakai, K., Moriguchi, M. Metal-characterization of N-acyl-D-glutamate amidohydrolase from Pseudomonas sp. strain 5f-1. Biosci. Biotechnol. Biochem. 59 (1995) 1489–1492. [DOI] [PMID: 7549100]
3.  Wakayama, M., Tsutsumi, T., Yada, H., Sakai, K., Moriguchi, M. Chemical modification of histidine residue of N-acyl-D-glutamate amidohydrolase from Pseudomonas sp. 5f-1. Biosci. Biotechnol. Biochem. 60 (1996) 650–653. [DOI] [PMID: 8829533]
[EC 3.5.1.82 created 1999]
 
 
EC 3.5.1.83     Relevance: 99.6%
Accepted name: N-acyl-D-aspartate deacylase
Reaction: N-acyl-D-aspartate + H2O = a carboxylate + D-aspartate
Systematic name: N-acyl-D-aspartate amidohydrolase
Comments: The enzyme from Alcaligenes xylosoxydans subsp. xylosoxydans is specific for N-acyl-D-aspartate. Requires zinc.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9031-86-1
References:
1.  Moriguchi, M., Sakai, K., Katsuno, Y., Maki, T., Wakayama, M. Purification and characterization of novel N-acyl-D-aspartate amidohydrolase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6. Biosci. Biotechnol. Biochem. 57 (1993) 1145–1148. [DOI] [PMID: 7763985]
2.  Wakayama, M., Watanabe, E., Takenaka, Y., Miyamoto, Y., Tau, Y., Sakai, K., Moriguchi, M. Cloning, expression and nucleotide sequence of the N-acyl-D-aspartate amidohydrolase gene from Alcaligenes xylosoxydans subsp. xylosoxydans A-6. J. Ferment. Bioeng. 80 (1995) 311–317.
[EC 3.5.1.83 created 1999]
 
 
EC 3.1.2.19     Relevance: 99.5%
Accepted name: ADP-dependent medium-chain-acyl-CoA hydrolase
Reaction: acyl-CoA + H2O = CoA + a carboxylate
Other name(s): medium-chain acyl coenzyme A hydrolase; medium-chain acyl-CoA hydrolase; medium-chain acyl-thioester hydrolase; medium-chain hydrolase; myristoyl-CoA thioesterase
Systematic name: ADP-dependent-medium-chain-acyl-CoA hydrolase
Comments: Requires ADP; inhibited by NADH. Maximum activity is shown with nonanoyl-CoA.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 63363-75-7
References:
1.  Alexson, S.E.H. and Nedergaard, J. A novel type of short- and medium-chain acyl-CoA hydrolases in brown adipose tissue mitochondria. J. Biol. Chem. 263 (1988) 13564–13571. [PMID: 2901416]
[EC 3.1.2.19 created 1992]
 
 
EC 1.3.8.8     Relevance: 99%
Accepted name: long-chain acyl-CoA dehydrogenase
Reaction: a long-chain acyl-CoA + electron-transfer flavoprotein = a long-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein
Glossary: a long-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains 13 to 22 carbon atoms.
Other name(s): palmitoyl-CoA dehydrogenase; palmitoyl-coenzyme A dehydrogenase; long-chain acyl-coenzyme A dehydrogenase; long-chain-acyl-CoA:(acceptor) 2,3-oxidoreductase; ACADL (gene name).
Systematic name: long-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase
Comments: Contains a tightly-bound FAD cofactor. One of several enzymes that catalyse the first step in fatty acids β-oxidation. The enzyme from pig liver can accept substrates with acyl chain lengths of 6 to at least 16 carbon atoms. The highest activity was found with C12, and the rates with C8 and C16 were 80 and 70%, respectively [2]. The enzyme from rat can accept substrates with C8-C22. It is most active with C14 and C16, and has no activity with C4, C6 or C24 [4]. cf. EC 1.3.8.1, short-chain acyl-CoA dehydrogenase, EC 1.3.8.8, medium-chain acyl-CoA dehydrogenase, and EC 1.3.8.9, very-long-chain acyl-CoA dehydrogenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 59536-74-2
References:
1.  Crane, F.L., Hauge, J.G. and Beinert, H. Flavoproteins involved in the first oxidative step of the fatty acid cycle. Biochim. Biophys. Acta 17 (1955) 292–294. [DOI] [PMID: 13239683]
2.  Hauge, J.G., Crane, F.L. and Beinert, H. On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. III. Palmityl CoA dehydrogenase. J. Biol. Chem. 219 (1956) 727–733. [PMID: 13319294]
3.  Hall, C.L., Heijkenkjold, L., Bartfai, T., Ernster, L. and Kamin, H. Acyl coenzyme A dehydrogenases and electron-transferring flavoprotein from beef heart mitochondria. Arch. Biochem. Biophys. 177 (1976) 402–414. [DOI] [PMID: 1015826]
4.  Ikeda, Y., Ikeda, K.O. and Tanaka, K. Purification and characterization of short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria. Isolation of the holo- and apoenzymes and conversion of the apoenzyme to the holoenzyme. J. Biol. Chem. 260 (1985) 1311–1325. [PMID: 3968063]
5.  Djordjevic, S., Dong, Y., Paschke, R., Frerman, F.E., Strauss, A.W. and Kim, J.J. Identification of the catalytic base in long chain acyl-CoA dehydrogenase. Biochemistry 33 (1994) 4258–4264. [PMID: 8155643]
[EC 1.3.8.8 created 1989 as EC 1.3.99.13, part transferred 2012 to EC 1.3.8.8]
 
 
EC 3.6.3.47      
Transferred entry: fatty-acyl-CoA-transporting ATPase. Now EC 7.6.2.4, fatty-acyl-CoA-transporting ATPase
[EC 3.6.3.47 created 2000, deleted 2018]
 
 
EC 2.3.1.180     Relevance: 98.3%
Accepted name: β-ketoacyl-[acyl-carrier-protein] synthase III
Reaction: acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Other name(s): 3-oxoacyl:ACP synthase III; 3-ketoacyl-acyl carrier protein synthase III; KASIII; KAS III; FabH; β-ketoacyl-acyl carrier protein synthase III; β-ketoacyl-ACP synthase III; β-ketoacyl (acyl carrier protein) synthase III; acetyl-CoA:malonyl-[acyl-carrier-protein] C-acyltransferase
Systematic name: acetyl-CoA:malonyl-[acyl-carrier protein] C-acyltransferase
Comments: The enzyme is responsible for initiating straight-chain fatty acid biosynthesis by the dissociated (or type II) fatty-acid biosynthesis system that occurs in plants and bacteria. In contrast to EC 2.3.1.41, β-ketoacyl-[acyl-carrier-protein] synthase I, and EC 2.3.1.179, β-ketoacyl-[acyl-carrier-protein] synthase II, this enzyme specifically uses short-chain acyl-CoA thioesters (preferably acetyl-CoA) rather than acyl-[acp] as its substrate [1]. The enzyme can also catalyse the reaction of EC 2.3.1.38, [acyl-carrier-protein] S-acetyltransferase, but to a much lesser extent [1]. The enzymes from some organisms (e.g. the Gram-positive bacterium Streptococcus pneumoniae) can accept branched-chain acyl-CoAs in addition to acetyl-CoA [5] (cf. EC 2.3.1.300, branched-chain β-ketoacyl-[acyl-carrier-protein] synthase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 1048646-78-1
References:
1.  Tsay, J.T., Oh, W., Larson, T.J., Jackowski, S. and Rock, C.O. Isolation and characterization of the β-ketoacyl-acyl carrier protein synthase III gene (fabH) from Escherichia coli K-12. J. Biol. Chem. 267 (1992) 6807–6814. [PMID: 1551888]
2.  Cronan, J.E., Jr. and Rock, C.O. Biosynthesis of membrane lipids. In: Neidhardt, F.C. (Ed.), Escherichia coli and Salmonella: Cellular and Molecular Biology, 2nd edn, vol. 1, ASM Press, Washington, DC, 1996, pp. 612–636.
3.  Han, L., Lobo, S. and Reynolds, K.A. Characterization of β-ketoacyl-acyl carrier protein synthase III from Streptomyces glaucescens and its role in initiation of fatty acid biosynthesis. J. Bacteriol. 180 (1998) 4481–4486. [DOI] [PMID: 9721286]
4.  Choi, K.H., Kremer, L., Besra, G.S. and Rock, C.O. Identification and substrate specificity of β-ketoacyl (acyl carrier protein) synthase III (mtFabH) from Mycobacterium tuberculosis. J. Biol. Chem. 275 (2000) 28201–28207. [DOI] [PMID: 10840036]
5.  Khandekar, S.S., Gentry, D.R., Van Aller, G.S., Warren, P., Xiang, H., Silverman, C., Doyle, M.L., Chambers, P.A., Konstantinidis, A.K., Brandt, M., Daines, R.A. and Lonsdale, J.T. Identification, substrate specificity, and inhibition of the Streptococcus pneumoniae β-ketoacyl-acyl carrier protein synthase III (FabH). J. Biol. Chem. 276 (2001) 30024–30030. [DOI] [PMID: 11375394]
6.  Qiu, X., Choudhry, A.E., Janson, C.A., Grooms, M., Daines, R.A., Lonsdale, J.T. and Khandekar, S.S. Crystal structure and substrate specificity of the β-ketoacyl-acyl carrier protein synthase III (FabH) from Staphylococcus aureus. Protein Sci. 14 (2005) 2087–2094. [DOI] [PMID: 15987898]
7.  Li, Y., Florova, G. and Reynolds, K.A. Alteration of the fatty acid profile of Streptomyces coelicolor by replacement of the initiation enzyme 3-ketoacyl acyl carrier protein synthase III (FabH). J. Bacteriol. 187 (2005) 3795–3799. [DOI] [PMID: 15901703]
[EC 2.3.1.180 created 2006, modified 2021]
 
 
EC 5.5.1.30     Relevance: 98.1%
Accepted name: labda-7,13-dienyl diphosphate synthase
Reaction: geranylgeranyl diphosphate = (13E)-labda-7,13-dien-15-yl diphosphate
For diagram of labdane diterpenoids biosynthesis, click here
Other name(s): SCLAV_p0490
Systematic name: (13E)-labda-7,13-dien-15-yl-diphosphate lyase (ring-opening)
Comments: Isolated from the bacterium Streptomyces clavuligerus.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Yamada, Y., Komatsu, M. and Ikeda, H. Chemical diversity of labdane-type bicyclic diterpene biosynthesis in Actinomycetales microorganisms. J. Antibiot. (Tokyo) 69 (2016) 515–523. [DOI] [PMID: 26814669]
[EC 5.5.1.30 created 2017]
 
