|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions → Protein-Modification Reactions|
|Reactions Classified By Substrate → Macromolecule Reactions → Protein-Reactions → Protein-Modification Reactions|
Enzymes and Genes:
|Arabidopsis thaliana col:||3-oxoacyl-[acyl-carrier-protein] reductase, chloroplastic: AT1G24360|
|Escherichia coli K-12 substr. MG1655:||3-oxoacyl-[acyl-carrier-protein] reductase: fabG|
|Homo sapiens:||fatty acid synthase: FASN|
|Mycobacterium tuberculosis H37Rv:||fatty acid synthase: fas|
|Pseudomonas aeruginosa:||NADPH-dependent β-ketoacyl reductase: rhlG|
|Saccharomyces cerevisiae:||fatty acid synthase, α subunit: FAS2|
Note that this reaction equation differs from the official Enzyme Commission reaction equation for this EC number, which can be found here .
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.
Most BioCyc compounds have been protonated to a reference pH value of 7.3. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
Enzyme Commission Primary Name for 188.8.131.52: 3-oxoacyl-[acyl-carrier-protein] reductase
Enzyme Commission Synonyms for 184.108.40.206: 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
Enzyme Commission Primary Name for 220.127.116.11: fatty-acid synthase
Enzyme Commission Synonyms for 18.104.22.168: FASN (gene name)
Enzyme Commission Primary Name for 22.214.171.124: fatty-acyl-CoA synthase
Enzyme Commission Synonyms for 126.96.36.199: yeast fatty acid synthase, FAS1 (gene name), FAS2 (gene name)
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): 20.375793 [Latendresse13]
Enzyme Commission Summary for 188.8.131.52:
Exhibits a marked preference for acyl-carrier-protein derivatives over CoA derivatives as substrates.
Enzyme Commission Summary for 184.108.40.206:
The animal enzyme is a multi-functional protein catalysing 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, β-ketoacyl-[acyl-carrier-protein] synthase I, EC 126.96.36.199, 3-oxoacyl-[acyl-carrier-protein] reductase, EC 188.8.131.52, 3-hydroxyacyl-[acyl-carrier-protein] dehydratase, EC 184.108.40.206, enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific) and EC 220.127.116.11, oleoyl-[acyl-carrier-protein] hydrolase. cf. EC 18.104.22.168, fatty-acyl-CoA synthase.
Enzyme Commission Summary for 22.214.171.124:
The enzyme from yeasts ( Ascomycota and Basidiomycota) is a multi-functional protein complex composed of two subunits. One subunit catalyses the reactions EC 126.96.36.199, 3-oxoacyl-[acyl-carrier-protein] reductase and EC 188.8.131.52, β-ketoacyl-[acyl-carrier-protein] synthase I, while the other subunit catalyses the reactions of EC 184.108.40.206, [acyl-carrier-protein] S-acetyltransferase, EC 220.127.116.11, [acyl-carrier-protein] S-malonyltransferase, EC 18.104.22.168, 3-hydroxyacyl-[acyl-carrier-protein] dehydratase, EC 22.214.171.124, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and EC 126.96.36.1999, (R)-3-hydroxyacid-ester dehydrogenase. The enzyme differs from the animal enzyme ( EC 188.8.131.52) 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:184.108.40.206, BRENDA:EC:220.127.116.11, BRENDA:EC:18.104.22.168, ENZYME:EC:22.214.171.124, ENZYME:EC:126.96.36.199, ENZYME:EC:188.8.131.52, IUBMB-ExplorEnz:EC:184.108.40.206, IUBMB-ExplorEnz:EC:220.127.116.11, IUBMB-ExplorEnz:EC:18.104.22.168
Shimakata82: Shimakata T, Stumpf PK (1982). "Purification and characterizations of beta-Ketoacyl-[acyl-carrier-protein] reductase, beta-hydroxyacyl-[acyl-carrier-protein] dehydrase, and enoyl-[acyl-carrier-protein] reductase from Spinacia oleracea leaves." Arch Biochem Biophys 218(1);77-91. PMID: 6756317
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
Toomey66: Toomey RE, Wakil SJ (1966). "Studies on the mechanism of fatty acid synthesis. XV. Preparation and general properties of beta-ketoacyl acyl carrier protein reductase from Escherichia coli." Biochim Biophys Acta 116(2);189-97. PMID: 4381013
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