The Enzyme Database

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EC 1.1.1.100     
Accepted name: 3-oxoacyl-[acyl-carrier-protein] reductase
Reaction: a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+ = a 3-oxoacyl-[acyl-carrier protein] + NADPH + H+
Other name(s): β-ketoacyl-[acyl-carrier protein](ACP) reductase; β-ketoacyl acyl carrier protein (ACP) reductase; β-ketoacyl reductase; β-ketoacyl thioester reductase; β-ketoacyl-ACP reductase; β-ketoacyl-acyl carrier protein reductase; 3-ketoacyl acyl carrier protein reductase; NADPH-specific 3-oxoacyl-[acylcarrier protein]reductase; 3-oxoacyl-[ACP]reductase; (3R)-3-hydroxyacyl-[acyl-carrier-protein]:NADP+ oxidoreductase
Systematic name: (3R)-3-hydroxyacyl-[acyl-carrier protein]:NADP+ oxidoreductase
Comments: Exhibits a marked preference for acyl-carrier-protein derivatives over CoA derivatives as substrates.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 37250-34-3
References:
1.  Prescott, D.J. and Vagelos, P.R. Acyl carrier protein. Adv. Enzymol. Relat. Areas Mol. Biol. 36 (1972) 269–311. [DOI] [PMID: 4561013]
2.  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]
3.  Toomey, R.E. and Wakil, S.J. Studies on the mechanism of fatty acid synthesis. XV. Preparation and general properties of β-ketoacyl acyl carrier protein reductase from Escherichia coli. Biochim. Biophys. Acta 116 (1966) 189–197. [DOI] [PMID: 4381013]
[EC 1.1.1.100 created 1972, modified 1976]
 
 
EC 1.1.1.212     
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 1.1.1.330     
Accepted name: very-long-chain 3-oxoacyl-CoA reductase
Reaction: a very-long-chain (3R)-3-hydroxyacyl-CoA + NADP+ = a very-long-chain 3-oxoacyl-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): very-long-chain 3-ketoacyl-CoA reductase; very-long-chain β-ketoacyl-CoA reductase; KCR (gene name); IFA38 (gene name)
Systematic name: (3R)-3-hydroxyacyl-CoA:NADP+ oxidoreductase
Comments: The second 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. The enzyme is active with substrates with chain length of C16 to C34, depending on the species. cf. EC 2.3.1.199, very-long-chain 3-oxoacyl-CoA synthase, EC 4.2.1.134, very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] dehydratase, and EC 1.3.1.93, very-long-chain enoyl-CoA reductase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Beaudoin, F., Gable, K., Sayanova, O., Dunn, T. and Napier, J.A. A Saccharomyces cerevisiae gene required for heterologous fatty acid elongase activity encodes a microsomal β-keto-reductase. J. Biol. Chem. 277 (2002) 11481–11488. [DOI] [PMID: 11792704]
2.  Han, G., Gable, K., Kohlwein, S.D., Beaudoin, F., Napier, J.A. and Dunn, T.M. The Saccharomyces cerevisiae YBR159w gene encodes the 3-ketoreductase of the microsomal fatty acid elongase. J. Biol. Chem. 277 (2002) 35440–35449. [DOI] [PMID: 12087109]
3.  Beaudoin, F., Wu, X., Li, F., Haslam, R.P., Markham, J.E., Zheng, H., Napier, J.A. and Kunst, L. Functional characterization of the Arabidopsis β-ketoacyl-coenzyme A reductase candidates of the fatty acid elongase. Plant Physiol. 150 (2009) 1174–1191. [DOI] [PMID: 19439572]
[EC 1.1.1.330 created 2012]
 
 
EC 1.2.1.80     
Accepted name: long-chain acyl-[acyl-carrier-protein] reductase
Reaction: a long-chain aldehyde + an [acyl-carrier protein] + NAD(P)+ = a long-chain acyl-[acyl-carrier protein] + NAD(P)H + H+
Glossary: a long-chain aldehyde = an aldehyde derived from a fatty acid with an aliphatic chain of 13-22 carbons.
an [acyl-carrier protein] = ACP = [acp]
Other name(s): long-chain acyl-[acp] reductase; fatty acyl-[acyl-carrier-protein] reductase; acyl-[acp] reductase
Systematic name: long-chain-aldehyde:NAD(P)+ oxidoreductase (acyl-[acyl-carrier protein]-forming)
Comments: Catalyses the reaction in the opposite direction. This enzyme, purified from the cyanobacterium Synechococcus elongatus PCC 7942, catalyses the NAD(P)H-dependent reduction of an activated fatty acid (acyl-[acp]) to the corresponding aldehyde. Together with EC 4.1.99.5, octadecanal decarbonylase, it is involved in alkane biosynthesis. The natural substrates of the enzyme are C16 and C18 activated fatty acids. Requires Mg2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Schirmer, A., Rude, M.A., Li, X., Popova, E. and del Cardayre, S.B. Microbial biosynthesis of alkanes. Science 329 (2010) 559–562. [DOI] [PMID: 20671186]
[EC 1.2.1.80 created 2011]
 
 
EC 1.3.1.9     
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 1.3.1.10     
Accepted name: enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific)
Reaction: an acyl-[acyl-carrier protein] + NADP+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
Other name(s): acyl-ACP dehydrogenase (ambiguous); enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADPH 2-enoyl Co A reductase; enoyl acyl-carrier-protein reductase (ambiguous); enoyl-ACP reductase (ambiguous); acyl-[acyl-carrier-protein]:NADP+ oxidoreductase (B-specific); acyl-[acyl-carrier protein]:NADP+ oxidoreductase (B-specific); enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific)
Systematic name: acyl-[acyl-carrier protein]:NADP+ oxidoreductase (Si-specific)
Comments: One of the activities of EC 2.3.1.86, fatty-acyl-CoA synthase system, an enzyme found in yeasts (Ascomycota and Basidiomycota). Catalyses the reduction of enoyl-acyl-[acyl-carrier protein] derivatives of carbon chain length from 4 to 16. The yeast enzyme is Si-specific with respect to NADP+. cf. EC 1.3.1.39, enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific) and EC 1.3.1.104, enoyl-[acyl-carrier-protein] reductase (NADPH), which describes enzymes whose stereo-specificity towards NADPH is not known. See also EC 1.3.1.9, enoyl-[acyl-carrier-protein] reductase (NADH).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37251-09-5
References:
1.  Seyama, T., Kasama, T., Yamakawa, T., Kawaguchi, A., Saito, K. and Okuda, S. Origin of hydrogen atoms in the fatty acids synthesized with yeast fatty acid synthetase. J. Biochem. (Tokyo) 82 (1977) 1325–1329. [PMID: 338601]
[EC 1.3.1.10 created 1972, modified 1986, modified 2013, modified 2014, modified 2018]
 
 
EC 1.3.1.39     
Accepted name: enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific)
Reaction: an acyl-[acyl-carrier protein] + NADP+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
Other name(s): acyl-ACP dehydrogenase; enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADPH 2-enoyl Co A reductase; enoyl-ACp reductase; enoyl-[acyl-carrier-protein] reductase (NADPH2, A-specific); acyl-[acyl-carrier-protein]:NADP+ oxidoreductase (A-specific); enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific); acyl-[acyl-carrier protein]:NADP+ oxidoreductase (A-specific)
Systematic name: acyl-[acyl-carrier protein]:NADP+ oxidoreductase (Re-specific)
Comments: This enzyme completes each cycle of fatty acid elongation by catalysing the stereospecific reduction of the double bond at position 2 of a growing fatty acid chain, while linked to an acyl-carrier protein. It is one of the activities of EC 2.3.1.85, fatty-acid synthase system. The mammalian enzyme is Re-specific with respect to NADP+. cf. EC 1.3.1.10, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and EC 1.3.1.104, enoyl-[acyl-carrier-protein] reductase (NADPH).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Dugan, R.E., Slakey, L.L. and Porter, L.W. Stereospecificity of the transfer of hydrogen from reduced nicotinamide adenine dinucleotide phosphate to the acyl chain in the dehydrogenase-catalyzed reactions of fatty acid synthesis. J. Biol. Chem. 245 (1970) 6312–6316. [PMID: 4394955]
2.  Carlisle-Moore, L., Gordon, C.R., Machutta, C.A., Miller, W.T. and Tonge, P.J. Substrate recognition by the human fatty-acid synthase. J. Biol. Chem. 280 (2005) 42612–42618. [DOI] [PMID: 16215233]
[EC 1.3.1.39 created 1986, modified 2013, modified 2018]
 
 
EC 1.3.1.104     
Accepted name: enoyl-[acyl-carrier-protein] reductase (NADPH)
Reaction: an acyl-[acyl-carrier protein] + NADP+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
Other name(s): acyl-ACP dehydrogenase (ambiguous); enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADPH 2-enoyl Co A reductase; enoyl-ACP reductase (ambiguous); fabL (gene name)
Systematic name: acyl-[acyl-carrier protein]:NADP+ oxidoreductase
Comments: The enzyme completes each cycle of fatty acid elongation by catalysing the stereospecific reduction of the double bond at position 2 of a growing fatty acid chain, while linked to the acyl-carrier protein, in an NADPH-dependent manner. This entry stands for enzymes whose stereo-specificity with respect to NADP+ is not known. [cf. EC 1.3.1.39 enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific), EC 1.3.1.10, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and EC 1.3.1.9, enoyl-[acyl-carrier-protein] reductase (NADH)].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Heath, R.J., Su, N., Murphy, C.K. and Rock, C.O. The enoyl-[acyl-carrier-protein] reductases FabI and FabL from Bacillus subtilis. J. Biol. Chem. 275 (2000) 40128–40133. [DOI] [PMID: 11007778]
2.  Kim, K.H., Park, J.K., Ha, B.H., Moon, J.H. and Kim, E.E. Crystallization and preliminary X-ray crystallographic analysis of enoyl-ACP reductase III (FabL) from Bacillus subtilis. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63 (2007) 246–248. [DOI] [PMID: 17329825]
3.  Kim, K.H., Ha, B.H., Kim, S.J., Hong, S.K., Hwang, K.Y. and Kim, E.E. Crystal structures of Enoyl-ACP reductases I (FabI) and III (FabL) from B. subtilis. J. Mol. Biol. 406 (2011) 403–415. [DOI] [PMID: 21185310]
[EC 1.3.1.104 created 2013]
 