 
EC 1.1.1.212     Relevance: 97.5%
Accepted name: 3-oxoacyl-[acyl-carrier-protein] reductase (NADH)
Reaction: a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NAD+ = a 3-oxoacyl-[acyl-carrier protein] + NADH + H+
Other name(s): 3-oxoacyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide) reductase; 3-oxoacyl-[acyl-carrier-protein] reductase (NADH); (3R)-3-hydroxyacyl-[acyl-carrier-protein]:NAD+ oxidoreductase
Systematic name: (3R)-3-hydroxyacyl-[acyl-carrier protein]:NAD+ oxidoreductase
Comments: Forms part of the fatty acid synthase system in plants. Can be separated from EC 1.1.1.100, 3-oxoacyl-[acyl-carrier-protein] reductase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 82047-86-7
References:
1.  Caughey, I. and Kekwick, R.G.O. The characteristics of some components of the fatty acid synthetase system in the plastids from the mesocarp of avocado (Persea americana) fruit. Eur. J. Biochem. 123 (1982) 553–561. [DOI] [PMID: 7075600]
[EC 1.1.1.212 created 1986]
 
 
EC 1.14.19.11     Relevance: 97.4%
Accepted name: acyl-[acyl-carrier-protein] 4-desaturase
Reaction: palmitoyl-[acyl-carrier protein] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = (4Z)-hexadec-4-enoyl-[acyl-carrier protein] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
Other name(s): Δ4-palmitoyl-[acyl carrier protein] desaturase
Systematic name: palmitoyl-[acyl-carrier protein],reduced acceptor:oxygen oxidoreductase (4,5 cis-dehydrogenating)
Comments: The enzymes from the plants Coriandrum sativum (coriander) and Hedera helix (English ivy) are involved in biosynthesis of petroselinate [(6Z)-octadec-6-enoate], which is formed by elongation of (4Z)-hexadec-4-enoate. The ivy enzyme can also act on oleoyl-[acyl-carrier protein] and palmitoleoyl-[acyl-carrier protein], generating the corresponding 4,9-diene.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Cahoon, E.B., Shanklin, J. and Ohlrogge, J.B. Expression of a coriander desaturase results in petroselinic acid production in transgenic tobacco. Proc. Natl. Acad. Sci. USA 89 (1992) 11184–11188. [DOI] [PMID: 1454797]
2.  Cahoon, E.B. and Ohlrogge, J.B. Metabolic evidence for the involvement of a Δ4-palmitoyl-acyl carrier protein desaturase in petroselinic acid synthesis in coriander endosperm and transgenic tobacco cells. Plant Physiol. 104 (1994) 827–837. [PMID: 12232129]
3.  Whittle, E., Cahoon, E.B., Subrahmanyam, S. and Shanklin, J. A multifunctional acyl-acyl carrier protein desaturase from Hedera helix L. (English ivy) can synthesize 16- and 18-carbon monoene and diene products. J. Biol. Chem. 280 (2005) 28169–28176. [DOI] [PMID: 15939740]
[EC 1.14.19.11 created 2015]
 
 
EC 7.6.2.4     Relevance: 97.1%
Accepted name: ABC-type fatty-acyl-CoA transporter
Reaction: ATP + H2O + fatty acyl CoA[side 1] = ADP + phosphate + fatty acyl CoA[side 2]
Other name(s): fatty-acyl-CoA-transporting ATPase
Systematic name: ATP phosphohydrolase (ABC-type, fatty-acyl-CoA-transporting)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. An animal and yeast enzyme that transports fatty acyl CoA into and out of peroxisomes. In humans, it is associated with Zellweger’s syndrome.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Kamijo, K., Taketani, S., Yokota, S., Osumi, T. and Hashimoto, T. The 70-kDa peroxisomal membrane protein is a member of the Mdr (P-glcoprotein)-related ATP-binding protein superfamily. J. Biol. Chem. 265 (1990) 4534–4540. [PMID: 1968461]
2.  Hettema, E.H., van Roermund, C.W.T., Distel, B. , van den Berg. M., Vilela, C., Rodrigues-Posada, C., Wanders, R.J.A. and Tabak, H.F. The ABC transporter proteins Pat1 and Pat2 are required for import of long-chain fatty acids into peroxisomes of Saccharomyces cerevisiae. EMBO J. 15 (1996) 3813–3822. [PMID: 8670886]
3.  Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81–136. [PMID: 9889977]
[EC 7.6.2.4 created 2000 as EC 3.6.3.47, transferred 2018 to EC 7.6.2.4]
 
 
EC 3.5.1.55     Relevance: 97%
Accepted name: long-chain-fatty-acyl-glutamate deacylase
Reaction: N-long-chain-fatty-acyl-L-glutamate + H2O = a long-chain carboxylate + L-glutamate
Other name(s): long-chain aminoacylase; long-chain-fatty-acyl-glutamate deacylase; long-chain acylglutamate amidase; N-acyl-D-glutamate deacylase
Systematic name: N-long-chain-fatty-acyl-L-glutamate amidohydrolase
Comments: Does not act on acyl derivates of other amino acids. Optimum chain length of acyl residue is 12 to 16.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 82249-69-2
References:
1.  Fukuda, H., Iwade, S. and Kimura, A. A new enzyme: long acyl aminoacylase from Pseudomonas diminuta. J. Biochem. (Tokyo) 91 (1982) 1731–1738. [PMID: 7096313]
[EC 3.5.1.55 created 1986]
 
 
EC 1.14.14.105     Relevance: 97%
Accepted name: taxane 10β-hydroxylase
Reaction: taxa-4(20),11-dien-5α-yl acetate + [reduced NADPH—hemoprotein reductase] + O2 = 10β-hydroxytaxa-4(20),11-dien-5α-yl acetate + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of taxadiene hydroxylation, click here
Other name(s): CYP725A1 (gene name); 5-α-taxadienol-10-β-hydroxylase
Systematic name: taxa-4(20),11-dien-5α-yl acetate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (10β-hydroxylating)
Comments: This microsomal cytochrome-P-450 (heme-thiolate) enzyme from the plant Taxus cuspidata is involved in the biosynthesis of the diterpenoid antineoplastic drug taxol (paclitaxel).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 337514-75-7
References:
1.  Wheeler, A.L., Long, R.M., Ketchum, R.E., Rithner, C.D., Williams, R.M. and Croteau, R. Taxol biosynthesis: differential transformations of taxadien-5α-ol and its acetate ester by cytochrome P450 hydroxylases from Taxus suspension cells. Arch. Biochem. Biophys. 390 (2001) 265. [DOI] [PMID: 11396929]
2.  Jennewein, S., Rithner, C.D., Williams, R.M. and Croteau, R.B. Taxol biosynthesis: taxane 13 α-hydroxylase is a cytochrome P450-dependent monooxygenase. Proc. Natl. Acad. Sci. USA 98 (2001) 13595. [DOI] [PMID: 11707604]
3.  Schoendorf, A., Rithner, C.D., Williams, R.M. and Croteau, R.B. Molecular cloning of a cytochrome P450 taxane 10β-hydroxylase cDNA from Taxus and functional expression in yeast. Proc. Natl. Acad. Sci. USA 98 (2001) 1501–1506. [DOI] [PMID: 11171980]
[EC 1.14.14.105 created 2002 as EC 1.14.13.76, transferred 2018 to EC 1.14.14.105]
 
 
EC 1.14.19.26     Relevance: 96.4%
Accepted name: acyl-[acyl-carrier-protein] 6-desaturase
Reaction: palmitoyl-[acyl-carrier protein] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = (6Z)-hexadec-6-enoyl-[acyl-carrier protein] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
Glossary: (6Z)-hexadec-6-enoyl-[acyl-carrier protein] = Δ6-hexadecenoyl-[acyl-carrier protein] = sapienoyl-[acyl-carrier-protein]
an [acyl-carrier protein] = ACP = [acp]
Other name(s): DELTA6 palmitoyl-ACP desaturase; DELTA6 16:0-ACP desaturase
Systematic name: palmitoyl-[acyl-carrier protein],reduced ferredoxin:oxygen oxidoreductase (6,7 cis-dehydrogenating)
Comments: The enzyme, characterized from the endosperm of the plant Thunbergia alata (black-eyed Susan vine), introduces a cis double bond at carbon 6 of several saturated acyl-[acp]s. It is most active with palmitoyl-[acp] (16:0), but can also act on myristoyl-[acp] (14:0) and stearoyl-[acp] (18:0). The position of the double bond is determined by its distance from the carboxyl end of the fatty acid.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Cahoon, E.B., Cranmer, A.M., Shanklin, J. and Ohlrogge, J.B. Δ6 Hexadecenoic acid is synthesized by the activity of a soluble Δ6 palmitoyl-acyl carrier protein desaturase in Thunbergia alata endosperm. J. Biol. Chem. 269 (1994) 27519–27526. [PMID: 7961667]
2.  Cahoon, E.B., Lindqvist, Y., Schneider, G. and Shanklin, J. Redesign of soluble fatty acid desaturases from plants for altered substrate specificity and double bond position. Proc. Natl. Acad. Sci. USA 94 (1997) 4872–4877. [DOI] [PMID: 9144157]
[EC 1.14.19.26 created 2015]
 
 
EC 4.2.1.121     Relevance: 96.4%
Accepted name: colneleate synthase
Reaction: (9S,10E,12Z)-9-hydroperoxyoctadeca-10,12-dienoate = (8E)-9-[(1E,3Z)-nona-1,3-dien-1-yloxy]non-8-enoate + H2O
Glossary: colneleate = (8E)-9-[(1E,3Z)-nona-1,3-dien-1-yloxy]non-8-enoate
Other name(s): 9-divinyl ether synthase; 9-DES; CYP74D; CYP74D1; CYP74 cytochrome P-450; DES1; (8E)-9-[(1E,3E)-nona-1,3-dien-1-yloxy]non-8-enoate synthase
Systematic name: (9S,10E,12Z)-9-hydroperoxyoctadeca-10,12-dienoate hydro-lyase
Comments: A heme-thiolate protein (P-450) [2]. It catalyses the selective removal of pro-R hydrogen at C-8 in the biosynthesis of colneleic acid [4]. It forms also (8E)-9-[(1E,3Z,6Z)-nona-1,3,6-trien-1-yloxy]non-8-enoic acid (i.e. colnelenate) from (9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate. The corresponding 13-hydroperoxides are poor substrates [1,3]. The divinyl ethers colneleate and colnelenate have antimicrobial activity.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Stumpe, M., Kandzia, R., Gobel, C., Rosahl, S. and Feussner, I. A pathogen-inducible divinyl ether synthase (CYP74D) from elicitor-treated potato suspension cells. FEBS Lett. 507 (2001) 371–376. [DOI] [PMID: 11696374]
2.  Itoh, A. and Howe, G.A. Molecular cloning of a divinyl ether synthase. Identification as a CYP74 cytochrome P-450. J. Biol. Chem. 276 (2001) 3620–3627. [DOI] [PMID: 11060314]
3.  Fammartino, A., Cardinale, F., Gobel, C., Mene-Saffrane, L., Fournier, J., Feussner, I. and Esquerre-Tugaye, M.T. Characterization of a divinyl ether biosynthetic pathway specifically associated with pathogenesis in tobacco. Plant Physiol. 143 (2007) 378–388. [DOI] [PMID: 17085514]
4.  Hamberg, M. Hidden stereospecificity in the biosynthesis of divinyl ether fatty acids. FEBS J. 272 (2005) 736–743. [DOI] [PMID: 15670154]
[EC 4.2.1.121 created 2011, modified 2014]
 
