|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions → Protein-Modification Reactions|
|Reactions Classified By Substrate → Macromolecule Reactions → Protein-Reactions → Protein-Modification Reactions|
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.
Mass balance status: Balanced.
Enzyme Commission Primary Name for 220.127.116.11: [acyl-carrier-protein] S-acetyltransferase
Enzyme Commission Synonyms for 18.104.22.168: acetyl coenzyme A-acyl-carrier-protein transacylase, [acyl-carrier-protein]acetyltransferase, [ACP]acetyltransferase, ACAT, acetyl-CoA:[acyl-carrier-protein] S-acetyltransferase
Enzyme Commission Primary Name for 22.214.171.124: fatty-acid synthase
Enzyme Commission Synonyms for 126.96.36.199: FASN (gene name)
Enzyme Commission Primary Name for 188.8.131.52: fatty-acyl-CoA synthase
Enzyme Commission Synonyms for 184.108.40.206: yeast fatty acid synthase, FAS1 (gene name), FAS2 (gene name)
One of the initial reactions in fatty acid biosynthesis.
Enzyme Commission Summary for 220.127.116.11:
This enzyme, along with EC 18.104.22.168, [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 [Lowe88]. This is one of the activities associated with β-ketoacyl-ACP synthase III ( EC 22.214.171.124) [Tsay92].
Enzyme Commission Summary for 126.96.36.199:
The animal enzyme is a multi-functional protein catalysing the reactions of EC 188.8.131.52, [acyl-carrier-protein] S-acetyltransferase, EC 184.108.40.206, [acyl-carrier-protein] S-malonyltransferase, EC 220.127.116.11, β-ketoacyl-[acyl-carrier-protein] synthase I, EC 18.104.22.168, 3-oxoacyl-[acyl-carrier-protein] reductase, EC 22.214.171.124, 3-hydroxyacyl-[acyl-carrier-protein] dehydratase, EC 126.96.36.199, enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific) and EC 188.8.131.52, oleoyl-[acyl-carrier-protein] hydrolase. cf. EC 184.108.40.206, fatty-acyl-CoA synthase.
Enzyme Commission Summary for 220.127.116.11:
The enzyme from yeasts ( Ascomycota and Basidiomycota) is a multi-functional protein complex composed of two subunits. One subunit catalyses the reactions EC 18.104.22.168, 3-oxoacyl-[acyl-carrier-protein] reductase and EC 22.214.171.124, β-ketoacyl-[acyl-carrier-protein] synthase I, while the other subunit catalyses the reactions of EC 126.96.36.199, [acyl-carrier-protein] S-acetyltransferase, EC 188.8.131.52, [acyl-carrier-protein] S-malonyltransferase, EC 184.108.40.206, 3-hydroxyacyl-[acyl-carrier-protein] dehydratase, EC 220.127.116.11, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and EC 18.104.22.1689, (R)-3-hydroxyacid-ester dehydrogenase. The enzyme differs from the animal enzyme ( EC 22.214.171.124) in that the enoyl reductase domain requires FMN as a cofactor, and the ultimate product is an acyl-CoA (usually palmitoyl-CoA) instead of a free fatty acid.
Relationship Links: BRENDA:EC:126.96.36.199, BRENDA:EC:188.8.131.52, BRENDA:EC:184.108.40.206, ENZYME:EC:220.127.116.11, ENZYME:EC:18.104.22.168, ENZYME:EC:22.214.171.124, IUBMB-ExplorEnz:EC:126.96.36.199, IUBMB-ExplorEnz:EC:188.8.131.52, IUBMB-ExplorEnz:EC:184.108.40.206
Rangan97: Rangan VS, Smith S (1997). "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(18);11975-8. PMID: 9115261
Stoops79: Stoops JK, Ross P, Arslanian MJ, Aune KC, Wakil SJ, Oliver RM (1979). "Physicochemical studies of the rat liver and adipose fatty acid synthetases." J Biol Chem 254(15);7418-26. PMID: 457689
Tsay92: Tsay JT, Oh W, Larson TJ, Jackowski S, Rock CO (1992). "Isolation and characterization of the beta-ketoacyl-acyl carrier protein synthase III gene (fabH) from Escherichia coli K-12." J Biol Chem 1992;267(10);6807-14. PMID: 1551888
Williamson66: Williamson IP, Wakil SJ (1966). "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(10);2326-32. PMID: 5330116
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