|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions → Protein-Modification Reactions|
|Reactions Classified By Substrate → Macromolecule Reactions → Protein-Reactions → Protein-Modification Reactions|
EC Number: 22.214.171.124
Enzymes and Genes:
|Escherichia coli K-12 substr. MG1655 :||3-oxoacyl-[acyl-carrier-protein] reductase
|Mycobacterium tuberculosis H37Rv :||3-oxoacyl-[acyl-carrier-protein] reductase
In Pathway: mycolate biosynthesis
Note that this reaction equation differs from the official Enzyme Commission reaction equation for this EC number, which can be found here .
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
Enzyme Commission Primary Name: 3-oxoacyl-[acyl-carrier-protein] reductase
Enzyme Commission Synonyms: 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
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): 20.375793 [Latendresse13]
Enzyme Commission Summary:
Exhibits a marked preference for acyl-carrier-protein derivatives over CoA derivatives as substrates.
Instance reaction of [a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+ ← a 3-oxoacyl-[acp] + NADPH + H+] (126.96.36.199/188.8.131.52/184.108.40.206):
i1: a cis-delta5-3-hydroxyC24:1-[acp] + NADP+ ← a cis-delta5-3-oxo-C24:1-[acp] + NADPH + H+ (220.127.116.11)
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
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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