 
EC 1.1.1.386     Relevance: 96.2%
Accepted name: ipsdienol dehydrogenase
Reaction: (R)-ipsdienol + NAD(P)+ = ipsdienone + NAD(P)H + H+
For diagram of acyclic monoterpenoid biosynthesis, click here
Glossary: ipsdienone = 2-methyl-6-methyleneocta-2,7-dien-4-one
(R)-ipsdienol = (4R)-2-methyl-6-methyleneocta-2,7-dien-4-ol
Other name(s): IDOLDH
Systematic name: (R)-ipsdienol:NAD(P)+ oxidoreductase
Comments: The enzyme is involved in pheromone production by the pine engraver beetle, Ips pini.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Figueroa-Teran, R., Welch, W.H., Blomquist, G.J. and Tittiger, C. Ipsdienol dehydrogenase (IDOLDH): a novel oxidoreductase important for Ips pini pheromone production. Insect Biochem. Mol. Biol. 42 (2012) 81–90. [DOI] [PMID: 22101251]
[EC 1.1.1.386 created 2015]
 
 
EC 2.3.1.184     Relevance: 96%
Accepted name: acyl-homoserine-lactone synthase
Reaction: an acyl-[acyl-carrier protein] + S-adenosyl-L-methionine = an [acyl-carrier protein] + S-methyl-5′-thioadenosine + an N-acyl-L-homoserine lactone
For diagram of reaction, click here
Other name(s): acyl-homoserine lactone synthase; acyl homoserine lactone synthase; acyl-homoserinelactone synthase; acylhomoserine lactone synthase; AHL synthase; AHS; AHSL synthase; AhyI; AinS; AinS protein; autoinducer synthase; autoinducer synthesis protein rhlI; EsaI; ExpISCC1; ExpISCC3065; LasI; LasR; LuxI; LuxI protein; LuxM; N-acyl homoserine lactone synthase; RhlI; YspI ; acyl-[acyl carrier protein]:S-adenosyl-L-methionine acyltranserase (lactone-forming, methylthioadenosine-releasing)
Systematic name: acyl-[acyl-carrier protein]:S-adenosyl-L-methionine acyltranserase (lactone-forming, methylthioadenosine-releasing)
Comments: Acyl-homoserine lactones (AHLs) are produced by a number of bacterial species and are used by them to regulate the expression of virulence genes in a process known as quorum-sensing. Each bacterial cell has a basal level of AHL and, once the population density reaches a critical level, it triggers AHL-signalling which, in turn, initiates the expression of particular virulence genes [5]. N-(3-Oxohexanoyl)-[acyl-carrier protein] and hexanoyl-[acyl-carrier protein] are the best substrates [1]. The fatty-acyl substrate is derived from fatty-acid biosynthesis through acyl-[acyl-carrier protein] rather than from fatty-acid degradation through acyl-CoA [1]. S-Adenosyl-L-methionine cannot be replaced by methionine, S-adenosylhomocysteine, homoserine or homoserine lactone [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 176023-66-8
References:
1.  Schaefer, A.L., Val, D.L., Hanzelka, B.L., Cronan, J.E., Jr. and Greenberg, E.P. Generation of cell-to-cell signals in quorum sensing: acyl homoserine lactone synthase activity of a purified Vibrio fischeri LuxI protein. Proc. Natl. Acad. Sci. USA 93 (1996) 9505–9509. [DOI] [PMID: 8790360]
2.  Watson, W.T., Murphy, F.V., 4th, Gould, T.A., Jambeck, P., Val, D.L., Cronan, J.E., Jr., Beck von Bodman, S. and Churchill, M.E. Crystallization and rhenium MAD phasing of the acyl-homoserinelactone synthase EsaI. Acta Crystallogr. D Biol. Crystallogr. 57 (2001) 1945–1949. [PMID: 11717525]
3.  Chakrabarti, S. and Sowdhamini, R. Functional sites and evolutionary connections of acylhomoserine lactone synthases. Protein Eng. 16 (2003) 271–278. [PMID: 12736370]
4.  Hanzelka, B.L., Parsek, M.R., Val, D.L., Dunlap, P.V., Cronan, J.E., Jr. and Greenberg, E.P. Acylhomoserine lactone synthase activity of the Vibrio fischeri AinS protein. J. Bacteriol. 181 (1999) 5766–5770. [PMID: 10482519]
5.  Parsek, M.R., Val, D.L., Hanzelka, B.L., Cronan, J.E., Jr. and Greenberg, E.P. Acyl homoserine-lactone quorum-sensing signal generation. Proc. Natl. Acad. Sci. USA 96 (1999) 4360–4365. [DOI] [PMID: 10200267]
6.  Ulrich, R.L. Quorum quenching: enzymatic disruption of N-acylhomoserine lactone-mediated bacterial communication in Burkholderia thailandensis. Appl. Environ. Microbiol. 70 (2004) 6173–6180. [DOI] [PMID: 15466564]
7.  Gould, T.A., Schweizer, H.P. and Churchill, M.E. Structure of the Pseudomonas aeruginosa acyl-homoserinelactone synthase LasI. Mol. Microbiol. 53 (2004) 1135–1146. [DOI] [PMID: 15306017]
8.  Raychaudhuri, A., Jerga, A. and Tipton, P.A. Chemical mechanism and substrate specificity of RhlI, an acylhomoserine lactone synthase from Pseudomonas aeruginosa. Biochemistry 44 (2005) 2974–2981. [DOI] [PMID: 15723540]
9.  Gould, T.A., Herman, J., Krank, J., Murphy, R.C. and Churchill, M.E. Specificity of acyl-homoserine lactone synthases examined by mass spectrometry. J. Bacteriol. 188 (2006) 773–783. [DOI] [PMID: 16385066]
[EC 2.3.1.184 created 2007]
 
 
EC 4.2.1.60      
Deleted entry: 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase. The reaction described is covered by EC 4.2.1.59.
[EC 4.2.1.60 created 1972, modified 2006, deleted 2012]
 
 
EC 6.2.1.39     Relevance: 95.7%
Accepted name: [butirosin acyl-carrier protein]—L-glutamate ligase
Reaction: (1) ATP + L-glutamate + BtrI acyl-carrier protein = ADP + phosphate + L-glutamyl-[BtrI acyl-carrier protein]
(2) ATP + L-glutamate + 4-amino butanoyl-[BtrI acyl-carrier protein] = ADP + phosphate + 4-(γ-L-glutamylamino)butanoyl-[BtrI acyl-carrier protein]
Other name(s): [BtrI acyl-carrier protein]—L-glutamate ligase; BtrJ
Systematic name: [BtrI acyl-carrier protein]:L-glutamate ligase (ADP-forming)
Comments: Catalyses two steps in the biosynthesis of the side chain of the aminoglycoside antibiotics of the butirosin family. The enzyme adds one molecule of L-glutamate to a dedicated acyl-carrier protein, and following decarboxylation of the product by EC 4.1.1.95, L-glutamyl-[BtrI acyl-carrier protein] decarboxylase, adds a second L-glutamate molecule. Requires Mg2+ or Mn2+, and activity is enhanced in the presence of Mn2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Li, Y., Llewellyn, N.M., Giri, R., Huang, F. and Spencer, J.B. Biosynthesis of the unique amino acid side chain of butirosin: possible protective-group chemistry in an acyl carrier protein-mediated pathway. Chem. Biol. 12 (2005) 665–675. [DOI] [PMID: 15975512]
[EC 6.2.1.39 created 2012]
 
 
EC 1.14.19.2     Relevance: 95.7%
Accepted name: stearoyl-[acyl-carrier-protein] 9-desaturase
Reaction: stearoyl-[acyl-carrier protein] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = oleoyl-[acyl-carrier protein] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
Other name(s): stearyl acyl carrier protein desaturase; stearyl-ACP desaturase; acyl-[acyl-carrier-protein] desaturase; acyl-[acyl-carrier protein],hydrogen-donor:oxygen oxidoreductase
Systematic name: stearoyl-[acyl-carrier protein],reduced ferredoxin:oxygen oxidoreductase (9,10 cis-dehydrogenating)
Comments: The enzyme is found in the lumen of plastids, where de novo biosynthesis of fatty acids occurs, and acts on freshly synthesized saturated fatty acids that are still linked to acyl-carrier protein. The enzyme determines the position of the double bond by its distance from the carboxylic acid end of the fatty acid. It also acts on palmitoyl-[acyl-carrier-protein] [4,5].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37256-86-3
References:
1.  Jaworski, J.G. and Stumpf, P.K. Fat metabolism in higher plants. Properties of a soluble stearyl-acyl carrier protein desaturase from maturing Carthamus tinctorius. Arch. Biochem. Biophys. 162 (1974) 158–165. [DOI] [PMID: 4831331]
2.  Nagai, J. and Bloch, K. Enzymatic desaturation of stearyl acyl carrier protein. J. Biol. Chem. 243 (1968) 4626–4633. [PMID: 4300868]
3.  Shanklin, J. and Somerville, C. Stearoyl-acyl-carrier-protein desaturase from higher plants is structurally unrelated to the animal and fungal homologs. Proc. Natl. Acad. Sci. USA 88 (1991) 2510–2514. [DOI] [PMID: 2006187]
4.  Cahoon, E.B., Lindqvist, Y., Schneider, G. and Shanklin, J. Redesign of soluble fatty acid desaturases from plants for altered substrate specificity and double bond position. Proc. Natl. Acad. Sci. USA 94 (1997) 4872–4877. [DOI] [PMID: 9144157]
5.  Cao, Y., Xian, M., Yang, J., Xu, X., Liu, W. and Li, L. Heterologous expression of stearoyl-acyl carrier protein desaturase (S-ACP-DES) from Arabidopsis thaliana in Escherichia coli. Protein Expr. Purif. 69 (2010) 209–214. [DOI] [PMID: 19716420]
[EC 1.14.19.2 created 1972 as EC 1.14.99.6, modified 2000, transferred 2000 to EC 1.14.19.2, modified 2015]
 
