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Escherichia coli K-12 substr. MG1655 Reaction: 2.3.1.38/2.3.1.85/2.3.1.86

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: 2.3.1.38 , 2.3.1.85 , 2.3.1.86

Enzymes and Genes:
KASIII Inferred from experiment : fabH

In Pathway: fatty acid biosynthesis initiation II , superpathway of fatty acid biosynthesis initiation (E. coli)

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 2.3.1.38: [acyl-carrier-protein] S-acetyltransferase

Enzyme Commission Synonyms for 2.3.1.38: 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 2.3.1.85: fatty-acid synthase

Enzyme Commission Synonyms for 2.3.1.85: FASN (gene name)

Enzyme Commission Primary Name for 2.3.1.86: fatty-acyl-CoA synthase

Enzyme Commission Synonyms for 2.3.1.86: yeast fatty acid synthase, FAS1 (gene name), FAS2 (gene name)

Summary:
One of the initial reactions in fatty acid biosynthesis.

Enzyme Commission Summary for 2.3.1.38:
This enzyme, along with EC 2.3.1.39, [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 2.3.1.180) [Tsay92].

Enzyme Commission Summary for 2.3.1.85:
The animal enzyme is a multi-functional protein catalysing the reactions of EC 2.3.1.38, [acyl-carrier-protein] S-acetyltransferase, EC 2.3.1.39, [acyl-carrier-protein] S-malonyltransferase, EC 2.3.1.41, β-ketoacyl-[acyl-carrier-protein] synthase I, EC 1.1.1.100, 3-oxoacyl-[acyl-carrier-protein] reductase, EC 4.2.1.59, 3-hydroxyacyl-[acyl-carrier-protein] dehydratase, EC 1.3.1.39, enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific) and EC 3.1.2.14, oleoyl-[acyl-carrier-protein] hydrolase. cf. EC 2.3.1.86, fatty-acyl-CoA synthase.

Enzyme Commission Summary for 2.3.1.86:
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: [Prescott72, Vance73, Williamson66, Rangan97, Stoops79, Wakil83, Schweizer73, Tehlivets07]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Relationship Links: BRENDA:EC:2.3.1.38 , BRENDA:EC:2.3.1.85 , BRENDA:EC:2.3.1.86 , ENZYME:EC:2.3.1.38 , ENZYME:EC:2.3.1.85 , ENZYME:EC:2.3.1.86 , IUBMB-ExplorEnz:EC:2.3.1.38 , IUBMB-ExplorEnz:EC:2.3.1.85 , IUBMB-ExplorEnz:EC:2.3.1.86


References

Lowe88: Lowe PN, Rhodes S (1988). "Purification and characterization of [acyl-carrier-protein] acetyltransferase from Escherichia coli." Biochem J 1988;250(3);789-96. PMID: 3291856

Prescott72: Prescott DJ, Vagelos PR (1972). "Acyl carrier protein." Adv Enzymol Relat Areas Mol Biol 36;269-311. PMID: 4561013

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

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

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

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

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

Vance73: Vance DE, Mitsuhashi O, Bloch K (1973). "Purification and properties of the fatty acid synthetase from Mycobacterium phlei." J Biol Chem 248(7);2303-9. PMID: 4698221

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

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


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 19.0 on Sat Sep 5, 2015, BIOCYC14B.