 
EC 1.3.1.118     
Accepted name: meromycolic acid enoyl-[acyl-carrier-protein] reductase
Reaction: a meromycolyl-[acyl-carrier protein] + NAD+ = a trans2-meromycolyl-[acyl-carrier protein] + NADH + H+
Glossary: meromycolic acids are one of the two precursors of the mycolic acids produced by Mycobacteria. They consist of a long chain typically of 50–60 carbons, which is functionalized by different groups.
Other name(s): inhA (gene name)
Systematic name: meromycolyl-[acyl-carrier protein]:NAD+ oxidoreductase
Comments: InhA is a component of the fatty acid synthase (FAS) II system of Mycobacterium tuberculosis, catalysing an enoyl-[acyl-carrier-protein] reductase step. The enzyme acts on very long and unsaturated fatty acids that form the meromycolic component of mycolic acids. It extends FASI-derived C20 fatty acids to form C60 to C90 mycolic acids. The enzyme, which forms a homotetramer, is the target of the preferred antitubercular drug isoniazid.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Quemard, A., Sacchettini, J.C., Dessen, A., Vilcheze, C., Bittman, R., Jacobs, W.R., Jr. and Blanchard, J.S. Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis. Biochemistry 34 (1995) 8235–8241. [PMID: 7599116]
2.  Rozwarski, D.A., Vilcheze, C., Sugantino, M., Bittman, R. and Sacchettini, J.C. Crystal structure of the Mycobacterium tuberculosis enoyl-ACP reductase, InhA, in complex with NAD+ and a C16 fatty acyl substrate. J. Biol. Chem. 274 (1999) 15582–15589. [PMID: 10336454]
3.  Marrakchi, H., Laneelle, G. and Quemard, A. InhA, a target of the antituberculous drug isoniazid, is involved in a mycobacterial fatty acid elongation system, FAS-II. Microbiology 146 (2000) 289–296. [PMID: 10708367]
4.  Vilcheze, C., Morbidoni, H.R., Weisbrod, T.R., Iwamoto, H., Kuo, M., Sacchettini, J.C. and Jacobs, W.R., Jr. Inactivation of the inhA-encoded fatty acid synthase II (FASII) enoyl-acyl carrier protein reductase induces accumulation of the FASI end products and cell lysis of Mycobacterium smegmatis. J. Bacteriol. 182 (2000) 4059–4067. [PMID: 10869086]
5.  Gurvitz, A., Hiltunen, J.K. and Kastaniotis, A.J. Function of heterologous Mycobacterium tuberculosis InhA, a type 2 fatty acid synthase enzyme involved in extending C20 fatty acids to C60-to-C90 mycolic acids, during de novo lipoic acid synthesis in Saccharomyces cerevisiae. Appl. Environ. Microbiol. 74 (2008) 5078–5085. [PMID: 18552191]
6.  Chollet, A., Mourey, L., Lherbet, C., Delbot, A., Julien, S., Baltas, M., Bernadou, J., Pratviel, G., Maveyraud, L. and Bernardes-Genisson, V. Crystal structure of the enoyl-ACP reductase of Mycobacterium tuberculosis (InhA) in the apo-form and in complex with the active metabolite of isoniazid pre-formed by a biomimetic approach. J. Struct. Biol. 190 (2015) 328–337. [PMID: 25891098]
[EC 1.3.1.118 created 2018]
 
 
EC 1.14.14.46     
Accepted name: pimeloyl-[acyl-carrier protein] synthase
Reaction: a long-chain acyl-[acyl-carrier protein] + 2 reduced flavodoxin + 3 O2 = pimeloyl-[acyl-carrier protein] + an n-alkanal + 2 oxidized flavodoxin + 3 H2O (overall reaction)
(1a) a long-chain acyl-[acyl-carrier protein] + reduced flavodoxin + O2 = a (7S)-7-hydroxy-long-chain-acyl-[acyl-carrier protein] + oxidized flavodoxin + H2O
(1b) a (7S)-7-hydroxy-long-chain-acyl-[acyl-carrier protein] + reduced flavodoxin + O2 = a (7R,8R)-7,8-dihydroxy-long-chain-acyl-[acyl-carrier protein] + oxidized flavodoxin + H2O
(1c) a (7R,8R)-7,8-dihydroxy-long-chain-acyl-[acyl-carrier protein] + reduced flavodoxin + O2 = a 7-oxoheptanoyl-[acyl-carrier protein] + an n-alkanal + oxidized flavodoxin + 2 H2O
(1d) a 7-oxoheptanoyl-[acyl-carrier protein] + oxidized flavodoxin + H2O = a pimeloyl-[acyl-carrier protein] + reduced flavodoxin + H+
Glossary: a long-chain acyl-[acyl-carrier protein] = an acyl-[acyl-carrier protein] thioester where the acyl chain contains 13 to 22 carbon atoms.
palmitoyl-[acyl-carrier protein] = hexadecanoyl-[acyl-carrier protein]
pimeloyl-[acyl-carrier protein] = 6-carboxyhexanoyl-[acyl-carrier protein]
Other name(s): bioI (gene name); P450BioI; CYP107H1
Systematic name: acyl-[acyl-carrier protein],reduced-flavodoxin:oxygen oxidoreductase (pimeloyl-[acyl-carrier protein]-forming)
Comments: A cytochrome P-450 (heme-thiolate) protein. The enzyme catalyses an oxidative C-C bond cleavage of long-chain acyl-[acyl-carrier protein]s of various lengths to generate pimeloyl-[acyl-carrier protein], an intermediate in the biosynthesis of biotin. The preferred substrate of the enzyme from the bacterium Bacillus subtilis is palmitoyl-[acyl-carrier protein] which then gives heptanal as the alkanal. The mechanism is similar to EC 1.14.15.6, cholesterol monooxygenase (side-chain-cleaving), followed by a hydroxylation step, which may occur spontaneously [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Stok, J.E. and De Voss, J. Expression, purification, and characterization of BioI: a carbon-carbon bond cleaving cytochrome P450 involved in biotin biosynthesis in Bacillus subtilis. Arch. Biochem. Biophys. 384 (2000) 351–360. [DOI] [PMID: 11368323]
2.  Cryle, M.J. and De Voss, J.J. Carbon-carbon bond cleavage by cytochrome p450(BioI)(CYP107H1). Chem. Commun. (Camb.) (2004) 86–87. [DOI] [PMID: 14737344]
3.  Cryle, M.J. and Schlichting, I. Structural insights from a P450 Carrier Protein complex reveal how specificity is achieved in the P450(BioI) ACP complex. Proc. Natl. Acad. Sci. USA 105 (2008) 15696–15701. [DOI] [PMID: 18838690]
4.  Cryle, M.J. Selectivity in a barren landscape: the P450(BioI)-ACP complex. Biochem. Soc. Trans. 38 (2010) 934–939. [DOI] [PMID: 20658980]
[EC 1.14.14.46 created 2013 as EC 1.14.15.12, transferred 2017 to EC 1.14.14.46]
 
 
EC 1.14.15.12      
Transferred entry: pimeloyl-[acyl-carrier protein] synthase. Now EC 1.14.14.46, pimeloyl-[acyl-carrier protein] synthase
[EC 1.14.15.12 created 2013, deleted 2017]
 
 
EC 1.14.19.2     
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 1.14.19.11     
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 1.14.19.26     
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 1.14.19.40     
Accepted name: hex-5-enoyl-[acyl-carrier protein] acetylenase
Reaction: hex-5-enoyl-[acyl-carrier protein] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = hex-5-ynoyl-[acyl-carrier protein] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
Other name(s): jamB (gene name)
Systematic name: hex-5-enoyl-[acyl-carrier protein],reduced ferredoxin:oxygen oxidoreductase (5,6-dehydrogenating)
Comments: The enzyme, characterized from the marine cyanobacterium Moorea producens, is involved in production of the ion channel blocker jamaicamide A. It is specific for hexanoate or hex-5-enoate loaded onto a dedicated acyl-carrier protein (JamC), which is encoded by a gene in the same operon.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Zhu, X., Liu, J. and Zhang, W. De novo biosynthesis of terminal alkyne-labeled natural products. Nat. Chem. Biol. 11 (2015) 115–120. [DOI] [PMID: 25531891]
[EC 1.14.19.40 created 2015]
 
 
EC 1.14.19.78     
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 2.1.1.197     
Accepted name: malonyl-[acyl-carrier protein] O-methyltransferase
Reaction: S-adenosyl-L-methionine + malonyl-[acyl-carrier protein] = S-adenosyl-L-homocysteine + malonyl-[acyl-carrier protein] methyl ester
Other name(s): BioC
Systematic name: S-adenosyl-L-methionine:malonyl-[acyl-carrier protein] O-methyltransferase
Comments: Involved in an early step of biotin biosynthesis in Gram-negative bacteria. This enzyme catalyses the transfer of a methyl group to the ω-carboxyl group of malonyl-[acyl-carrier protein] forming a methyl ester. The methyl ester is recognized by the fatty acid synthetic enzymes, which process it via the fatty acid elongation cycle to give pimelyl-[acyl-carrier-protein] methyl ester [5]. While the enzyme can also accept malonyl-CoA, it has a much higher activity with malonyl-[acyl-carrier protein] [6]
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Del Campillo-Campbell, A., Kayajanian, G., Campbell, A. and Adhya, S. Biotin-requiring mutants of Escherichia coli K-12. J. Bacteriol. 94 (1967) 2065–2066. [PMID: 4864413]
2.  Rolfe, B. and Eisenberg, M.A. Genetic and biochemical analysis of the biotin loci of Escherichia coli K-12. J. Bacteriol. 96 (1968) 515–524. [PMID: 4877129]
3.  Otsuka, A.J., Buoncristiani, M.R., Howard, P.K., Flamm, J., Johnson, C., Yamamoto, R., Uchida, K., Cook, C., Ruppert, J. and Matsuzaki, J. The Escherichia coli biotin biosynthetic enzyme sequences predicted from the nucleotide sequence of the bio operon. J. Biol. Chem. 263 (1988) 19577–19585. [PMID: 3058702]
4.  Cleary, P.P. and Campbell, A. Deletion and complementation analysis of biotin gene cluster of Escherichia coli. J. Bacteriol. 112 (1972) 830–839. [PMID: 4563978]
5.  Lin, S., Hanson, R.E. and Cronan, J.E. Biotin synthesis begins by hijacking the fatty acid synthetic pathway. Nat. Chem. Biol. 6 (2010) 682–688. [DOI] [PMID: 20693992]
6.  Lin, S. and Cronan, J.E. The BioC O-methyltransferase catalyzes methyl esterification of malonyl-acyl carrier protein, an essential step in biotin synthesis. J. Biol. Chem. 287 (2012) 37010–37020. [DOI] [PMID: 22965231]
[EC 2.1.1.197 created 2010, modified 2013]
 
