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MetaCyc Reaction: 2.3.1.86

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: 2.3.1.86

Enzymes and Genes:

Arabidopsis thaliana col : 3-oxoacyl-[acyl-carrier-protein] reductase, chloroplastic Inferred from experiment : 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 Inferred by computational analysis : fas
Pseudomonas aeruginosa : NADPH-dependent β-ketoacyl reductase : rhlG
Saccharomyces cerevisiae : fatty acid synthase, α subunit : FAS2

In Pathway: palmitate biosynthesis I (animals and fungi) , palmitate biosynthesis II (bacteria and plants)

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.

Direct generic reaction:
a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+ ← a 3-oxoacyl-[acp] + NADPH + H+ (2.3.1.86)

Enzyme Commission Primary Name: fatty-acyl-CoA synthase

Enzyme Commission Synonyms: yeast fatty acid synthase, FAS1 (gene name), FAS2 (gene name)

Standard Gibbs Free Energy (ΔrG in kcal/mol): 20.375793 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
The enzyme from yeasts (Ascomycota and Basidiomycota) is a multi-functional protein complex composed of two subunits. One subunit catalyses the reactions EC 1.1.1.100, 3-oxoacyl-[acyl-carrier-protein] reductase and EC 2.3.1.41, β-ketoacyl-[acyl-carrier-protein] synthase I, while the other subunit catalyses the reactions of EC 2.3.1.38, [acyl-carrier-protein] S-acetyltransferase, EC 2.3.1.39, [acyl-carrier-protein] S-malonyltransferase, EC 4.2.1.59, 3-hydroxyacyl-[acyl-carrier-protein] dehydratase, EC 1.3.1.10, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and EC 1.1.1.279, (R)-3-hydroxyacid-ester dehydrogenase. The enzyme differs from the animal enzyme (EC 2.3.1.85) 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.

Citations: [Schweizer73, Wakil83, Tehlivets07]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Instance reaction of [a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+ ← a 3-oxoacyl-[acp] + NADPH + H+] (2.3.1.86):
i1: a (3R)-3-hydroxyoctanoyl-[acp] + NADP+ ← a 3-oxo-octanoyl-[acp] + NADPH + H+ (2.3.1.86)

Relationship Links: BRENDA:EC:2.3.1.86 , ENZYME:EC:2.3.1.86 , IUBMB-ExplorEnz:EC:2.3.1.86


References

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Schweizer73: Schweizer E, Kniep B, Castorph H, Holzner U (1973). "Pantetheine-free mutants of the yeast fatty-acid-synthetase complex." Eur J Biochem 39(2);353-62. PMID: 4590449

Tehlivets07: Tehlivets O, Scheuringer K, Kohlwein SD (2007). "Fatty acid synthesis and elongation in yeast." Biochim Biophys Acta 1771(3);255-70. PMID: 16950653

Wakil83: Wakil SJ, Stoops JK, Joshi VC (1983). "Fatty acid synthesis and its regulation." Annu Rev Biochem 52;537-79. PMID: 6137188


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 19.0 on Wed Jul 29, 2015, biocyc14.