|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 reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Mass balance status: Balanced.
Enzyme Commission Primary Name for 126.96.36.199: [acyl-carrier-protein] S-acetyltransferase
Enzyme Commission Synonyms for 188.8.131.52: 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 184.108.40.206: fatty-acid synthase
Enzyme Commission Synonyms for 220.127.116.11: FASN (gene name)
Enzyme Commission Primary Name for 18.104.22.168: fatty-acyl-CoA synthase
Enzyme Commission Synonyms for 22.214.171.124: yeast fatty acid synthase, FAS1 (gene name), FAS2 (gene name)
One of the initial reactions in fatty acid biosynthesis.
Enzyme Commission Summary for 126.96.36.199:
This enzyme, along with EC 188.8.131.52, [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 184.108.40.206) [Tsay92].
Enzyme Commission Summary for 220.127.116.11:
The animal enzyme is a multi-functional protein catalysing the reactions of EC 18.104.22.168, [acyl-carrier-protein] S-acetyltransferase, EC 22.214.171.124, [acyl-carrier-protein] S-malonyltransferase, EC 126.96.36.199, β-ketoacyl-[acyl-carrier-protein] synthase I, EC 188.8.131.52, 3-oxoacyl-[acyl-carrier-protein] reductase, EC 184.108.40.206, 3-hydroxyacyl-[acyl-carrier-protein] dehydratase, EC 220.127.116.11, enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific) and EC 18.104.22.168, oleoyl-[acyl-carrier-protein] hydrolase. cf. EC 22.214.171.124, fatty-acyl-CoA synthase.
Enzyme Commission Summary for 126.96.36.199:
The enzyme from yeasts (Ascomycota and Basidiomycota) is a multi-functional protein complex composed of two subunits. One subunit catalyses the reactions EC 188.8.131.52, 3-oxoacyl-[acyl-carrier-protein] reductase and EC 184.108.40.206, β-ketoacyl-[acyl-carrier-protein] synthase I, while the other subunit catalyses the reactions of EC 220.127.116.11, [acyl-carrier-protein] S-acetyltransferase, EC 18.104.22.168, [acyl-carrier-protein] S-malonyltransferase, EC 22.214.171.124, 3-hydroxyacyl-[acyl-carrier-protein] dehydratase, EC 126.96.36.199, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and EC 188.8.131.529, (R)-3-hydroxyacid-ester dehydrogenase. The enzyme differs from the animal enzyme (EC 184.108.40.206) 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:220.127.116.11 , BRENDA:EC:18.104.22.168 , BRENDA:EC:22.214.171.124 , ENZYME:EC:126.96.36.199 , ENZYME:EC:188.8.131.52 , ENZYME:EC:184.108.40.206 , IUBMB-ExplorEnz:EC:220.127.116.11 , IUBMB-ExplorEnz:EC:18.104.22.168 , IUBMB-ExplorEnz:EC:22.214.171.124
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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