 
EC 2.1.3.10     
Accepted name: malonyl-S-ACP:biotin-protein carboxyltransferase
Reaction: a malonyl-[acyl-carrier protein] + a biotinyl-[protein] = an acetyl-[acyl-carrier protein] + a carboxybiotinyl-[protein]
For diagram of malonate decarboxylase, click here
Other name(s): malonyl-S-acyl-carrier protein:biotin-protein carboxyltransferase; MadC/MadD; MadC,D; malonyl-[acyl-carrier protein]:biotinyl-[protein] carboxyltransferase
Systematic name: malonyl-[acyl-carrier protein]:biotinyl-[protein] carboxytransferase
Comments: Derived from the components MadC and MadD of the anaerobic bacterium Malonomonas rubra, this enzyme is a component of EC 7.2.4.4, biotin-dependent malonate decarboxylase. The carboxy group is transferred from malonate to the cofactor of the biotin protein (MadF) with retention of configuration [2]. Similar to EC 4.1.1.87, malonyl-S-ACP decarboxylase, which forms part of the biotin-independent malonate decarboxylase (EC 4.1.1.88), this enzyme also follows on from EC 2.3.1.187, acetyl-S-ACP:malonate ACP transferase, and results in the regeneration of the acetyl-[acyl-carrier protein] [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  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]
2.  Micklefield, J., Harris, K.J., Gröger, S., Mocek, U., Hilbi, H., Dimroth, P. and Floss, H.G. Stereochemical course of malonate decarboxylase in Malonomonas rubra has biotin decarboxylation with retention. J. Am. Chem. Soc. 117 (1995) 1153–1154. [DOI]
3.  Dimroth, P. and Hilbi, H. Enzymic and genetic basis for bacterial growth on malonate. Mol. Microbiol. 25 (1997) 3–10. [DOI] [PMID: 11902724]
[EC 2.1.3.10 created 2008, modified 2018]
 
 
EC 2.3.1.15     
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 2.3.1.38     
Accepted name: [acyl-carrier-protein] S-acetyltransferase
Reaction: acetyl-CoA + an [acyl-carrier protein] = CoA + an acetyl-[acyl-carrier protein]
For diagram of malonate decarboxylase, click here
Other name(s): acetyl coenzyme A-acyl-carrier-protein transacylase; [acyl-carrier-protein]-acetyltransferase; [ACP]-acetyltransferase; acetyl-CoA:[acyl-carrier-protein] S-acetyltransferase
Systematic name: acetyl-CoA:[acyl-carrier protein] S-acetyltransferase
Comments: This enzyme, along with EC 2.3.1.39, [acyl-carrier-protein] S-malonyltransferase, is essential for the initiation of fatty-acid biosynthesis in bacteria. The substrate acetyl-CoA protects the enzyme against inhibition by N-ethylmaleimide or iodoacetamide [4]. This is one of the activities associated with β-ketoacyl-[acyl-carrier-protein] synthase III (EC 2.3.1.180) [5].
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 37257-16-2
References:
1.  Prescott, D.J. and Vagelos, P.R. Acyl carrier protein. Adv. Enzymol. Relat. Areas Mol. Biol. 36 (1972) 269–311. [DOI] [PMID: 4561013]
2.  Vance, D.E., Mituhashi, O. and Bloch, K. Purification and properties of the fatty acid synthetase from Mycobacterium phlei. J. Biol. Chem. 248 (1973) 2303–2309. [PMID: 4698221]
3.  Williamson, I.P. and Wakil, S.J. Studies on the mechanism of fatty acid synthesis. XVII. Preparation and general properties of acetyl coenzyme A and malonyl coenzyme A-acyl carrier protein transacylases. J. Biol. Chem. 241 (1966) 2326–2332. [DOI] [PMID: 5330116]
4.  Lowe, P.N. and Rhodes, S. Purification and characterization of [acyl-carrier-protein] acetyltransferase from Escherichia coli. Biochem. J. 250 (1988) 789–796. [PMID: 3291856]
5.  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]
6.  Rangan, V.S. and Smith, S. Alteration of the substrate specificity of the malonyl-CoA/acetyl-CoA:acyl carrier protein S-acyltransferase domain of the multifunctional fatty acid synthase by mutation of a single arginine residue. J. Biol. Chem. 272 (1997) 11975–11978. [DOI] [PMID: 9115261]
[EC 2.3.1.38 created 1972, modified 2006]
 
 
EC 2.3.1.39     
Accepted name: [acyl-carrier-protein] S-malonyltransferase
Reaction: malonyl-CoA + an [acyl-carrier protein] = CoA + a malonyl-[acyl-carrier protein]
For diagram of malonate decarboxylase, click here
Other name(s): [acyl carrier protein]malonyltransferase; FabD; malonyl coenzyme A-acyl carrier protein transacylase; malonyl transacylase; malonyl transferase; malonyl-CoA-acyl carrier protein transacylase; malonyl-CoA:[acyl-carrier-protein] S-malonyltransferase; malonyl-CoA:ACP transacylase; malonyl-CoA:ACP-SH transacylase; malonyl-CoA:AcpM transacylase; malonyl-CoA:acyl carrier protein transacylase; malonyl-CoA:acyl-carrier-protein transacylase; malonyl-CoA/dephospho-CoA acyltransferase; MAT; MCAT; MdcH
Systematic name: malonyl-CoA:[acyl-carrier protein] S-malonyltransferase
Comments: This enzyme, along with EC 2.3.1.38, [acyl-carrier-protein] S-acetyltransferase, is essential for the initiation of fatty-acid biosynthesis in bacteria. This enzyme also provides the malonyl groups for polyketide biosynthesis [7]. The product of the reaction, malonyl-ACP, is an elongation substrate in fatty-acid biosynthesis. In Mycobacterium tuberculosis, holo-ACP (the product of EC 2.7.8.7, holo-[acyl-carrier-protein] synthase) is the preferred substrate [5]. This enzyme also forms part of the multienzyme complexes EC 4.1.1.88, biotin-independent malonate decarboxylase and EC 7.2.4.4, biotin-dependent malonate decarboxylase. Malonylation of ACP is immediately followed by decarboxylation within the malonate-decarboxylase complex to yield acetyl-ACP, the catalytically active species of the decarboxylase [12]. In the enzyme from Klebsiella pneumoniae, methylmalonyl-CoA can also act as a substrate but acetyl-CoA cannot [10] whereas the enzyme from Pseudomonas putida can use both as substrates [11]. The ACP subunit found in fatty-acid biosynthesis contains a pantetheine-4′-phosphate cofactor; that from malonate decarboxylase also contains pantetheine-4′-phosphate but in the form of a 2′-(5-triphosphoribosyl)-3′-dephospho-CoA cofactor.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 37257-17-3
References:
1.  Alberts, A.W., Majerus, P.W. and Vagelos, P.R. Acetyl-CoA acyl carrier protein transacylase. Methods Enzymol. 14 (1969) 50–53. [DOI]
2.  Prescott, D.J. and Vagelos, P.R. Acyl carrier protein. Adv. Enzymol. Relat. Areas Mol. Biol. 36 (1972) 269–311. [DOI] [PMID: 4561013]
3.  Williamson, I.P. and Wakil, S.J. Studies on the mechanism of fatty acid synthesis. XVII. Preparation and general properties of acetyl coenzyme A and malonyl coenzyme A-acyl carrier protein transacylases. J. Biol. Chem. 241 (1966) 2326–2332. [DOI] [PMID: 5330116]
4.  Joshi, V.C. and Wakil, S.J. Studies on the mechanism of fatty acid synthesis. XXVI. Purification and properties of malonyl-coenzyme A--acyl carrier protein transacylase of Escherichia coli. Arch. Biochem. Biophys. 143 (1971) 493–505. [DOI] [PMID: 4934182]
5.  Kremer, L., Nampoothiri, K.M., Lesjean, S., Dover, L.G., Graham, S., Betts, J., Brennan, P.J., Minnikin, D.E., Locht, C. and Besra, G.S. Biochemical characterization of acyl carrier protein (AcpM) and malonyl-CoA:AcpM transacylase (mtFabD), two major components of Mycobacterium tuberculosis fatty acid synthase II. J. Biol. Chem. 276 (2001) 27967–27974. [DOI] [PMID: 11373295]
6.  Keatinge-Clay, A.T., Shelat, A.A., Savage, D.F., Tsai, S.C., Miercke, L.J., O'Connell, J.D., 3rd, Khosla, C. and Stroud, R.M. Catalysis, specificity, and ACP docking site of Streptomyces coelicolor malonyl-CoA:ACP transacylase. Structure 11 (2003) 147–154. [DOI] [PMID: 12575934]
7.  Szafranska, A.E., Hitchman, T.S., Cox, R.J., Crosby, J. and Simpson, T.J. Kinetic and mechanistic analysis of the malonyl CoA:ACP transacylase from Streptomyces coelicolor indicates a single catalytically competent serine nucleophile at the active site. Biochemistry 41 (2002) 1421–1427. [DOI] [PMID: 11814333]
8.  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]
9.  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]
10.  Hoenke, S. and Dimroth, P. Formation of catalytically active acetyl-S-malonate decarboxylase requires malonyl-coenzyme A:acyl carrier protein transacylase as auxiliary enzyme. Eur. J. Biochem. 259 (1999) 181–187. [DOI] [PMID: 9914491]
11.  Chohnan, S., Fujio, T., Takaki, T., Yonekura, M., Nishihara, H. and Takamura, Y. Malonate decarboxylase of Pseudomonas putida is composed of five subunits. FEMS Microbiol. Lett. 169 (1998) 37–43. [DOI] [PMID: 9851033]
12.  Dimroth, P. and Hilbi, H. Enzymic and genetic basis for bacterial growth on malonate. Mol. Microbiol. 25 (1997) 3–10. [DOI] [PMID: 11902724]
[EC 2.3.1.39 created 1972, modified 2006, modified 2008]
 
 
EC 2.3.1.40     
Accepted name: acyl-[acyl-carrier-protein]—phospholipid O-acyltransferase
Reaction: an acyl-[acyl-carrier protein] + O-(2-acyl-sn-glycero-3-phospho)ethanolamine = an [acyl-carrier protein] + O-(1,2-diacyl-sn-glycero-3-phospho)ethanolamine
Other name(s): acyl-[acyl-carrier protein]:O-(2-acyl-sn-glycero-3-phospho)-ethanolamine O-acyltransferase
Systematic name: acyl-[acyl-carrier protein]:O-(2-acyl-sn-glycero-3-phospho)ethanolamine O-acyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37257-18-4
References:
1.  Taylor, S.S. and Heath, E.C. The incorporation of β-hydroxy fatty acids into a phospholipid of Escherichia coli B. J. Biol. Chem. 244 (1969) 6605–6616. [PMID: 4902888]
[EC 2.3.1.40 created 1972]
 