 
EC 1.3.1.93     Relevance: 95.7%
Accepted name: very-long-chain enoyl-CoA reductase
Reaction: a very-long-chain acyl-CoA + NADP+ = a very-long-chain trans-2,3-dehydroacyl-CoA + NADPH + H+
Glossary: a very-long-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains 23 or more carbon atoms.
Other name(s): TSC13 (gene name); CER10 (gene name)
Systematic name: very-long-chain acyl-CoA:NADP+ oxidoreductase
Comments: This is the fourth component of the elongase, a microsomal protein complex responsible for extending palmitoyl-CoA and stearoyl-CoA (and modified forms thereof) to very-long-chain acyl CoAs. cf. EC 2.3.1.199, very-long-chain 3-oxoacyl-CoA synthase, EC 1.1.1.330, very-long-chain 3-oxoacyl-CoA reductase, and EC 4.2.1.134, very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Kohlwein, S.D., Eder, S., Oh, C.S., Martin, C.E., Gable, K., Bacikova, D. and Dunn, T. Tsc13p is required for fatty acid elongation and localizes to a novel structure at the nuclear-vacuolar interface in Saccharomyces cerevisiae. Mol. Cell Biol. 21 (2001) 109–125. [DOI] [PMID: 11113186]
2.  Gable, K., Garton, S., Napier, J.A. and Dunn, T.M. Functional characterization of the Arabidopsis thaliana orthologue of Tsc13p, the enoyl reductase of the yeast microsomal fatty acid elongating system. J. Exp. Bot. 55 (2004) 543–545. [DOI] [PMID: 14673020]
3.  Kvam, E., Gable, K., Dunn, T.M. and Goldfarb, D.S. Targeting of Tsc13p to nucleus-vacuole junctions: a role for very-long-chain fatty acids in the biogenesis of microautophagic vesicles. Mol. Biol. Cell 16 (2005) 3987–3998. [DOI] [PMID: 15958487]
4.  Zheng, H., Rowland, O. and Kunst, L. Disruptions of the Arabidopsis enoyl-CoA reductase gene reveal an essential role for very-long-chain fatty acid synthesis in cell expansion during plant morphogenesis. Plant Cell 17 (2005) 1467–1481. [DOI] [PMID: 15829606]
[EC 1.3.1.93 created 2012]
 
 
EC 3.5.1.17     Relevance: 95.3%
Accepted name: acyl-lysine deacylase
Reaction: N6-acyl-L-lysine + H2O = a carboxylate + L-lysine
Other name(s): ε-lysine acylase; 6-N-acyl-L-lysine amidohydrolase
Systematic name: N6-acyl-L-lysine amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9025-11-0
References:
1.  Paik, W.K., Bloch-Frankenthal, L., Birnbaum, S.M., Winitz, M. and Greenstein, J.P. ε-Lysine acylase. Arch. Biochem. Biophys. 69 (1957) 56–66. [PMID: 13445179]
[EC 3.5.1.17 created 1965]
 
 
EC 2.3.1.301     Relevance: 95.1%
Accepted name: mycobacterial β-ketoacyl-[acyl carrier protein] synthase III
Reaction: dodecanoyl-CoA + a malonyl-[acyl-carrier protein] = a 3-oxotetradecanoyl-[acyl-carrier protein] + CoA + CO2
Glossary: dodecanoyl-CoA = lauroyl-CoA
Other name(s): fabH (gene name) (ambiguous); mycobacterial 3-oxoacyl-[acyl carrier protein] synthase III
Systematic name: dodecanoyl-CoA:malonyl-[acyl-carrier protein] C-acyltransferase
Comments: The enzyme, characterized from mycobacteria, provides a link between the type I and type II fatty acid synthase systems (FAS-I and FAS-II, respectively) found in these organisms. The enzyme acts on medium- and long-chain acyl-CoAs (C12-C16) produced by the FAS-I system, condensing them with malonyl-[acyl-carrier protein] (malonyl-AcpM) and forming starter molecules for the FAS-II system, which elongates them into meromycolic acids. The enzyme has no activity with short-chain acyl-CoAs (e.g. acetyl-CoA), which are used by EC 2.3.1.180, β-ketoacyl-[acyl-carrier-protein] synthase III, or branched-chain acyl-CoAs, which are used by EC 2.3.1.300, branched-chain β-ketoacyl-[acyl-carrier-protein] synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Scarsdale, J.N., Kazanina, G., He, X., Reynolds, K.A. and Wright, H.T. Crystal structure of the Mycobacterium tuberculosis β-ketoacyl-acyl carrier protein synthase III. J. Biol. Chem. 276 (2001) 20516–20522. [DOI] [PMID: 11278743]
2.  Musayev, F., Sachdeva, S., Scarsdale, J.N., Reynolds, K.A. and Wright, H.T. Crystal structure of a substrate complex of Mycobacterium tuberculosis β-ketoacyl-acyl carrier protein synthase III (FabH) with lauroyl-coenzyme A. J. Mol. Biol. 346 (2005) 1313–1321. [DOI] [PMID: 15713483]
3.  Brown, A.K., Sridharan, S., Kremer, L., Lindenberg, S., Dover, L.G., Sacchettini, J.C. and Besra, G.S. Probing the mechanism of the Mycobacterium tuberculosis β-ketoacyl-acyl carrier protein synthase III mtFabH: factors influencing catalysis and substrate specificity. J. Biol. Chem. 280 (2005) 32539–32547. [DOI] [PMID: 16040614]
4.  Sachdeva, S., Musayev, F.N., Alhamadsheh, M.M., Scarsdale, J.N., Wright, H.T. and Reynolds, K.A. Separate entrance and exit portals for ligand traffic in Mycobacterium tuberculosis FabH. Chem. Biol. 15 (2008) 402–412. [DOI] [PMID: 18420147]
[EC 2.3.1.301 created 2021]
 
 
EC 4.2.1.61      
Deleted entry: 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase. The reaction described is covered by EC 4.2.1.59.
[EC 4.2.1.61 created 1972, deleted 2012]
 
 
EC 2.3.1.68     Relevance: 94.9%
Accepted name: glutamine N-acyltransferase
Reaction: acyl-CoA + L-glutamine = CoA + N-acyl-L-glutamine
Systematic name: acyl-CoA:L-glutamine N-acyltransferase
Comments: Phenylacetyl-CoA and (indol-3-yl)acetyl-CoA, but not benzoyl-CoA, can act as acyl donors. Not identical with EC 2.3.1.13 glycine N-acyltransferase or EC 2.3.1.71 glycine N-benzoyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9030-00-6
References:
1.  Webster, L.T., Jr., Siddiqui, U.A., Lucas, S.V., Strong, J.M. and Mieyal, J.J. Identification of N-acyltransferase activities in mitochondrial fractions from liver of rhesus monkey and man. J. Biol. Chem. 251 (1976) 3352–3358. [PMID: 931988]
[EC 2.3.1.68 created 1984]
 
 
EC 6.2.1.35     Relevance: 94.9%
Accepted name: acetate—[acyl-carrier protein] ligase
Reaction: ATP + acetate + an [acyl-carrier protein] = AMP + diphosphate + an acetyl-[acyl-carrier protein]
For diagram of malonate decarboxylase, click here
Other name(s): HS-acyl-carrier protein:acetate ligase; [acyl-carrier protein]:acetate ligase; MadH; ACP-SH:acetate ligase
Systematic name: acetate:[acyl-carrier-protein] ligase (AMP-forming)
Comments: This enzyme, from the anaerobic bacterium Malonomonas rubra, is a component of the multienzyme complex EC 7.2.4.4, biotin-dependent malonate decarboxylase. The enzyme uses the energy from hydrolysis of ATP to convert the thiol group of the acyl-carrier-protein-bound 2′-(5-phosphoribosyl)-3′-dephospho-CoA cofactor into its acetyl thioester [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hilbi, H., Dehning, I., Schink, B. and Dimroth, P. Malonate decarboxylase of Malonomonas rubra, a novel type of biotin-containing acetyl enzyme. Eur. J. Biochem. 207 (1992) 117–123. [DOI] [PMID: 1628643]
2.  Berg, M., Hilbi, H. and Dimroth, P. The acyl carrier protein of malonate decarboxylase of Malonomonas rubra contains 2′-(5"-phosphoribosyl)-3′-dephosphocoenzyme A as a prosthetic group. Biochemistry 35 (1996) 4689–4696. [DOI] [PMID: 8664258]
3.  Berg, M., Hilbi, H. and Dimroth, P. Sequence of a gene cluster from Malonomonas rubra encoding components of the malonate decarboxylase Na+ pump and evidence for their function. Eur. J. Biochem. 245 (1997) 103–115. [DOI] [PMID: 9128730]
4.  Dimroth, P. and Hilbi, H. Enzymic and genetic basis for bacterial growth on malonate. Mol. Microbiol. 25 (1997) 3–10. [DOI] [PMID: 11902724]
[EC 6.2.1.35 created 2008, modified 2018]
 
 
EC 4.1.1.95     Relevance: 94.9%
Accepted name: L-glutamyl-[BtrI acyl-carrier protein] decarboxylase
Reaction: L-glutamyl-[BtrI acyl-carrier protein] = 4-amino butanoyl-[BtrI acyl-carrier protein] + CO2
Other name(s): btrK (gene name)
Systematic name: L-glutamyl-[BtrI acyl-carrier protein] carboxy-lyase
Comments: Binds pyridoxal 5′-phosphate. Catalyses a step in the biosynthesis of the side chain of the aminoglycoside antibiotics of the butirosin family. Has very low activity with substrates not bound to an acyl-carrier protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Li, Y., Llewellyn, N.M., Giri, R., Huang, F. and Spencer, J.B. Biosynthesis of the unique amino acid side chain of butirosin: possible protective-group chemistry in an acyl carrier protein-mediated pathway. Chem. Biol. 12 (2005) 665–675. [DOI] [PMID: 15975512]
[EC 4.1.1.95 created 2012]
 
 
EC 2.3.1.179     Relevance: 94.8%
Accepted name: β-ketoacyl-[acyl-carrier-protein] synthase II
Reaction: a (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = a (Z)-3-oxooctadec-11-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
Glossary: palmitoleoyl-[acyl-carrier protein] = (Z)-hexadec-9-enoyl-[acyl-carrier protein]
cis-vaccenoyl-[acyl-carrier protein] = (Z)-octadec-11-enoyl-[acyl-carrier protein]
Other name(s): KASII; KAS II; FabF; 3-oxoacyl-acyl carrier protein synthase II; β-ketoacyl-ACP synthase II
Systematic name: (Z)-hexadec-9-enoyl-[acyl-carrier protein]:malonyl-[acyl-carrier protein] C-acyltransferase (decarboxylating)
Comments: Involved in the dissociated (or type II) fatty acid biosynthesis system that occurs in plants and bacteria. While the substrate specificity of this enzyme is very similar to that of EC 2.3.1.41, β-ketoacyl-[acyl-carrier-protein] synthase I, it differs in that palmitoleoyl-[acyl-carrier protein] is not a good substrate of EC 2.3.1.41 but is an excellent substrate of this enzyme [1,2]. The fatty-acid composition of Escherichia coli changes as a function of growth temperature, with the proportion of unsaturated fatty acids increasing with lower growth temperature. This enzyme controls the temperature-dependent regulation of fatty-acid composition, with mutants lacking this acivity being deficient in the elongation of palmitoleate to cis-vaccenate at low temperatures [3,4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 1048648-42-5
References:
1.  D'Agnolo, G., Rosenfeld, I.S. and Vagelos, P.R. Multiple forms of β-ketoacyl-acyl carrier protein synthetase in Escherichia coli. J. Biol. Chem. 250 (1975) 5289–5294. [PMID: 237914]
2.  Garwin, J.L., Klages, A.L. and Cronan, J.E., Jr.. Structural, enzymatic, and genetic studies of β-ketoacyl-acyl carrier protein synthases I and II of Escherichia coli. J. Biol. Chem. 255 (1980) 11949–11956. [PMID: 7002930]
3.  Price, A.C., Rock, C.O. and White, S.W. The 1.3-Angstrom-resolution crystal structure of β-ketoacyl-acyl carrier protein synthase II from Streptococcus pneumoniae. J. Bacteriol. 185 (2003) 4136–4143. [DOI] [PMID: 12837788]
4.  Garwin, J.L., Klages, A.L. and Cronan, J.E., Jr. β-Ketoacyl-acyl carrier protein synthase II of Escherichia coli. Evidence for function in the thermal regulation of fatty acid synthesis. J. Biol. Chem. 255 (1980) 3263–3265. [PMID: 6988423]
5.  Magnuson, K., Carey, M.R. and Cronan, J.E., Jr. The putative fabJ gene of Escherichia coli fatty acid synthesis is the fabF gene. J. Bacteriol. 177 (1995) 3593–3595. [DOI] [PMID: 7768872]
6.  Cronan, J.E., Jr. and Rock, C.O. Biosynthesis of membrane lipids. In: Neidhardt, F.C. (Ed.), Escherichia coli and Salmonella: Cellular and Molecular Biology, 2nd edn, vol. 1, ASM Press, Washington, DC, 1996, pp. 612–636.
[EC 2.3.1.179 created 2006, modified 2020]
 
 
EC 2.3.1.125     Relevance: 94.7%
Accepted name: 1-alkyl-2-acetylglycerol O-acyltransferase
Reaction: acyl-CoA + 1-O-alkyl-2-acetyl-sn-glycerol = CoA + 1-O-alkyl-2-acetyl-3-acyl-sn-glycerol
Other name(s): 1-hexadecyl-2-acetylglycerol acyltransferase
Systematic name: acyl-CoA:1-O-alkyl-2-acetyl-sn-glycerol O-acyltransferase
Comments: A number of acyl-CoAs can act as acyl donor; maximum activity is obtained with linoleoyl-CoA. Not identical with EC 2.3.1.20 diacylglycerol O-acyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 114704-90-4
References:
1.  Kawasaki, T. and Snyder, F. Synthesis of a novel acetylated neutral lipid related to platelet-activating factor by acyl-CoA:1-O-alkyl-2-acetyl-sn-glycerol acyltransferase in HL-60 cells. J. Biol. Chem. 263 (1988) 2593–2596. [PMID: 3422635]
[EC 2.3.1.125 created 1990]
 
 
EC 6.2.1.3     Relevance: 94.5%
Accepted name: long-chain-fatty-acid—CoA ligase
Reaction: ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA
Glossary: a long-chain-fatty acid = a fatty acid with an aliphatic chain of 13-22 carbons.
Other name(s): acyl-CoA synthetase; fatty acid thiokinase (long chain); acyl-activating enzyme; palmitoyl-CoA synthase; lignoceroyl-CoA synthase; arachidonyl-CoA synthetase; acyl coenzyme A synthetase; acyl-CoA ligase; palmitoyl coenzyme A synthetase; thiokinase; palmitoyl-CoA ligase; acyl-coenzyme A ligase; fatty acid CoA ligase; long-chain fatty acyl coenzyme A synthetase; oleoyl-CoA synthetase; stearoyl-CoA synthetase; long chain fatty acyl-CoA synthetase; long-chain acyl CoA synthetase; fatty acid elongase; LCFA synthetase; pristanoyl-CoA synthetase; ACS3; long-chain acyl-CoA synthetase I; long-chain acyl-CoA synthetase II; fatty acyl-coenzyme A synthetase; long-chain acyl-coenzyme A synthetase; FAA1
Systematic name: long-chain fatty acid:CoA ligase (AMP-forming)
Comments: Acts on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. The liver enzyme acts on acids from C6 to C20; that from brain shows high activity up to C24.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9013-18-7
References:
1.  Bakken, A.M. and Farstad, M. Identical subcellular distribution of palmitoyl-CoA and arachidonoyl-CoA synthetase activities in human blood platelets. Biochem. J. 261 (1989) 71–76. [PMID: 2528345]
2.  Hosaka, K., Mishima, M., Tanaka, T., Kamiryo, T. and Numa, S. Acyl-coenzyme-A synthetase I from Candida lipolytica. Purification, properties and immunochemical studies. Eur. J. Biochem. 93 (1979) 197–203. [DOI] [PMID: 108099]
3.  Nagamatsu, K., Soeda, S., Mori, M. and Kishimoto, Y. Lignoceroyl-coenzyme A synthetase from developing rat brain: partial purification, characterization and comparison with palmitoyl-coenzyme A synthetase activity and liver enzyme. Biochim. Biophys. Acta 836 (1985) 80–88. [DOI] [PMID: 3161545]
4.  Tanaka, T., Hosaka, K., Hoshimaru, M. and Numa, S. Purification and properties of long-chain acyl-coenzyme-A synthetase from rat liver. Eur. J. Biochem. 98 (1979) 165–172. [DOI] [PMID: 467438]
[EC 6.2.1.3 created 1961, modified 1989, modified 2011]
 
 
EC 2.3.1.85     Relevance: 93.2%
Accepted name: fatty-acid synthase system
Reaction: acetyl-CoA + n malonyl-CoA + 2n NADPH + 2n H+ = a long-chain fatty acid + (n+1) CoA + n CO2 + 2n NADP+
Glossary: a long-chain-fatty acid = a fatty acid with an aliphatic chain of 13–22 carbons.
Other name(s): FASN (gene name); fatty-acid synthase
Systematic name: acyl-CoA:malonyl-CoA C-acyltransferase (decarboxylating, oxoacyl- and enoyl-reducing and thioester-hydrolysing)
Comments: The animal enzyme is a multi-functional protein catalysing the reactions of EC 2.3.1.38 [acyl-carrier-protein] S-acetyltransferase, EC 2.3.1.39 [acyl-carrier-protein] S-malonyltransferase, EC 2.3.1.41 β-ketoacyl-[acyl-carrier-protein] synthase I, EC 1.1.1.100 3-oxoacyl-[acyl-carrier-protein] reductase, EC 4.2.1.59 3-hydroxyacyl-[acyl-carrier-protein] dehydratase, EC 1.3.1.39 enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific) and EC 3.1.2.14 oleoyl-[acyl-carrier-protein] hydrolase. cf. EC 2.3.1.86, fatty-acyl-CoA synthase system.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9045-77-6
References:
1.  Stoops, J.K., Ross, P., Arslanian, M.J., Aune, K.C., Wakil, S.J. and Oliver, R.M. Physicochemical studies of the rat liver and adipose fatty acid synthetases. J. Biol. Chem. 254 (1979) 7418–7426. [PMID: 457689]
2.  Wakil, S.J., Stoops, J.K. and Joshi, V.C. Fatty acid synthesis and its regulation. Annu. Rev. Biochem. 52 (1983) 537–579. [DOI] [PMID: 6137188]
[EC 2.3.1.85 created 1984, modified 2019]
 
 
EC 2.3.1.198     Relevance: 93.1%
Accepted name: glycerol-3-phosphate 2-O-acyltransferase
Reaction: an acyl-CoA + sn-glycerol 3-phosphate = CoA + a 2-acyl-sn-glycerol 3-phosphate
Other name(s): sn-2-glycerol-3-phosphate O-acyltransferase; glycerol-3-phosphate O-acyltransferase (ambiguous)
Systematic name: acyl-CoA:sn-glycerol 3-phosphate 2-O-acyltransferase
Comments: A membrane-associated enzyme required for suberin or cutin synthesis in plants. Active with a wide range of acyl-CoA substrates (C16:0-C24:0). The enzyme from some sources has much higher activity with ω-oxidized acyl-CoAs. Some enzymes are bifunctional and have an additional phosphatase activity producing sn-2-monoacylglycerols.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Yang, W., Pollard, M., Li-Beisson, Y., Beisson, F., Feig, M. and Ohlrogge, J. A distinct type of glycerol-3-phosphate acyltransferase with sn-2 preference and phosphatase activity producing 2-monoacylglycerol. Proc. Natl. Acad. Sci. USA 107 (2010) 12040–12045. [DOI] [PMID: 20551224]
[EC 2.3.1.198 created 2012]
 