 
EC 2.3.1.41     
Accepted name: β-ketoacyl-[acyl-carrier-protein] synthase I
Reaction: an acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = a 3-oxoacyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
Glossary: acyl-[acyl-carrier protein] = R-CO-[acyl-carrier protein]
malonyl-[acyl-carrier protein] = HOOC-CH2-CO-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] = R-CO-CH2-CO-[acyl-carrier protein]
Other name(s): β-ketoacyl-ACP synthase I; β-ketoacyl synthetase; β-ketoacyl-ACP synthetase; β-ketoacyl-acyl carrier protein synthetase; β-ketoacyl-[acyl carrier protein] synthase; β-ketoacylsynthase; condensing enzyme (ambiguous); 3-ketoacyl-acyl carrier protein synthase; fatty acid condensing enzyme; acyl-malonyl(acyl-carrier-protein)-condensing enzyme; acyl-malonyl acyl carrier protein-condensing enzyme; β-ketoacyl acyl carrier protein synthase; 3-oxoacyl-[acyl-carrier-protein] synthase; 3-oxoacyl:ACP synthase I; KASI; KAS I; FabF1; FabB; acyl-[acyl-carrier-protein]:malonyl-[acyl-carrier-protein] C-acyltransferase (decarboxylating)
Systematic name: acyl-[acyl-carrier protein]:malonyl-[acyl-carrier protein] C-acyltransferase (decarboxylating)
Comments: This enzyme is responsible for the chain-elongation step of dissociated (type II) fatty-acid biosynthesis, i.e. the addition of two C atoms to the fatty-acid chain. Escherichia coli mutants that lack this enzyme are deficient in unsaturated fatty acids. The enzyme can use fatty acyl thioesters of ACP (C2 to C16) as substrates, as well as fatty acyl thioesters of Co-A (C4 to C16) [4]. The substrate specificity is very similar to that of EC 2.3.1.179, β-ketoacyl-ACP synthase II, with the exception that the latter enzyme is far more active with palmitoleoyl-ACP (C16Δ9) as substrate, allowing the organism to regulate its fatty-acid composition with changes in temperature [4,5].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9077-10-5
References:
1.  Alberts, A.W., Majerus, P.W. and Vagelos, P.R. Acetyl-CoA acyl carrier protein transacylase. Methods Enzymol. 14 (1969) 50–53. [DOI]
2.  Prescott, D.J. and Vagelos, P.R. Acyl carrier protein. Adv. Enzymol. Relat. Areas Mol. Biol. 36 (1972) 269–311. [DOI] [PMID: 4561013]
3.  Toomey, R.E. and Wakil, S.J. Studies on the mechanism of fatty acid synthesis. XVI. Preparation and general properties of acyl-malonyl acyl carrier protein-condensing enzyme from Escherichia coli. J. Biol. Chem. 241 (1966) 1159–1165. [PMID: 5327099]
4.  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]
5.  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]
6.  Wang, H. and Cronan, J.E. Functional replacement of the FabA and FabB proteins of Escherichia coli fatty acid synthesis by Enterococcus faecalis FabZ and FabF homologues. J. Biol. Chem. 279 (2004) 34489–34495. [DOI] [PMID: 15194690]
7.  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 2.3.1.41 created 1972, modified 2006]
 
 
EC 2.3.1.47     
Accepted name: 8-amino-7-oxononanoate synthase
Reaction: pimeloyl-[acyl-carrier protein] + L-alanine = 8-amino-7-oxononanoate + CO2 + holo-[acyl-carrier protein]
Glossary: pimeloyl-[acyl-carrier protein] = 6-carboxyhexanoyl-[acyl-carrier protein]
Other name(s): 7-keto-8-aminopelargonic acid synthetase; 7-keto-8-aminopelargonic synthetase; 8-amino-7-oxopelargonate synthase; bioF (gene name)
Systematic name: 6-carboxyhexanoyl-[acyl-carrier protein]:L-alanine C-carboxyhexanoyltransferase (decarboxylating)
Comments: A pyridoxal-phosphate protein. The enzyme catalyses the decarboxylative condensation of L-alanine and pimeloyl-[acyl-carrier protein], a key step in the pathway for biotin biosynthesis. Pimeloyl-CoA can be used with lower efficiency [5].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9075-61-0
References:
1.  Eisenberg, M.A. and Star, C. Synthesis of 7-oxo-8-aminopelargonic acid, a biotin vitamer, in cell-free extracts of Escherichia coli biotin auxotrophs. J. Bacteriol. 96 (1968) 1291–1297. [PMID: 4879561]
2.  Alexeev, D., Alexeeva, M., Baxter, R.L., Campopiano, D.J., Webster, S.P. and Sawyer, L. The crystal structure of 8-amino-7-oxononanoate synthase: a bacterial PLP-dependent, acyl-CoA-condensing enzyme. J. Mol. Biol. 284 (1998) 401–419. [DOI] [PMID: 9813126]
3.  Ploux, O., Breyne, O., Carillon, S. and Marquet, A. Slow-binding and competitive inhibition of 8-amino-7-oxopelargonate synthase, a pyridoxal-5′-phosphate-dependent enzyme involved in biotin biosynthesis, by substrate and intermediate analogs. Kinetic and binding studies. Eur. J. Biochem. 259 (1999) 63–70. [PMID: 9914476]
4.  Webster, S.P. , Alexeev. D., Campopiano, D.J., Watt, R.M., Alexeeva, M., Sawyer, L. and Baxter, R. Mechanism of 8-amino-7-oxononanoate synthase: spectroscopic, kinetic, and crystallographic studies. Biochemistry 39 (2000) 516–528. [DOI] [PMID: 10642176]
5.  Lin, S., Hanson, R.E. and Cronan, J.E. Biotin synthesis begins by hijacking the fatty acid synthetic pathway. Nat. Chem. Biol. 6 (2010) 682–688. [DOI] [PMID: 20693992]
[EC 2.3.1.47 created 1976, modified 2013]
 
 
EC 2.3.1.51     
Accepted name: 1-acylglycerol-3-phosphate O-acyltransferase
Reaction: acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Other name(s): 1-acyl-sn-glycero-3-phosphate acyltransferase; 1-acyl-sn-glycerol 3-phosphate acyltransferase; 1-acylglycero-3-phosphate acyltransferase; 1-acylglycerolphosphate acyltransferase; 1-acylglycerophosphate acyltransferase; lysophosphatidic acid-acyltransferase
Systematic name: acyl-CoA:1-acyl-sn-glycerol-3-phosphate 2-O-acyltransferase
Comments: Acyl-[acyl-carrier protein] can also act as an acyl donor. The animal enzyme is specific for the transfer of unsaturated fatty acyl groups.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 51901-16-7
References:
1.  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]
2.  Hill, E.E. and Lands, W.E.M. Incorporation of long-chain and polyunsaturated acids into phosphatidate and phosphatidylcholine. Biochim. Biophys. Acta 152 (1968) 645–648. [DOI] [PMID: 5661029]
3.  Yamashita, S., Hosaka, K. and Numa, S. Acyl-donor specificities of partially purified 1-acylglycerophosphate acyltransferase, 2-acylglycerophosphate acyltransferase and 1-acylglycerophosphorylcholine acyltransferase from rat-liver microsomes. Eur. J. Biochem. 38 (1973) 25–31. [DOI] [PMID: 4774123]
[EC 2.3.1.51 created 1976, modified 1990]
 
 
EC 2.3.1.129     
Accepted name: acyl-[acyl-carrier-protein]—UDP-N-acetylglucosamine O-acyltransferase
Reaction: a (3R)-3-hydroxyacyl-[acyl-carrier protein] + UDP-N-acetyl-α-D-glucosamine = an [acyl-carrier protein] + a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-α-D-glucosamine
For diagram of lipid IVA biosynthesis, click here
Other name(s): lpxA (gene name); UDP-N-acetylglucosamine acyltransferase; uridine diphosphoacetylglucosamine acyltransferase; acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase; (R)-3-hydroxytetradecanoyl-[acyl-carrier-protein]:UDP-N-acetylglucosamine 3-O-(3-hydroxytetradecanoyl)transferase
Systematic name: (3R)-3-hydroxyacyl-[acyl-carrier protein]:UDP-N-acetyl-α-D-glucosamine 3-O-(3-hydroxyacyl)transferase
Comments: Involved with EC 2.4.1.182, lipid-A-disaccharide synthase, and EC 2.7.1.130, tetraacyldisaccharide 4′-kinase, in the biosynthesis of the phosphorylated glycolipid, Lipid A, in the outer membrane of Gram-negative bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 105843-69-4
References:
1.  Anderson, M.S., Bulawa, C.E. and Raetz, C.R.H. The biosynthesis of gram-negative endotoxin. Formation of lipid A precursors from UDP-GlcNAc in extracts of Escherichia coli. J. Biol. Chem. 260 (1985) 15536–15541. [PMID: 3905795]
2.  Anderson, M.S., Bull, H.G., Galloway, S.M., Kelly, T.M., Mohan, S., Radika, K. and Raetz, C.R. UDP-N-acetylglucosamine acyltransferase of Escherichia coli. The first step of endotoxin biosynthesis is thermodynamically unfavorable. J. Biol. Chem. 268 (1993) 19858–19865. [PMID: 8366124]
3.  Raetz, C.R. and Roderick, S.L. A left-handed parallel β helix in the structure of UDP-N-acetylglucosamine acyltransferase. Science 270 (1995) 997–1000. [DOI] [PMID: 7481807]
4.  Williams, A.H. and Raetz, C.R. Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase. Proc. Natl. Acad. Sci. USA 104 (2007) 13543–13550. [DOI] [PMID: 17698807]
5.  Bainbridge, B.W., Karimi-Naser, L., Reife, R., Blethen, F., Ernst, R.K. and Darveau, R.P. Acyl chain specificity of the acyltransferases LpxA and LpxD and substrate availability contribute to lipid A fatty acid heterogeneity in Porphyromonas gingivalis. J. Bacteriol. 190 (2008) 4549–4558. [DOI] [PMID: 18456814]
[EC 2.3.1.129 created 1990, modified 2021]
 
 
EC 2.3.1.141     
Accepted name: galactosylacylglycerol O-acyltransferase
Reaction: an acyl-[acyl-carrier protein] + a 2-acyl-3-O-(β-D-galactosyl)-sn-glycerol = an [acyl-carrier protein] + a 1,2-diacyl-3-O-(β-D-galactosyl)-sn-glycerol
Other name(s): acyl-acyl-carrier protein: lysomonogalactosyldiacylglycerol acyltransferase; acyl-ACP:lyso-MGDG acyltransferase; acyl-[acyl-carrier-protein]:D-galactosylacylglycerol O-acyltransferase
Systematic name: acyl-[acyl-carrier protein]:2-acyl-3-O-(β-D-galactosyl)-sn-glycerol O-acyltransferase
Comments: Transfers long-chain acyl groups to the sn-1 position of the glycerol residue.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 119129-68-9
References:
1.  Chen, H.-H., Wickrema, A. and Jaworski, J.G. Acyl-acyl-carrier protein: lysomonogalactosyldiacylglycerol acyltransferase from the cyanobacterium Anabaena variabilis. Biochim. Biophys. Acta 963 (1988) 493–500. [DOI] [PMID: 3143419]
[EC 2.3.1.141 created 1992]
 