 
EC 1.2.1.50     Relevance: 93%
Accepted name: long-chain acyl-protein thioester reductase
Reaction: a long-chain aldehyde + [protein]-L-cysteine + NADP+ = a [protein]-S-(long-chain fatty acyl)-L-cysteine + NADPH + H+
Other name(s): luxC (gene name); acyl-CoA reductase; acyl coenzyme A reductase; long-chain-aldehyde:NADP+ oxidoreductase (acyl-CoA-forming); long-chain-fatty-acyl-CoA reductase
Systematic name: long-chain-aldehyde:NADP+ oxidoreductase (protein thioester-forming)
Comments: Together with a hydrolase component (EC 3.1.2.2 and EC 3.1.2.14) and a synthetase component (EC 6.2.1.19), this enzyme forms a multienzyme fatty acid reductase complex that produces the long-chain aldehyde substrate of the bacterial luciferase enzyme (EC 1.14.14.3). The enzyme is acylated by receiving an acyl group from EC 6.2.1.19, and catalyses the reduction of the acyl group, releasing the aldehyde product. The enzyme is also able to accept the acyl group from a long-chain acyl-CoA.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 50936-56-6
References:
1.  Riendeau, D., Rodrigues, A. and Meighen, E. Resolution of the fatty acid reductase from Photobacterium phosphoreum into acyl protein synthetase and acyl-CoA reductase activities. Evidence for an enzyme complex. J. Biol. Chem. 257 (1982) 6908–6915. [PMID: 7085612]
2.  Wall, L. and Meighen, E.A. Subunit structure of the fatty-acid reductase complex from Photobacterium phosphoreum. Biochemistry 25 (1986) 4315–4321.
3.  Lin, J.W., Chao, Y.F. and Weng, S.F. Nucleotide sequence of the luxC gene encoding fatty acid reductase of the lux operon from Photobacterium leiognathi. Biochem. Biophys. Res. Commun. 191 (1993) 314–318. [DOI] [PMID: 8447834]
[EC 1.2.1.50 created 1986, modified 2016]
 
 
EC 2.3.1.86     Relevance: 92.7%
Accepted name: fatty-acyl-CoA synthase system
Reaction: acetyl-CoA + n malonyl-CoA + 2n NADPH + 4n H+ = long-chain-acyl-CoA + n CoA + n CO2 + 2n NADP+
Other name(s): yeast fatty acid synthase; FAS1 (gene name); FAS2 (gene name); fatty-acyl-CoA synthase
Systematic name: acyl-CoA:malonyl-CoA C-acyltransferase (decarboxylating, oxoacyl- and enoyl-reducing)
Comments: The enzyme from yeasts (Ascomycota and Basidiomycota) is a multi-functional protein complex composed of two subunits. One subunit catalyses the reactions EC 1.1.1.100, 3-oxoacyl-[acyl-carrier-protein] reductase and EC 2.3.1.41, β-ketoacyl-[acyl-carrier-protein] synthase I, while the other subunit catalyses the reactions of EC 2.3.1.38, [acyl-carrier-protein] S-acetyltransferase, EC 2.3.1.39, [acyl-carrier-protein] S-malonyltransferase, EC 4.2.1.59, 3-hydroxyacyl-[acyl-carrier-protein] dehydratase, EC 1.3.1.10, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and EC 1.1.1.279, (R)-3-hydroxyacid-ester dehydrogenase. The enzyme system differs from the animal system (EC 2.3.1.85, fatty-acid synthase system) in that the enoyl reductase domain requires FMN as a cofactor, and the ultimate product is an acyl-CoA (usually palmitoyl-CoA) instead of a free fatty acid.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 94219-29-1
References:
1.  Schweitzer, E., Kniep, B., Castorph, H. and Holzner, U. Pantetheine-free mutants of the yeast fatty-acid-synthetase complex. Eur. J. Biochem. 39 (1973) 353–362. [DOI] [PMID: 4590449]
2.  Wakil, S.J., Stoops, J.K. and Joshi, V.C. Fatty acid synthesis and its regulation. Annu. Rev. Biochem. 52 (1983) 537–579. [DOI] [PMID: 6137188]
3.  Tehlivets, O., Scheuringer, K. and Kohlwein, S.D. Fatty acid synthesis and elongation in yeast. Biochim. Biophys. Acta 1771 (2007) 255–270. [DOI] [PMID: 16950653]
[EC 2.3.1.86 created 1984, modified 2003, modified 2013, modified 2019]
 
 
EC 2.3.1.314     Relevance: 92.7%
Accepted name: phytol O-acyltransferase
Reaction: an acyl-CoA + phytol = a fatty acid phytyl ester + CoA
Other name(s): phytyl ester synthase; PES1 (gene name); PES2 (gene name); slr2103 (locus name)
Systematic name: acyl-CoA:phytol O-acyltransferase
Comments: The enzyme is found in plant chloroplasts and cyanobacteria. The plant enzyme can also employ acyl carrier proteins and galactolipids as acyl donors, while the enzyme from the cyanobacterium Synechocystis sp. PCC 6803 only uses acyl-CoAs. The enzyme also catalyses the activity of EC 2.3.1.20, diacylglycerol O-acyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ischebeck, T., Zbierzak, A.M., Kanwischer, M. and Dormann, P. A salvage pathway for phytol metabolism in Arabidopsis. J. Biol. Chem. 281 (2006) 2470–2477. [DOI] [PMID: 16306049]
2.  Lippold, F., vom Dorp, K., Abraham, M., Holzl, G., Wewer, V., Yilmaz, J.L., Lager, I., Montandon, C., Besagni, C., Kessler, F., Stymne, S. and Dormann, P. Fatty acid phytyl ester synthesis in chloroplasts of Arabidopsis. Plant Cell 24 (2012) 2001–2014. [DOI] [PMID: 22623494]
3.  Aizouq, M., Peisker, H., Gutbrod, K., Melzer, M., Holzl, G. and Dormann, P. Triacylglycerol and phytyl ester synthesis in Synechocystis sp. PCC6803. Proc. Natl. Acad. Sci. USA 117 (2020) 6216–6222. [DOI] [PMID: 32123083]
4.  Tanaka, M., Ishikawa, T., Tamura, S., Saito, Y., Kawai-Yamada, M. and Hihara, Y. Quantitative and qualitative analyses of triacylglycerol production in the wild-type Cyanobacterium Synechocystis sp. PCC 6803 and the strain expressing AtfA from Acinetobacter baylyi ADP1. Plant Cell Physiol. 61 (2020) 1537–1547. [DOI] [PMID: 32433767]
[EC 2.3.1.314 created 2024]
 
 
EC 6.2.1.20     Relevance: 92.6%
Accepted name: long-chain-fatty-acid—[acyl-carrier-protein] ligase
Reaction: ATP + a long-chain fatty acid + an [acyl-carrier protein] = AMP + diphosphate + a long-chain acyl-[acyl-carrier protein]
Other name(s): acyl-[acyl-carrier-protein] synthetase (ambiguous); acyl-ACP synthetase (ambiguous); stearoyl-ACP synthetase; acyl-acyl carrier protein synthetase (ambiguous); long-chain-fatty-acid:[acyl-carrier-protein] ligase (AMP-forming)
Systematic name: long-chain-fatty-acid:[acyl-carrier protein] ligase (AMP-forming)
Comments: The enzyme ligates long chain fatty acids (with aliphatic chain of 13-22 carbons) to an acyl-carrier protein. Not identical with EC 6.2.1.3 long-chain-fatty-acid—CoA ligase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 77322-37-3
References:
1.  Ray, T.K. and Cronan, J.E., Jr. Activation of long chain fatty acids with acyl carrier protein: demonstration of a new enzyme, acyl-acyl carrier protein synthetase, in Escherichia coli. Proc. Natl. Acad. Sci. USA 73 (1976) 4374–4378. [DOI] [PMID: 794875]
2.  Kaczmarzyk, D. and Fulda, M. Fatty acid activation in cyanobacteria mediated by acyl-acyl carrier protein synthetase enables fatty acid recycling. Plant Physiol. 152 (2010) 1598–1610. [DOI] [PMID: 20061450]
[EC 6.2.1.20 created 1986]
 
 
EC 1.3.8.1     Relevance: 92.5%
Accepted name: short-chain acyl-CoA dehydrogenase
Reaction: a short-chain acyl-CoA + electron-transfer flavoprotein = a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein
Glossary: a short-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains less than 6 carbon atoms.
Other name(s): butyryl-CoA dehydrogenase; butanoyl-CoA dehydrogenase; butyryl dehydrogenase; unsaturated acyl-CoA reductase; ethylene reductase; enoyl-coenzyme A reductase; unsaturated acyl coenzyme A reductase; butyryl coenzyme A dehydrogenase; short-chain acyl CoA dehydrogenase; short-chain acyl-coenzyme A dehydrogenase; 3-hydroxyacyl CoA reductase; butanoyl-CoA:(acceptor) 2,3-oxidoreductase; ACADS (gene name).
Systematic name: short-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase
Comments: Contains a tightly-bound FAD cofactor. One of several enzymes that catalyse the first step in fatty acids β-oxidation. The enzyme catalyses the oxidation of saturated short-chain acyl-CoA thioesters to give a trans 2,3-unsaturated product by removal of the two pro-R-hydrogen atoms. The enzyme from beef liver accepts substrates with acyl chain lengths of 3 to 8 carbon atoms. The highest activity was reported with either butanoyl-CoA [2] or pentanoyl-CoA [4]. The enzyme from rat has only 10% activity with hexanoyl-CoA (compared to butanoyl-CoA) and no activity with octanoyl-CoA [6]. cf. EC 1.3.8.7, medium-chain acyl-CoA dehydrogenase, EC 1.3.8.8, long-chain acyl-CoA dehydrogenase, and EC 1.3.8.9, very-long-chain acyl-CoA dehydrogenase.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9027-88-7
References:
1.  Mahler, H.R. Studies on the fatty acid oxidizing system of animal tissue. IV. The prosthetic group of butyryl coenzyme A dehydrogenase. J. Biol. Chem. 206 (1954) 13–26. [PMID: 13130522]
2.  Green, D.E., Mii, S., Mahler, H.R. and Bock, R.M. Studies on the fatty acid oxidizing system of animal tissue. III. Butyryl coenzyme A dehydrogenase. J. Biol. Chem. 206 (1954) 1–12. [PMID: 13130521]
3.  Beinert, H. Acyl coenzyme A dehydrogenase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 447–466.
4.  Shaw, L. and Engel, P.C. The purification and properties of ox liver short-chain acyl-CoA dehydrogenase. Biochem. J. 218 (1984) 511–520. [PMID: 6712627]
5.  Thorpe, C. and Kim, J.J. Structure and mechanism of action of the acyl-CoA dehydrogenases. FASEB J. 9 (1995) 718–725. [PMID: 7601336]
6.  Ikeda, Y., Ikeda, K.O. and Tanaka, K. Purification and characterization of short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria. Isolation of the holo- and apoenzymes and conversion of the apoenzyme to the holoenzyme. J. Biol. Chem. 260 (1985) 1311–1325. [PMID: 3968063]
7.  McMahon, B., Gallagher, M.E. and Mayhew, S.G. The protein coded by the PP2216 gene of Pseudomonas putida KT2440 is an acyl-CoA dehydrogenase that oxidises only short-chain aliphatic substrates. FEMS Microbiol. Lett. 250 (2005) 121–127. [DOI] [PMID: 16024185]
[EC 1.3.8.1 created 1961 as EC 1.3.2.1, transferred 1964 to EC 1.3.99.2, transferred 2011 to EC 1.3.8.1, modified 2012]
 