 
EC 2.3.1.179     
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 2.3.1.180     
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 2.3.1.181     
Accepted name: lipoyl(octanoyl) transferase
Reaction: an octanoyl-[acyl-carrier protein] + a protein = a protein N6-(octanoyl)lysine + an [acyl-carrier protein]
Glossary: lipoyl group
Other name(s): LipB; lipoyl (octanoyl)-[acyl-carrier-protein]-protein N-lipoyltransferase; lipoyl (octanoyl)-acyl carrier protein:protein transferase; lipoate/octanoate transferase; lipoyltransferase; octanoyl-[acyl carrier protein]-protein N-octanoyltransferase; lipoyl(octanoyl)transferase; octanoyl-[acyl-carrier-protein]:protein N-octanoyltransferase
Systematic name: octanoyl-[acyl-carrier protein]:protein N-octanoyltransferase
Comments: This is the first committed step in the biosynthesis of lipoyl cofactor. Lipoylation is essential for the function of several key enzymes involved in oxidative metabolism, as it converts apoprotein into the biologically active holoprotein. Examples of such lipoylated proteins include pyruvate dehydrogenase (E2 domain), 2-oxoglutarate dehydrogenase (E2 domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein) [2,3]. Lipoyl-ACP can also act as a substrate [4] although octanoyl-ACP is likely to be the true substrate [6]. The other enzyme involved in the biosynthesis of lipoyl cofactor is EC 2.8.1.8, lipoyl synthase. An alternative lipoylation pathway involves EC 6.3.1.20, lipoate—protein ligase, which can lipoylate apoproteins using exogenous lipoic acid (or its analogues).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 392687-64-8
References:
1.  Nesbitt, N.M., Baleanu-Gogonea, C., Cicchillo, R.M., Goodson, K., Iwig, D.F., Broadwater, J.A., Haas, J.A., Fox, B.G. and Booker, S.J. Expression, purification, and physical characterization of Escherichia coli lipoyl(octanoyl)transferase. Protein Expr. Purif. 39 (2005) 269–282. [DOI] [PMID: 15642479]
2.  Vanden Boom, T.J., Reed, K.E. and Cronan, J.E., Jr. Lipoic acid metabolism in Escherichia coli: isolation of null mutants defective in lipoic acid biosynthesis, molecular cloning and characterization of the E. coli lip locus, and identification of the lipoylated protein of the glycine cleavage system. J. Bacteriol. 173 (1991) 6411–6420. [DOI] [PMID: 1655709]
3.  Jordan, S.W. and Cronan, J.E., Jr. A new metabolic link. The acyl carrier protein of lipid synthesis donates lipoic acid to the pyruvate dehydrogenase complex in Escherichia coli and mitochondria. J. Biol. Chem. 272 (1997) 17903–17906. [DOI] [PMID: 9218413]
4.  Zhao, X., Miller, J.R., Jiang, Y., Marletta, M.A. and Cronan, J.E. Assembly of the covalent linkage between lipoic acid and its cognate enzymes. Chem. Biol. 10 (2003) 1293–1302. [DOI] [PMID: 14700636]
5.  Wada, M., Yasuno, R., Jordan, S.W., Cronan, J.E., Jr. and Wada, H. Lipoic acid metabolism in Arabidopsis thaliana: cloning and characterization of a cDNA encoding lipoyltransferase. Plant Cell Physiol. 42 (2001) 650–656. [PMID: 11427685]
6.  Perham, R.N. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu. Rev. Biochem. 69 (2000) 961–1004. [DOI] [PMID: 10966480]
[EC 2.3.1.181 created 2006, modified 2016]
 
 
EC 2.3.1.184     
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 2.3.1.187     
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]
 
 
EC 2.3.1.191     
Accepted name: UDP-3-O-(3-hydroxyacyl)glucosamine N-acyltransferase
Reaction: a (3R)-3-hydroxyacyl-[acyl-carrier protein] + a UDP-3-O-[(3R)-3-hydroxyacyl]-α-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosamine + a holo-[acyl-carrier protein]
For diagram of lipid IVA biosynthesis, click here
Other name(s): lpxD (gene name); UDP-3-O-acyl-glucosamine N-acyltransferase; UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase; acyltransferase LpxD; acyl-ACP:UDP-3-O-(3-hydroxyacyl)-GlcN N-acyltransferase; firA (gene name); (3R)-3-hydroxymyristoyl-[acyl-carrier protein]:UDP-3-O-[(3R)-3-hydroxymyristoyl]-α-D-glucosamine N-acetyltransferase; UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase; (3R)-3-hydroxytetradecanoyl-[acyl-carrier protein]:UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-α-D-glucosamine N-acetyltransferase
Systematic name: (3R)-3-hydroxyacyl-[acyl-carrier protein]:UDP-3-O-[(3R)-3-hydroxyacyl]-α-D-glucosamine N-acyltransferase
Comments: The enzyme catalyses a step of lipid A biosynthesis. LpxD from Escherichia coli prefers (3R)-3-hydroxytetradecanoyl-[acyl-carrier protein] [3], but it does not have an absolute specificity for 14-carbon hydroxy fatty acids, as it can transfer other fatty acids, including odd-chain fatty acids, if they are available to the organism [5].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Kelly, T.M., Stachula, S.A., Raetz, C.R. and Anderson, M.S. The firA gene of Escherichia coli encodes UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase. The third step of endotoxin biosynthesis. J. Biol. Chem. 268 (1993) 19866–19874. [PMID: 8366125]
2.  Buetow, L., Smith, T.K., Dawson, A., Fyffe, S. and Hunter, W.N. Structure and reactivity of LpxD, the N-acyltransferase of lipid A biosynthesis. Proc. Natl. Acad. Sci. USA 104 (2007) 4321–4326. [DOI] [PMID: 17360522]
3.  Bartling, C.M. and Raetz, C.R. Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis. Biochemistry 47 (2008) 5290–5302. [DOI] [PMID: 18422345]
4.  Bainbridge, B.W., Karimi-Naser, L., Reife, R., Blethen, F., Ernst, R.K. and Darveau, R.P. Acyl chain specificity of the acyltransferases LpxA and LpxD and substrate availability contribute to lipid A fatty acid heterogeneity in Porphyromonas gingivalis. J. Bacteriol. 190 (2008) 4549–4558. [DOI] [PMID: 18456814]
5.  Bartling, C.M. and Raetz, C.R. Crystal structure and acyl chain selectivity of Escherichia coli LpxD, the N-acyltransferase of lipid A biosynthesis. Biochemistry 48 (2009) 8672–8683. [DOI] [PMID: 19655786]
6.  Badger, J., Chie-Leon, B., Logan, C., Sridhar, V., Sankaran, B., Zwart, P.H. and Nienaber, V. Structure determination of LpxD from the lipopolysaccharide-synthesis pathway of Acinetobacter baumannii. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 69 (2013) 6–9. [DOI] [PMID: 23295477]
7.  Kroeck, K.G., Sacco, M.D., Smith, E.W., Zhang, X., Shoun, D., Akhtar, A., Darch, S.E., Cohen, F., Andrews, L.D., Knox, J.E. and Chen, Y. Discovery of dual-activity small-molecule ligands of Pseudomonas aeruginosa LpxA and LpxD using SPR and X-ray crystallography. Sci. Rep. 9:15450 (2019). [DOI] [PMID: 31664082]
[EC 2.3.1.191 created 2010, modified 2021]
 
 
EC 2.3.1.199     
Accepted name: very-long-chain 3-oxoacyl-CoA synthase
Reaction: a very-long-chain acyl-CoA + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
Glossary: a very-long-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains 23 or more carbon atoms.
Other name(s): very-long-chain 3-ketoacyl-CoA synthase; very-long-chain β-ketoacyl-CoA synthase; condensing enzyme (ambiguous); CUT1 (gene name); CER6 (gene name); FAE1 (gene name); KCS (gene name); ELO (gene name)
Systematic name: malonyl-CoA:very-long-chain acyl-CoA malonyltransferase (decarboxylating and thioester-hydrolysing)
Comments: This is the first 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. Multiple forms exist with differing preferences for the substrate, and thus the specific form expressed determines the local composition of very-long-chain fatty acids [6,7]. For example, the FAE1 form from the plant Arabidopsis thaliana accepts only 16 and 18 carbon substrates, with oleoyl-CoA (18:1) being the preferred substrate [5], while CER6 from the same plant prefers substrates with chain length of C22 to C32 [4,8]. cf. EC 1.1.1.330, very-long-chain 3-oxoacyl-CoA reductase, EC 4.2.1.134, very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] dehydratase, and EC 1.3.1.93, very-long-chain enoyl-CoA reductase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Toke, D.A. and Martin, C.E. Isolation and characterization of a gene affecting fatty acid elongation in Saccharomyces cerevisiae. J. Biol. Chem. 271 (1996) 18413–18422. [DOI] [PMID: 8702485]
2.  Oh, C.S., Toke, D.A., Mandala, S. and Martin, C.E. ELO2 and ELO3, homologues of the Saccharomyces cerevisiae ELO1 gene, function in fatty acid elongation and are required for sphingolipid formation. J. Biol. Chem. 272 (1997) 17376–17384. [DOI] [PMID: 9211877]
3.  Dittrich, F., Zajonc, D., Huhne, K., Hoja, U., Ekici, A., Greiner, E., Klein, H., Hofmann, J., Bessoule, J.J., Sperling, P. and Schweizer, E. Fatty acid elongation in yeast--biochemical characteristics of the enzyme system and isolation of elongation-defective mutants. Eur. J. Biochem. 252 (1998) 477–485. [DOI] [PMID: 9546663]
4.  Millar, A.A., Clemens, S., Zachgo, S., Giblin, E.M., Taylor, D.C. and Kunst, L. CUT1, an Arabidopsis gene required for cuticular wax biosynthesis and pollen fertility, encodes a very-long-chain fatty acid condensing enzyme. Plant Cell 11 (1999) 825–838. [PMID: 10330468]
5.  Ghanevati, M. and Jaworski, J.G. Engineering and mechanistic studies of the Arabidopsis FAE1 β-ketoacyl-CoA synthase, FAE1 KCS. Eur. J. Biochem. 269 (2002) 3531–3539. [DOI] [PMID: 12135493]
6.  Blacklock, B.J. and Jaworski, J.G. Substrate specificity of Arabidopsis 3-ketoacyl-CoA synthases. Biochem. Biophys. Res. Commun. 346 (2006) 583–590. [DOI] [PMID: 16765910]
7.  Denic, V. and Weissman, J.S. A molecular caliper mechanism for determining very long-chain fatty acid length. Cell 130 (2007) 663–677. [DOI] [PMID: 17719544]
8.  Tresch, S., Heilmann, M., Christiansen, N., Looser, R. and Grossmann, K. Inhibition of saturated very-long-chain fatty acid biosynthesis by mefluidide and perfluidone, selective inhibitors of 3-ketoacyl-CoA synthases. Phytochemistry 76 (2012) 162–171. [DOI] [PMID: 22284369]
[EC 2.3.1.199 created 2012]
 