 
EC 3.1.2.18     Relevance: 92.1%
Accepted name: ADP-dependent short-chain-acyl-CoA hydrolase
Reaction: acyl-CoA + H2O = CoA + a carboxylate
Other name(s): short-chain acyl coenzyme A hydrolase; propionyl coenzyme A hydrolase; propionyl-CoA hydrolase; propionyl-CoA thioesterase; short-chain acyl-CoA hydrolase; short-chain acyl-CoA thioesterase
Systematic name: ADP-dependent-short-chain-acyl-CoA hydrolase
Comments: Requires ADP; inhibited by NADH. Maximum activity is shown with propanoyl-CoA.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 117698-16-5
References:
1.  Alexson, S.E.H. and Nedergaard, J. A novel type of short- and medium-chain acyl-CoA hydrolases in brown adipose tissue mitochondria. J. Biol. Chem. 263 (1988) 13564–13571. [PMID: 2901416]
2.  Alexson, S.E.H., Svensson, L.T. and Nedergaard, J. NADH-sensitive propionyl-CoA hydrolase in brown-adipose-tissue mitochondria of the rat. Biochim. Biophys. Acta 1005 (1989) 13–19. [DOI] [PMID: 2570608]
[EC 3.1.2.18 created 1992]
 
 
EC 2.3.1.22     Relevance: 91.8%
Accepted name: 2-acylglycerol O-acyltransferase
Reaction: acyl-CoA + 2-acylglycerol = CoA + diacylglycerol
Other name(s): acylglycerol palmitoyltransferase; monoglyceride acyltransferase; acyl coenzyme A-monoglyceride acyltransferase; monoacylglycerol acyltransferase
Systematic name: acyl-CoA:2-acylglycerol O-acyltransferase
Comments: Various 2-acylglycerols can act as acceptor; palmitoyl-CoA and other long-chain acyl-CoAs can act as donors. The sn-1 position and the sn-3 position are both acylated, at about the same rate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9055-17-8
References:
1.  Manganaro, F. and Kuksis, A. Purification and preliminary characterization of 2-monoacylglycerol acyltransferase from rat intestinal villus cells. Can. J. Biochem. Cell Biol. 63 (1985) 341–347. [DOI] [PMID: 4016575]
[EC 2.3.1.22 created 1972, modified 1986, modified 1989]
 
 
EC 1.3.99.13      
Transferred entry: long-chain-acyl-CoA dehydrogenase. Now EC 1.3.8.8, long-chain-acyl-CoA dehydrogenase
[EC 1.3.99.13 created 1989, deleted 2012]
 
 
EC 2.3.1.121     Relevance: 91.2%
Accepted name: 1-alkenylglycerophosphoethanolamine O-acyltransferase
Reaction: acyl-CoA + 1-alkenylglycerophosphoethanolamine = CoA + 1-alkenyl-2-acylglycerophosphoethanolamine
Systematic name: acyl-CoA:1-alkenylglycerophosphoethanolamine O-acyltransferase
Comments: Long-chain unsaturated acyl-CoAs are the best substrates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 112445-17-7
References:
1.  Arthur, G., Page, L. and Choy, P.C. Acylation of 1-alkenylglycerophosphoethanolamine and 1-acylglycerophosphoethanolamine in guinea-pig heart microsomes. Biochim. Biophys. Acta 921 (1987) 259–265. [DOI] [PMID: 3651487]
[EC 2.3.1.121 created 1990]
 
 
EC 6.7.1.2     Relevance: 91.1%
Accepted name: 3-aminoavenalumate diazotase
Reaction: ATP + 3-aminoavenalumate + nitrite = AMP + diphosphate + 3-diazoavenalumate + H2O
Glossary: 3-aminoavenalumate = (2E,4E)-5-(3-amino-4-hydroxyphenyl)penta-2,4-dienoate
3-diazoavenalumate = 1-{3-[(1E,3E)-4-carboxylatobuta-1,3-dien-1-yl]-6-oxocyclohexa-2,4-dien-1-ylidene}diazenium
Other name(s): avaA6 (gene name)
Systematic name: 3-aminoavenalumate:nitrite ligase (AMP-forming)
Comments: The enzyme, characterized from the bacterium Streptomyces sp. RI-77, participates in the biosynthesis of avenalumate, a phenolic acid originally described from oat (Avena sativa). It can also act on 3-aminocoumarate and 3-amino-4-hydroxybenzoate with lower activity.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kawai, S., Hagihara, R., Shin-Ya, K., Katsuyama, Y. and Ohnishi, Y. Bacterial avenalumic acid biosynthesis includes substitution of an aromatic amino group for hydride by nitrous acid dependent diazotization. Angew. Chem. Int. Ed. Engl. 61 (2022) e202211728. [DOI] [PMID: 36115045]
[EC 6.7.1.2 created 2023]
 
 
EC 2.3.1.294     Relevance: 91.1%
Accepted name: meromycolic acid 3-oxoacyl-(acyl carrier protein) synthase II
Reaction: an ultra-long-chain di-unsaturated acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = an ultra-long-chain di-unsaturated 3-oxo-fatty acyl-[acyl-carrier protein] + CO2 + a holo-[acyl-carrier protein]
Other name(s): kasB (gene name); β-ketoacyl-acyl carrier protein synthase KasB
Systematic name: ultra-long-chain di-unsaturated fattyl acyl-[acyl-carrier protein]:malonyl-[acyl-carrier protein] C-acyltransferase (decarboxylating)
Comments: The enzyme is part of the fatty acid synthase (FAS) II system of mycobacteria, which extends modified products of the FAS I system, eventually forming meromycolic acids that are incorporated into mycolic acids. Meromycolic acids consist of a long chain, typically 50-60 carbons, which is functionalized by different groups.Two 3-oxoacyl-(acyl carrier protein) synthases function within the FAS II system, encoded by the kasA and kasB genes. The two enzymes share some sequence identity but function independently on separate sets of substrates. KasB differs from KasA (EC 2.3.1.293, meromycolic acid 3-oxoacyl-(acyl carrier protein) synthase I), by preferring longer substrates (closer to the upper limit), which also contain two double bonds.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Schaeffer, M.L., Agnihotri, G., Volker, C., Kallender, H., Brennan, P.J. and Lonsdale, J.T. Purification and biochemical characterization of the Mycobacterium tuberculosis β-ketoacyl-acyl carrier protein synthases KasA and KasB. J. Biol. Chem. 276 (2001) 47029–47037. [PMID: 11600501]
2.  Gao, L.Y., Laval, F., Lawson, E.H., Groger, R.K., Woodruff, A., Morisaki, J.H., Cox, J.S., Daffe, M. and Brown, E.J. Requirement for kasB in Mycobacterium mycolic acid biosynthesis, cell wall impermeability and intracellular survival: implications for therapy. Mol. Microbiol. 49 (2003) 1547–1563. [PMID: 12950920]
3.  Molle, V., Brown, A.K., Besra, G.S., Cozzone, A.J. and Kremer, L. The condensing activities of the Mycobacterium tuberculosis type II fatty acid synthase are differentially regulated by phosphorylation. J. Biol. Chem. 281 (2006) 30094–30103. [PMID: 16873379]
4.  Bhatt, A., Fujiwara, N., Bhatt, K., Gurcha, S.S., Kremer, L., Chen, B., Chan, J., Porcelli, S.A., Kobayashi, K., Besra, G.S. and Jacobs, W.R., Jr. Deletion of kasB in Mycobacterium tuberculosis causes loss of acid-fastness and subclinical latent tuberculosis in immunocompetent mice. Proc. Natl. Acad. Sci. USA 104 (2007) 5157–5162. [PMID: 17360388]
5.  Yamada, H., Bhatt, A., Danev, R., Fujiwara, N., Maeda, S., Mitarai, S., Chikamatsu, K., Aono, A., Nitta, K., Jacobs, W.R., Jr. and Nagayama, K. Non-acid-fastness in Mycobacterium tuberculosis Δ kasB mutant correlates with the cell envelope electron density. Tuberculosis (Edinb) 92 (2012) 351–357. [PMID: 22516756]
6.  Vilcheze, C., Molle, V., Carrere-Kremer, S., Leiba, J., Mourey, L., Shenai, S., Baronian, G., Tufariello, J., Hartman, T., Veyron-Churlet, R., Trivelli, X., Tiwari, S., Weinrick, B., Alland, D., Guerardel, Y., Jacobs, W.R., Jr. and Kremer, L. Phosphorylation of KasB regulates virulence and acid-fastness in Mycobacterium tuberculosis. PLoS Pathog. 10:e1004115 (2014). [PMID: 24809459]
[EC 2.3.1.294 created 2019]
 
 
EC 1.14.19.78     Relevance: 90.9%
Accepted name: decanoyl-[acyl-carrier protein] acetylenase
Reaction: decanoyl-[acyl-carrier protein] + 4 reduced ferredoxin [iron-sulfur] cluster + 2 O2 + 4 H+ = dec-9-ynoyl-[acyl-carrier protein] + 4 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O (overall reaction)
(1a) decanoyl-[acyl-carrier protein] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = dec-9-enoyl-[acyl-carrier protein] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
(1b) dec-9-enoyl-[acyl-carrier protein] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = dec-9-ynoyl-[acyl-carrier protein] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
Other name(s): ttuB (gene name) (ambiguous)
Systematic name: decanoyl-[acyl-carrier protein],reduced ferredoxin:oxygen oxidoreductase (9,10-dehydrogenating)
Comments: The enzyme, characterized from the bacterium Teredinibacter turnerae, is specific for decanoyl-[acyl-carrier protein]. Activity is maximal when decanoate is loaded onto a dedicated acyl-carrier protein (TtuC), which is encoded by a gene in the same operon.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Zhu, X., Su, M., Manickam, K. and Zhang, W. Bacterial genome mining of enzymatic tools for alkyne biosynthesis. ACS Chem. Biol. 10 (2015) 2785–2793. [DOI] [PMID: 26441143]
[EC 1.14.19.78 created 2021]
 