 
EC 2.3.1.207     
Accepted name: β-ketodecanoyl-[acyl-carrier-protein] synthase
Reaction: octanoyl-CoA + a malonyl-[acyl-carrier protein] = a 3-oxodecanoyl-[acyl-carrier protein] + CoA + CO2
Glossary: [acyl-carrier protein] = [acp]
Systematic name: octanoyl-CoA:malonyl-[acyl-carrier protein] C-heptanoylltransferase (decarboxylating, CoA-forming)
Comments: This enzyme, which has been characterized from the bacterium Pseudomonas aeruginosa PAO1, catalyses the condensation of octanoyl-CoA, obtained from exogenously supplied fatty acids via β-oxidation, with malonyl-[acp], forming 3-oxodecanoyl-[acp], an intermediate of the fatty acid elongation cycle. The enzyme provides a shunt for β-oxidation degradation intermediates into de novo fatty acid biosynthesis.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Yuan, Y., Leeds, J.A. and Meredith, T.C. Pseudomonas aeruginosa directly shunts β-oxidation degradation intermediates into de novo fatty acid biosynthesis. J. Bacteriol. 194 (2012) 5185–5196. [DOI] [PMID: 22753057]
[EC 2.3.1.207 created 2012]
 
 
EC 2.3.1.221     
Accepted name: noranthrone synthase
Reaction: 7 malonyl-CoA + hexanoyl-[acyl-carrier protein] = 7 CoA + norsolorinic acid anthrone + [acyl-carrier protein] + 7 CO2 + 2 H2O
For diagram of polyketides biosynthesis, click here
Glossary: norsolorinic acid anthrone = noranthrone = 2-hexanoyl-1,3,6,8-tetrahydroxyanthracen-9(10H)-one
Other name(s): polyketide synthase A (ambiguous); PksA (ambiguous); norsolorinic acid anthrone synthase
Systematic name: malonyl-CoA:hexanoate malonyltransferase (norsolorinic acid anthrone-forming)
Comments: A multi-domain polyketide synthase involved in the synthesis of aflatoxins in the fungus Aspergillus parasiticus. The hexanoyl starter unit is provided to the acyl-carrier protein (ACP) domain by a dedicated fungal fatty acid synthase [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Crawford, J.M., Thomas, P.M., Scheerer, J.R., Vagstad, A.L., Kelleher, N.L. and Townsend, C.A. Deconstruction of iterative multidomain polyketide synthase function. Science 320 (2008) 243–246. [DOI] [PMID: 18403714]
2.  Crawford, J.M., Korman, T.P., Labonte, J.W., Vagstad, A.L., Hill, E.A., Kamari-Bidkorpeh, O., Tsai, S.C. and Townsend, C.A. Structural basis for biosynthetic programming of fungal aromatic polyketide cyclization. Nature 461 (2009) 1139–1143. [DOI] [PMID: 19847268]
3.  Korman, T.P., Crawford, J.M., Labonte, J.W., Newman, A.G., Wong, J., Townsend, C.A. and Tsai, S.C. Structure and function of an iterative polyketide synthase thioesterase domain catalyzing Claisen cyclization in aflatoxin biosynthesis. Proc. Natl. Acad. Sci. USA 107 (2010) 6246–6251. [DOI] [PMID: 20332208]
[EC 2.3.1.221 created 2013]
 
 
EC 2.3.1.228     
Accepted name: isovaleryl-homoserine lactone synthase
Reaction: isovaleryl-CoA + S-adenosyl-L-methionine = CoA + S-methyl-5′-thioadenosine + N-isovaleryl-L-homoserine lactone
Glossary: S-methyl-5′-thioadenosine = 5′-deoxy-5′-(methylsulfanyl)adenosine
Other name(s): IV-HSL synthase; BjaI
Systematic name: isovaleryl-CoA:S-adenosyl-L-methionine isovaleryltranserase (lactone-forming, methylthioadenosine-releasing)
Comments: The enzyme, found in the bacterium Bradyrhizobium japonicum, does not accept isovaleryl-[acyl-carrier protein] as acyl donor (cf. EC 2.3.1.184, acyl-homoserine-lactone synthase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Lindemann, A., Pessi, G., Schaefer, A.L., Mattmann, M.E., Christensen, Q.H., Kessler, A., Hennecke, H., Blackwell, H.E., Greenberg, E.P. and Harwood, C.S. Isovaleryl-homoserine lactone, an unusual branched-chain quorum-sensing signal from the soybean symbiont Bradyrhizobium japonicum. Proc. Natl. Acad. Sci. USA 108 (2011) 16765–16770. [DOI] [PMID: 21949379]
[EC 2.3.1.228 created 2013]
 
 
EC 2.3.1.241     
Accepted name: Kdo2-lipid IVA acyltransferase
Reaction: a fatty acyl-[acyl-carrier protein] + an α-Kdo-(2→4)-α-Kdo-(2→6)-[lipid IVA] = an α-Kdo-(2→4)-α-Kdo-(2→6)-(acyl)-[lipid IVA] + an [acyl-carrier protein]
For diagram of Kdo-Kdo-Lipid IVA metabolism, click here
Glossary: Kdo = 3-deoxy-D-manno-oct-2-ulopyranosylonic acid
a lipid IVA = 2-deoxy-2-{[(3R)-3-hydroxyacyl]amino}-3-O-[(3R)-3-hydroxyacyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-{[(3R)-3-hydroxyacyl]amino}-1-O-phospho-α-D-glucopyranose
an α-Kdo-(2→4)-α-Kdo-(2→6)-(acyl)-[lipid IVA] = 3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→4)-3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→6)-2-deoxy-2-{[(3R)-3-(acyloxy)acyl]amino}-3-O-[(3R)-3-hydroxyacyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-{[(3R)-3-hydroxyacyl]amino}-1-O-phosphono-α-D-glucopyranose
Other name(s): LpxL; htrB (gene name); dodecanoyl-[acyl-carrier protein]:α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA O-dodecanoyltransferase; lauroyl-[acyl-carrier protein]:Kdo2-lipid IVA O-lauroyltransferase; (Kdo)2-lipid IVA lauroyltransferase; α-Kdo-(2→4)-α-(2→6)-lipid IVA lauroyltransferase; dodecanoyl-[acyl-carrier protein]:Kdo2-lipid IVA O-dodecanoyltransferase; Kdo2-lipid IVA lauroyltransferase
Systematic name: fatty acyl-[acyl-carrier protein]:α-Kdo-(2→4)-α-Kdo-(2→6)-[lipid IVA] O-acyltransferase
Comments: The enzyme is involved in the biosynthesis of the phosphorylated outer membrane glycolipid lipid A. It transfers an acyl group to the 3-O position of the 3R-hydroxyacyl already attached to the nitrogen of the non-reducing glucosamine molecule. The enzyme from the bacterium Escherichia coli is specific for lauryl (C12) acyl groups, giving the enzyme its previous accepted name. However, enzymes from different species accept highly variable substrates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Clementz, T., Bednarski, J.J. and Raetz, C.R. Function of the htrB high temperature requirement gene of Escherichia coli in the acylation of lipid A: HtrB catalyzed incorporation of laurate. J. Biol. Chem. 271 (1996) 12095–12102. [DOI] [PMID: 8662613]
2.  van der Ley, P., Steeghs, L., Hamstra, H.J., ten Hove, J., Zomer, B. and van Alphen, L. Modification of lipid A biosynthesis in Neisseria meningitidis lpxL mutants: influence on lipopolysaccharide structure, toxicity, and adjuvant activity. Infect. Immun. 69 (2001) 5981–5990. [DOI] [PMID: 11553534]
3.  McLendon, M.K., Schilling, B., Hunt, J.R., Apicella, M.A. and Gibson, B.W. Identification of LpxL, a late acyltransferase of Francisella tularensis. Infect. Immun. 75 (2007) 5518–5531. [DOI] [PMID: 17724076]
4.  Six, D.A., Carty, S.M., Guan, Z. and Raetz, C.R. Purification and mutagenesis of LpxL, the lauroyltransferase of Escherichia coli lipid A biosynthesis. Biochemistry 47 (2008) 8623–8637. [DOI] [PMID: 18656959]
5.  Fathy Mohamed, Y., Hamad, M., Ortega, X.P. and Valvano, M.A. The LpxL acyltransferase is required for normal growth and penta-acylation of lipid A in Burkholderia cenocepacia. Mol. Microbiol. 104 (2017) 144–162. [DOI] [PMID: 28085228]
[EC 2.3.1.241 created 2014, modified 2021]
 
 
EC 2.3.1.242     
Accepted name: Kdo2-lipid IVA palmitoleoyltransferase
Reaction: a (9Z)-hexadec-9-enoyl-[acyl-carrier protein] + Kdo2-lipid IVA = (9Z)-hexadec-9-enoyl-Kdo2-lipid IVA + an [acyl-carrier protein]
For diagram of Kdo-Kdo-Lipid IVA metabolism, click here
Glossary: Kdo = 3-deoxy-D-manno-oct-2-ulopyranosylonic acid
lipid IVA = 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate
Kdo2-lipid IVA = α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA
(9Z)-hexadec-9-enoyl = palmitoleoyl
(9Z)-hexadec-9-enoyl-Kdo2-lipid IVA = α-Kdo-(2→4)-α-Kdo-(2→6)-2-deoxy-2-{(3R)-3-[(9Z)-hexadec-9-enoyl]tetradecanamido}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate
Other name(s): LpxP; palmitoleoyl-acyl carrier protein-dependent acyltransferase; cold-induced palmitoleoyl transferase; palmitoleoyl-[acyl-carrier protein]:Kdo2-lipid IVA O-palmitoleoyltransferase; (Kdo)2-lipid IVA palmitoleoyltransferase; α-Kdo-(2→4)-α-(2→6)-lipid IVA palmitoleoyltransferase
Systematic name: (9Z)-hexadec-9-enoyl-[acyl-carrier protein]:Kdo2-lipid IVA O-palmitoleoyltransferase
Comments: The enzyme, characterized from the bacterium Escherichia coli, is induced upon cold shock and is involved in the formation of a cold-adapted variant of the outer membrane glycolipid lipid A.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Carty, S.M., Sreekumar, K.R. and Raetz, C.R. Effect of cold shock on lipid A biosynthesis in Escherichia coli. Induction At 12 degrees C of an acyltransferase specific for palmitoleoyl-acyl carrier protein. J. Biol. Chem. 274 (1999) 9677–9685. [DOI] [PMID: 10092655]
2.  Vorachek-Warren, M.K., Carty, S.M., Lin, S., Cotter, R.J. and Raetz, C.R. An Escherichia coli mutant lacking the cold shock-induced palmitoleoyltransferase of lipid A biosynthesis: absence of unsaturated acyl chains and antibiotic hypersensitivity at 12 degrees C. J. Biol. Chem. 277 (2002) 14186–14193. [DOI] [PMID: 11830594]
[EC 2.3.1.242 created 2014]
 