 
EC 2.3.1.62     Relevance: 90.8%
Accepted name: 2-acylglycerophosphocholine O-acyltransferase
Reaction: acyl-CoA + 2-acyl-sn-glycero-3-phosphocholine = CoA + phosphatidylcholine
Other name(s): 2-acylglycerol-3-phosphorylcholine acyltransferase; 2-acylglycerophosphocholine acyltransferase
Systematic name: acyl-CoA:2-acyl-sn-glycero-3-phosphocholine O-acyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 64295-73-4
References:
1.  Lands, W.E.M. and Hart, P. Metabolism of glycerolipids. VI. Specificities of acyl coenzyme A:phospholipid acyltransferases. J. Biol. Chem. 240 (1965) 1905–1911. [PMID: 14299609]
2.  van den Bosch, H., van Golde, L.M.G., Slotboom, A.J. and van Deenen, L.L.M. The acylation of isomeric monoacyl phosphatidylcholines. Biochim. Biophys. Acta 152 (1968) 694–703. [DOI] [PMID: 5660084]
[EC 2.3.1.62 created 1978]
 
 
EC 2.3.1.15     Relevance: 90.7%
Accepted name: glycerol-3-phosphate 1-O-acyltransferase
Reaction: acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate
Other name(s): α-glycerophosphate acyltransferase; 3-glycerophosphate acyltransferase; ACP:sn-glycerol-3-phosphate acyltransferase; glycerol 3-phosphate acyltransferase; glycerol phosphate acyltransferase; glycerol phosphate transacylase; glycerophosphate acyltransferase; glycerophosphate transacylase; sn-glycerol 3-phosphate acyltransferase; sn-glycerol-3-phosphate acyltransferase; glycerol-3-phosphate O-acyltransferase (ambiguous)
Systematic name: acyl-CoA:sn-glycerol-3-phosphate 1-O-acyltransferase
Comments: Acyl-[acyl-carrier protein] can also act as acyl donor. The enzyme acts only on derivatives of fatty acids of chain length larger than C10.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9029-96-3
References:
1.  Bertrams, M. and Heinz, E. Positional specificity and fatty-acid selectivity of purified sn-glycerol 3-phosphate acyltransferases from chloroplasts. Plant Physiol. 68 (1981) 653–657. [PMID: 16661974]
2.  Frentzen, M., Heinz, E., McKeon, T.A. and Stumpf, P.K. Specificities and selectivities of glycerol-3-phosphate acyltransferase and monoacylglycerol-3-phosphate acyltransferase from pea and spinach chloroplasts. Eur. J. Biochem. 129 (1983) 629–636. [DOI] [PMID: 6825679]
3.  Green, P.R., Merrill, A.H. and Bell, R.M. Membrane phospholipid synthesis in Escherichia coli. Purification, reconstitution, and characterization of sn-glycerol-3-phosphate acyltransferase. J. Biol. Chem. 256 (1981) 11151–11159. [PMID: 6350296]
4.  Yamashita, S. and Numa, N. Partial purification and properties of glycerophosphate acyltransferase from rat liver. Formation of 1-acylglycerol 3-phosphate from sn-glycerol 3-phosphate and palmityl coenzyme A. Eur. J. Biochem. 31 (1972) 565–573. [DOI] [PMID: 4650158]
[EC 2.3.1.15 created 1961, modified 1976, modified 1990]
 
 
EC 2.1.1.41     Relevance: 90.6%
Accepted name: sterol 24-C-methyltransferase
Reaction: S-adenosyl-L-methionine + 5α-cholesta-8,24-dien-3β-ol = S-adenosyl-L-homocysteine + 24-methylene-5α-cholest-8-en-3β-ol
For diagram of sterol sidechain modification, click here
Glossary: desmosterol = cholesta-5,24-dien-3β-ol
zymostrol = 5α-cholesta-8,24-dien-3β-ol
Other name(s): Δ24-methyltransferase; Δ24-sterol methyltransferase; zymosterol-24-methyltransferase; S-adenosyl-4-methionine:sterol Δ24-methyltransferase; SMT1; 24-sterol C-methyltransferase; S-adenosyl-L-methionine:Δ24(23)-sterol methyltransferase; phytosterol methyltransferase
Systematic name: S-adenosyl-L-methionine:zymosterol 24-C-methyltransferase
Comments: Requires glutathione. Acts on a range of sterols with a 24(25)-double bond in the sidechain. While zymosterol is the preferred substrate it also acts on desmosterol, 5α-cholesta-7,24-dien-3β-ol, 5α-cholesta-5,7,24-trien-3β-ol, 4α-methylzymosterol and others. S-Adenosyl-L-methionine attacks the Si-face of the 24(25) double bond and the C-24 hydrogen is transferred to C-25 on the Re face of the double bond.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37257-07-1
References:
1.  Moore, J.T., Jr. and Gaylor, J.L. Isolation and purification of an S-adenosylmethionine: Δ24-sterol methyltransferase from yeast. J. Biol. Chem. 244 (1969) 6334–6340. [PMID: 5354959]
2.  Venkatramesh, M., Guo, D., Jia, Z. and Nes, W.D. Mechanism and structural requirements for transformations of substrates by the S-adenosyl-L-methionine:Δ24(25)-sterol methyl transferase enzyme from Saccharomyces cerevisiae. Biochim. Biophys. Acta 1299 (1996) 313–324. [DOI] [PMID: 8597586]
3.  Tong, Y., McCourt, B.S., Guo, D., Mangla, A.T., Zhou, W.X., Jenkins, M.D., Zhou, W., Lopez, M. and Nes, W.D. , Stereochemical features of C-methylation on the path to Δ24(28)-methylene and Δ24(28)-ethylidene sterols: studies on the recombinant phytosterol methyl transferase from Arabidopsis thaliana. Tetrahedron Lett. 38 (1997) 6115–6118.
4.  Bouvier-Navé, P., Husselstein, T. and Benveniste, P. Two families of sterol methyltransferases are involved in the first and the second methylation steps of plant biosynthesis. Eur. J. Biochem. 256 (1998) 88–96. [DOI] [PMID: 9746350]
5.  Nes, W.D., McCourt, B.S., Zhou, W., Ma, J., Marshall, J.A., Peek, L.A. and Brennan, M. Overexpression, purification, and stereochemical studies of the recombinant S-adenosyl-L-methionine:Δ24(25)- to Δ24(28)-sterol methyl transferase enzyme from Saccharomyces cerevisiae sterol methyl transferase. Arch. Biochem. Biophys. 353 (1998) 297–311. [DOI] [PMID: 9606964]
[EC 2.1.1.41 created 1972, modified 2001]
 
 
EC 2.3.1.278     Relevance: 90.5%
Accepted name: mycolipenoyl-CoA—2-(long-chain-fatty acyl)-trehalose mycolipenoyltransferase
Reaction: a mycolipenoyl-CoA + a 2-(long-chain-fatty acyl)-trehalose = a 2-(long-chain-fatty acyl)-3-mycolipenoyl-trehalose + CoA
Glossary: a mycolipenoyl-CoA = a (2E,2S,4S,6S)-2,4,6-trimethyl-2-enoyl-CoA
polyacyltrehalose = PAT = a 2-(long-chain-fatty acyl)-2′,3,4′,6-tetramycolipenoyl-trehalose
Other name(s): papA3 (gene name)
Systematic name: mycolipenoyl-CoA:2-(long-chain-fatty acyl)-trehalose 3-mycolipenoyltransferase
Comments: The enzyme, characterized from the bacterium Mycobacterium tuberculosis, participates in the biosynthesis of polyacyltrehalose (PAT), a pentaacylated, trehalose-based glycolipid found in the cell wall of pathogenic strains. The enzyme catalyses two successive activities - it first transfers an acyl (often palmitoyl) group to position 2 (see EC 2.3.1.279, long-chain-acyl-CoA—trehalose acyltransferase), followed by the transfer of a mycolipenyl group to position 3.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hatzios, S.K., Schelle, M.W., Holsclaw, C.M., Behrens, C.R., Botyanszki, Z., Lin, F.L., Carlson, B.L., Kumar, P., Leary, J.A. and Bertozzi, C.R. PapA3 is an acyltransferase required for polyacyltrehalose biosynthesis in Mycobacterium tuberculosis. J. Biol. Chem. 284 (2009) 12745–12751. [PMID: 19276083]
[EC 2.3.1.278 created 2018]
 
 
EC 2.3.1.187     Relevance: 90.3%
Accepted name: acetyl-S-ACP:malonate ACP transferase
Reaction: an acetyl-[acyl-carrier protein] + malonate = a malonyl-[acyl-carrier protein] + acetate
For diagram of malonate decarboxylase, click here
Other name(s): acetyl-S-ACP:malonate ACP-SH transferase; acetyl-S-acyl-carrier protein:malonate acyl-carrier-protein-transferase; MdcA; MadA; ACP transferase; malonate/acetyl-CoA transferase; malonate:ACP transferase; acetyl-S-acyl carrier protein:malonate acyl carrier protein-SH transferase
Systematic name: acetyl-[acyl-carrier-protein]:malonate S-[acyl-carrier-protein]transferase
Comments: This is the first step in the catalysis of malonate decarboxylation and involves the exchange of an acetyl thioester residue bound to the activated acyl-carrier protein (ACP) subunit of the malonate decarboxylase complex for a malonyl thioester residue [2]. This enzyme forms the α subunit of the multienzyme complexes biotin-independent malonate decarboxylase (EC 4.1.1.88) and biotin-dependent malonate decarboxylase (EC 7.2.4.4). The enzyme can also use acetyl-CoA as a substrate but more slowly [4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hilbi, H. and Dimroth, P. Purification and characterization of a cytoplasmic enzyme component of the Na+-activated malonate decarboxylase system of Malonomonas rubra: acetyl-S-acyl carrier protein: malonate acyl carrier protein-SH transferase. Arch. Microbiol. 162 (1994) 48–56. [PMID: 18251085]
2.  Hoenke, S., Schmid, M. and Dimroth, P. Sequence of a gene cluster from Klebsiella pneumoniae encoding malonate decarboxylase and expression of the enzyme in Escherichia coli. Eur. J. Biochem. 246 (1997) 530–538. [DOI] [PMID: 9208947]
3.  Koo, J.H. and Kim, Y.S. Functional evaluation of the genes involved in malonate decarboxylation by Acinetobacter calcoaceticus. Eur. J. Biochem. 266 (1999) 683–690. [DOI] [PMID: 10561613]
4.  Chohnan, S., Akagi, K. and Takamura, Y. Functions of malonate decarboxylase subunits from Pseudomonas putida. Biosci. Biotechnol. Biochem. 67 (2003) 214–217. [DOI] [PMID: 12619701]
5.  Dimroth, P. and Hilbi, H. Enzymic and genetic basis for bacterial growth on malonate. Mol. Microbiol. 25 (1997) 3–10. [DOI] [PMID: 11902724]
[EC 2.3.1.187 created 2008, modified 2018]
 
 


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