 
EC 2.3.1.243     
Accepted name: acyl-Kdo2-lipid IVA acyltransferase
Reaction: a fatty acyl-[acyl-carrier protein] + an α-Kdo-(2→4)-α-Kdo-(2→6)-(acyl)-[lipid IVA] = an α-Kdo-(2→4)-α-Kdo-(2→6)-(acyl)2-[lipid IVA] + an [acyl-carrier protein]
For diagram of Kdo-Kdo-Lipid IVA metabolism, click here
Glossary: Kdo = 3-deoxy-D-manno-oct-2-ulopyranosylonic acid
a lipid IVA = 2-deoxy-2-{[(3R)-3-hydroxyacyl]amino}-3-O-[(3R)-3-hydroxyacyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-{[(3R)-3-hydroxyacyl]amino}-1-O-phospho-α-D-glucopyranose
an α-Kdo-(2→4)-α-Kdo-(2→6)-(acyl)-[lipid IVA] = 3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→4)-3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→6)-2-deoxy-2-{[(3R)-3-(acyloxy)acyl]amino}-3-O-[(3R)-3-hydroxyacyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-{[(3R)-3-hydroxyacyl]amino}-1-O-phosphono-α-D-glucopyranose
an α-Kdo-(2→4)-α-Kdo-(2→6)-(acyl)2-[lipid IVA] = 3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→4)-3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→6)-2-deoxy-2-{[(3R)-3-(acyloxy)acyl]amino}-3-O-[(3R)-3-(acyloxy)acyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-{[(3R)-3-hydroxyacyl]amino}-1-O-phospho-α-D-glucopyranose
Other name(s): lpxM (gene name); MsbB acyltransferase; myristoyl-[acyl-carrier protein]:α-Kdo-(2→4)-α-Kdo-(2→6)-(dodecanoyl)-lipid IVA O-myristoyltransferase; tetradecanoyl-[acyl-carrier protein]:dodecanoyl-Kdo2-lipid IVA O-tetradecanoyltransferase; lauroyl-Kdo2-lipid IVA myristoyltransferase
Systematic name: fatty acyl-[acyl-carrier protein]:α-Kdo-(2→4)-α-Kdo-(2→6)-(acyl)-[lipid IVA] O-acyltransferase
Comments: The enzyme is involved in the biosynthesis of the phosphorylated outer membrane glycolipid lipid A. It transfers an acyl group to the 3-O position of the 3R-hydroxyacyl already attached at the 2-O position of the non-reducing glucosamine molecule. The enzyme from the bacterium Escherichia coli is specific for myristoyl (C14) acyl groups, giving the enzyme its previous accepted name. However, enzymes from different species accept highly variable substrates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Clementz, T., Zhou, Z. and Raetz, C.R. Function of the Escherichia coli msbB gene, a multicopy suppressor of htrB knockouts, in the acylation of lipid A. Acylation by MsbB follows laurate incorporation by HtrB. J. Biol. Chem. 272 (1997) 10353–10360. [DOI] [PMID: 9099672]
2.  Dovala, D., Rath, C.M., Hu, Q., Sawyer, W.S., Shia, S., Elling, R.A., Knapp, M.S. and Metzger, L.E., 4th. Structure-guided enzymology of the lipid A acyltransferase LpxM reveals a dual activity mechanism. Proc. Natl. Acad. Sci. USA 113 (2016) E6064–E6071. [DOI] [PMID: 27681620]
[EC 2.3.1.243 created 2014, modified 2021]
 
 
EC 2.3.1.270     
Accepted name: lyso-ornithine lipid O-acyltransferase
Reaction: a lyso-ornithine lipid + an acyl-[acyl-carrier protein] = an ornithine lipid + a holo-[acyl-carrier protein]
Glossary: a lyso-ornithine lipid = an Nα-[(3R)-3-hydroxyacyl]-L-ornithine
an ornithine lipid = an Nα-[(3R)-3-(acyloxy)acyl]-L-ornithine
Other name(s): olsA (gene name)
Systematic name: Nα-[(3R)-hydroxy-acyl]-L-ornithine O-acyltransferase
Comments: This bacterial enzyme catalyses the second step in the formation of ornithine lipids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Weissenmayer, B., Gao, J.L., Lopez-Lara, I.M. and Geiger, O. Identification of a gene required for the biosynthesis of ornithine-derived lipids. Mol. Microbiol. 45 (2002) 721–733. [PMID: 12139618]
2.  Aygun-Sunar, S., Bilaloglu, R., Goldfine, H. and Daldal, F. Rhodobacter capsulatus OlsA is a bifunctional enzyme active in both ornithine lipid and phosphatidic acid biosynthesis. J. Bacteriol. 189 (2007) 8564–8574. [PMID: 17921310]
3.  Lewenza, S., Falsafi, R., Bains, M., Rohs, P., Stupak, J., Sprott, G.D. and Hancock, R.E. The olsA gene mediates the synthesis of an ornithine lipid in Pseudomonas aeruginosa during growth under phosphate-limiting conditions, but is not involved in antimicrobial peptide susceptibility. FEMS Microbiol. Lett. 320 (2011) 95–102. [DOI] [PMID: 21535098]
[EC 2.3.1.270 created 2018]
 
 
EC 2.3.1.274     
Accepted name: phosphate acyltransferase
Reaction: an acyl-[acyl-carrier protein] + phosphate = an acyl phosphate + an [acyl-carrier protein]
Other name(s): plsX (gene name); acyl-ACP phosphotransacylase; acyl-[acyl-carrier-protein]—phosphate acyltransferase; phosphate-acyl-ACP acyltransferase
Systematic name: an acyl-[acyl-carrier protein]:phosphate acyltransferase
Comments: The enzyme, found in bacteria, catalyses the synthesis of fatty acyl-phosphate from acyl-[acyl-carrier protein], a step in the most widely distributed bacterial pathway for the initiation of phospholipid formation. While the activity is modestly enhanced by Mg2+, the enzyme does not require a divalent cation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Lu, Y.J., Zhang, Y.M., Grimes, K.D., Qi, J., Lee, R.E. and Rock, C.O. Acyl-phosphates initiate membrane phospholipid synthesis in Gram-positive pathogens. Mol. Cell 23 (2006) 765–772. [PMID: 16949372]
2.  Yoshimura, M., Oshima, T. and Ogasawara, N. Involvement of the YneS/YgiH and PlsX proteins in phospholipid biosynthesis in both Bacillus subtilis and Escherichia coli. BMC Microbiol. 7:69 (2007). [PMID: 17645809]
3.  Kim, Y., Li, H., Binkowski, T.A., Holzle, D. and Joachimiak, A. Crystal structure of fatty acid/phospholipid synthesis protein PlsX from Enterococcus faecalis. J Struct Funct Genomics 10 (2009) 157–163. [PMID: 19058030]
4.  Kaczmarzyk, D., Cengic, I., Yao, L. and Hudson, E.P. Diversion of the long-chain acyl-ACP pool in Synechocystis to fatty alcohols through CRISPRi repression of the essential phosphate acyltransferase PlsX. Metab. Eng. 45 (2018) 59–66. [PMID: 29199103]
[EC 2.3.1.274 created 2018]
 
 
EC 2.3.1.277     
Accepted name: 2-oxo-3-(phosphooxy)propyl 3-oxoalkanoate synthase
Reaction: a medium-chain 3-oxoacyl-[acyl-carrier protein] + glycerone phosphate = 2-oxo-3-(phosphooxy)propyl 3-oxoalkanoate + a holo-[acyl-carrier protein]
Glossary: glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
Other name(s): afsA (gene name); scbA (gene name); barX (gene name)
Systematic name: 3-oxoacyl-[acyl-carrier protein]:glycerone phosphate 3-oxonacylltransferase
Comments: The enzyme catalyses the first committed step in the biosynthesis of γ-butyrolactone autoregulators that control secondary metabolism and morphological development in Streptomyces bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Horinouchi, S., Suzuki, H., Nishiyama, M. and Beppu, T. Nucleotide sequence and transcriptional analysis of the Streptomyces griseus gene (afsA) responsible for A-factor biosynthesis. J. Bacteriol. 171 (1989) 1206–1210. [PMID: 2492509]
2.  Kato, J.Y., Funa, N., Watanabe, H., Ohnishi, Y. and Horinouchi, S. Biosynthesis of γ-butyrolactone autoregulators that switch on secondary metabolism and morphological development in Streptomyces. Proc. Natl. Acad. Sci. USA 104 (2007) 2378–2383. [DOI] [PMID: 17277085]
3.  Hsiao, N.H., Soding, J., Linke, D., Lange, C., Hertweck, C., Wohlleben, W. and Takano, E. ScbA from Streptomyces coelicolor A3(2) has homology to fatty acid synthases and is able to synthesize γ-butyrolactones. Microbiology 153 (2007) 1394–1404. [PMID: 17464053]
4.  Lee, Y.J., Kitani, S. and Nihira, T. Null mutation analysis of an afsA-family gene, barX, that is involved in biosynthesis of the γ-butyrolactone autoregulator in Streptomyces virginiae. Microbiology 156 (2010) 206–210. [PMID: 19778967]
[EC 2.3.1.277 created 2018]
 
 
EC 2.3.1.293     
Accepted name: meromycolic acid 3-oxoacyl-(acyl carrier protein) synthase I
Reaction: an ultra-long-chain mono-unsaturated acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = an ultra-long-chain mono-unsaturated 3-oxo-fatty acyl-[acyl-carrier protein] + CO2 + a holo-[acyl-carrier protein]
Other name(s): kasA (gene name); β-ketoacyl-acyl carrier protein synthase KasA
Systematic name: ultra-long-chain mono-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. KasA differs from KasB [EC 2.3.1.294, meromycolic acid 3-oxoacyl-(acyl carrier protein) synthase II], by preferring shorter (C-22 to C-36) and more saturated (only one double bond) substrates.
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.  Bhatt, A., Kremer, L., Dai, A.Z., Sacchettini, J.C. and Jacobs, W.R., Jr. Conditional depletion of KasA, a key enzyme of mycolic acid biosynthesis, leads to mycobacterial cell lysis. J. Bacteriol. 187 (2005) 7596–7606. [PMID: 16267284]
3.  Luckner, S.R., Machutta, C.A., Tonge, P.J. and Kisker, C. Crystal structures of Mycobacterium tuberculosis KasA show mode of action within cell wall biosynthesis and its inhibition by thiolactomycin. Structure 17 (2009) 1004–1013. [PMID: 19604480]
[EC 2.3.1.293 created 2019]
 
 
EC 2.3.1.294     
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 2.3.1.300     
Accepted name: branched-chain β-ketoacyl-[acyl-carrier-protein] synthase
Reaction: (1) 3-methylbutanoyl-CoA + a malonyl-[acyl-carrier protein] = a 5-methyl-3-oxohexanoyl-[acyl-carrier-protein] + CoA + CO2
(2) 2-methylpropanoyl-CoA + a malonyl-[acyl-carrier protein] = a 4-methyl-3-oxopentanoyl-[acyl-carrier-protein] + CoA + CO2
(3) (2S)-2-methylbutanoyl-CoA + a malonyl-[acyl-carrier protein] = a (4S)-4-methyl-3-oxohexanoyl-[acyl-carrier-protein] + CoA + CO2
Glossary: 3-methylbutanoyl-CoA = isovaleryl-CoA
2-methylpropanoyl-CoA = isobutanoyl-CoA = isobutyryl-CoA
Systematic name: 3-methylbutanoyl-CoA:malonyl-[acyl-carrier protein] C-acyltransferase
Comments: The enzyme is responsible for initiating branched-chain fatty acid biosynthesis by the dissociated (or type II) fatty-acid biosynthesis system (FAS-II) in some bacteria, using molecules derived from degradation of the branched-chain amino acids L-leucine, L-valine, and L-isoleucine to form the starting molecules for elongation by the FAS-II system. In some organisms the enzyme is also able to use acetyl-CoA, leading to production of a mix of branched-chain and straight-chain fatty acids [3] (cf. EC 2.3.1.180, β-ketoacyl-[acyl-carrier-protein] synthase III).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  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]
2.  Choi, K.H., Heath, R.J. and Rock, C.O. β-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis. J. Bacteriol. 182 (2000) 365–370. [DOI] [PMID: 10629181]
3.  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]
4.  Singh, A.K., Zhang, Y.M., Zhu, K., Subramanian, C., Li, Z., Jayaswal, R.K., Gatto, C., Rock, C.O. and Wilkinson, B.J. FabH selectivity for anteiso branched-chain fatty acid precursors in low-temperature adaptation in Listeria monocytogenes. FEMS Microbiol. Lett. 301 (2009) 188–192. [DOI] [PMID: 19863661]
5.  Yu, Y.H., Hu, Z., Dong, H.J., Ma, J.C. and Wang, H.H. Xanthomonas campestris FabH is required for branched-chain fatty acid and DSF-family quorum sensing signal biosynthesis. Sci. Rep. 6:32811 (2016). [DOI] [PMID: 27595587]
[EC 2.3.1.300 created 2021]
 
 
EC 2.3.1.301     
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 2.3.1.305     
Accepted name: acyl-[acyl-carrier protein]—UDP-2-acetamido-3-amino-2,3-dideoxy-α-D-glucopyranose N-acyltransferase
Reaction: a (3R)-3-hydroxyacyl-[acyl-carrier protein] + UDP-2-acetamido-3-amino-2,3-dideoxy-α-D-glucopyranose = an [acyl-carrier protein] + a UDP-2-acetamido-2,3-dideoxy-3-{[(3R)-3-hydroxyacyl]amino}-α-D-glucopyranose
Other name(s): lpxA (gene name) (ambiguous)
Systematic name: (3R)-3-hydroxyacyl-[acyl-carrier-protein]:UDP-2-acetamido-3-amino-2,3-dideoxy-α-D-glucopyranose 3-N-[(3R)-hydroxyacyl]transferase
Comments: The enzyme is found in bacterial species whose lipid A contains 2,3-diamino-2,3-dideoxy-D-glucopyranose. Some enzymes, such as that from Leptospira interrogans, are highly specific for 2,3-diamino-2,3-dideoxy-D-glucopyranose, while others, such as the enzyme from Acidithiobacillus ferrooxidans, are also able to accept UDP-N-acetyl-α-D-glucosamine (cf. EC 2.3.1.129, acyl-[acyl-carrier-protein]—UDP-N-acetylglucosamine O-acyltransferase). The enzymes from different organisms also differ in their specificity for the acyl donor. The enzyme from Leptospira interrogans is highly specific for (3R)-3-hydroxydodecanoyl-[acp], while that from Mesorhizobium loti functions almost equally well with 10-, 12-, and 14-carbon 3-hydroxyacyl-[acp]s.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Sweet, C.R., Williams, A.H., Karbarz, M.J., Werts, C., Kalb, S.R., Cotter, R.J. and Raetz, C.R. Enzymatic synthesis of lipid A molecules with four amide-linked acyl chains. LpxA acyltransferases selective for an analog of UDP-N-acetylglucosamine in which an amine replaces the 3"-hydroxyl group. J. Biol. Chem. 279 (2004) 25411–25419. [DOI] [PMID: 15044493]
2.  Robins, L.I., Williams, A.H. and Raetz, C.R. Structural basis for the sugar nucleotide and acyl-chain selectivity of Leptospira interrogans LpxA. Biochemistry 48 (2009) 6191–6201. [DOI] [PMID: 19456129]
[EC 2.3.1.305 created 2021]
 
 
EC 2.3.2.30     
Accepted name: L-ornithine Nα-acyltransferase
Reaction: L-ornithine + a (3R)-3-hydroxyacyl-[acyl-carrier protein] = a lyso-ornithine lipid + a holo-[acyl-carrier protein]
Glossary: a lyso-ornithine lipid = an Nα-[(3R)-hydroxy-acyl]-L-ornithine
Other name(s): olsB (gene name)
Systematic name: L-ornithine Nα-(3R)-3-hydroxy-acyltransferase
Comments: The enzyme, found in bacteria, catalyses the first step in the biosynthesis of ornithine lipids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Gao, J.L., Weissenmayer, B., Taylor, A.M., Thomas-Oates, J., Lopez-Lara, I.M. and Geiger, O. Identification of a gene required for the formation of lyso-ornithine lipid, an intermediate in the biosynthesis of ornithine-containing lipids. Mol. Microbiol. 53 (2004) 1757–1770. [DOI] [PMID: 15341653]
2.  Vences-Guzman, M.A., Guan, Z., Bermudez-Barrientos, J.R., Geiger, O. and Sohlenkamp, C. Agrobacteria lacking ornithine lipids induce more rapid tumour formation. Environ. Microbiol. 15 (2013) 895–906. [DOI] [PMID: 22958119]
[EC 2.3.2.30 created 2017]
 
 
EC 2.3.3.22     
Accepted name: 3-carboxymethyl-3-hydroxy-acyl-[acp] synthase
Reaction: an acetyl-[acp] + a 3-oxoacyl-[acp] = a 3-carboxymethyl-3-hydroxy-acyl-[acp] + [acp]
Other name(s): HMG-CoA synthase-like enzyme; aprE (gene name); curD (gene name); corE (gene name); bryR (gene name); pedP (gene name); 3-carboxymethyl-3-hydroxy-acyl-[acyl-carrier protein] synthase
Systematic name: acetyl-[acp]:3-oxoacyl-[acp] C-acetyltransferase (thioester-hydrolysing, carboxymethyl-forming)
Comments: This family of enzymes participates in a process that introduces a methyl branch into nascent polyketide products. The process begins with EC 4.1.1.124, malonyl-[acp] decarboxylase, which converts the common extender unit malonyl-[acp] to acetyl-[acp]. The enzyme is a mutated form of a ketosynthase enzyme, in which a Cys residue in the active site is modified to a Ser residue, leaving the decarboxylase function intact, but nulifying the ability of the enzyme to form a carbon-carbon bond. Next, EC 2.3.3.22, 3-carboxymethyl-3-hydroxy-acyl-[acp] synthase, utilizes the acetyl group to introduce the branch at the β position of 3-oxoacyl intermediates attached to a polyketide synthase, forming a 3-hydroxy-3-carboxymethyl intermediate. This is followed by dehydration catalysed by EC 4.2.1.181, 3-carboxymethyl-3-hydroxy-acyl-[acp] dehydratase (often referred to as an ECH1 domain), leaving a 3-carboxymethyl group and forming a double bond between the α and β carbons. The process concludes with decarboxylation catalysed by EC 4.1.1.125, 4-carboxy-3-alkylbut-2-enoyl-[acp] decarboxylase (often referred to as an ECH2 domain), leaving a methyl branch at the β carbon. The enzymes are usually encoded by a cluster of genes referred to as an "HMGS cassette", based on the similarity of the key enzyme to EC 2.3.3.10, hydroxymethylglutaryl-CoA synthase. While the enzyme is similar to EC 2.3.3.10, it is specific for an [acyl-carrier protein] (acp)-bound donor and does not interact with a CoA substrate as donor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Erol, O., Schaberle, T.F., Schmitz, A., Rachid, S., Gurgui, C., El Omari, M., Lohr, F., Kehraus, S., Piel, J., Muller, R. and Konig, G.M. Biosynthesis of the myxobacterial antibiotic corallopyronin A. Chembiochem 11 (2010) 1253–1265. [DOI] [PMID: 20503218]
2.  Buchholz, T.J., Rath, C.M., Lopanik, N.B., Gardner, N.P., Hakansson, K. and Sherman, D.H. Polyketide β-branching in bryostatin biosynthesis: identification of surrogate acetyl-ACP donors for BryR, an HMG-ACP synthase. Chem. Biol. 17 (2010) 1092–1100. [DOI] [PMID: 21035732]
3.  Grindberg, R.V., Ishoey, T., Brinza, D., Esquenazi, E., Coates, R.C., Liu, W.T., Gerwick, L., Dorrestein, P.C., Pevzner, P., Lasken, R. and Gerwick, W.H. Single cell genome amplification accelerates identification of the apratoxin biosynthetic pathway from a complex microbial assemblage. PLoS One 6:e18565 (2011). [DOI] [PMID: 21533272]
4.  Maloney, F.P., Gerwick, L., Gerwick, W.H., Sherman, D.H. and Smith, J.L. Anatomy of the β-branching enzyme of polyketide biosynthesis and its interaction with an acyl-ACP substrate. Proc. Natl. Acad. Sci. USA 113 (2016) 10316–10321. [DOI] [PMID: 27573844]
5.  Slocum, S.T., Lowell, A.N., Tripathi, A., Shende, V.V., Smith, J.L. and Sherman, D.H. Chemoenzymatic dissection of polyketide β-branching in the bryostatin pathway. Methods Enzymol. 604 (2018) 207–236. [DOI] [PMID: 29779653]
[EC 2.3.3.22 created 2023]
 
 


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