twitter

Escherichia coli K-12 substr. MG1655 Reaction: 2.3.1.39/2.3.1.85/2.3.1.86

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: 2.3.1.39 , 2.3.1.85 , 2.3.1.86

Enzymes and Genes:
malonyl-CoA-ACP transacylase Inferred from experiment : fabD

In Pathway: fatty acid biosynthesis initiation I

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 2.3.1.39: [acyl-carrier-protein] S-malonyltransferase

Enzyme Commission Synonyms for 2.3.1.39: [acyl carrier protein]malonyltransferase, FabD, malonyl coenzyme A-acyl carrier protein transacylase, malonyl transacylase, malonyl transferase, malonyl-CoA-acyl carrier protein transacylase, malonyl-CoA:[acyl-carrier-protein] S-malonyltransferase, malonyl-CoA:ACP transacylase, malonyl-CoA:ACP-SH transacylase, malonyl-CoA:AcpM transacylase, malonyl-CoA:acyl carrier protein transacylase, malonyl-CoA:acyl-carrier-protein transacylase, malonyl-CoA/dephospho-CoA acyltransferase, MAT, MCAT, MdcH

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:
This reaction prepares malonate for use in the biosynthesis of fatty acids. The energy-rich bonds in acyl-CoAs and acyl-ACPs are identical.

Enzyme Commission Summary for 2.3.1.39:
This enzyme, along with EC 2.3.1.38, [acyl-carrier-protein] S-acetyltransferase, is essential for the initiation of fatty-acid biosynthesis in bacteria. This enzyme also provides the malonyl groups for polyketide biosynthesis [Szafranska02]. The product of the reaction, malonyl-ACP, is an elongation substrate in fatty-acid biosynthesis. In Mycobacterium tuberculosis, holo-ACP (the product of EC 2.7.8.7, holo-[acyl-carrier-protein] synthase) is the preferred substrate [Kremer01]. This enzyme also forms part of the multienzyme complexes EC 4.1.1.88, biotin-independent malonate decarboxylase and EC 4.1.1.89, biotin-dependent malonate decarboxylase. Malonylation of ACP is immediately followed by decarboxylation within the malonate-decarboxylase complex to yield acetyl-ACP, the catalytically active species of the decarboxylase [Dimroth97]. In the enzyme from Klebsiella pneumoniae, methylmalonyl-CoA can also act as a substrate but acetyl-CoA cannot [Hoenke99] whereas the enzyme from Pseudomonas putida can use both as substrates [Chohnan98]. The ACP subunit found in fatty-acid biosynthesis contains a pantetheine-4'-phosphate prosthetic group; that from malonate decarboxylase also contains pantetheine-4'-phosphate but in the form of a 2'-(5-triphosphoribosyl)-3'-dephospho-CoA prosthetic group.

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, Williamson66, Joshi71, KeatingeClay03, Hoenke97, Koo99, Stoops79, Wakil83, Schweizer73, Tehlivets07]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Relationship Links: BRENDA:EC:2.3.1.39 , BRENDA:EC:2.3.1.85 , BRENDA:EC:2.3.1.86 , ENZYME:EC:2.3.1.39 , ENZYME:EC:2.3.1.85 , ENZYME:EC:2.3.1.86 , IUBMB-ExplorEnz:EC:2.3.1.39 , IUBMB-ExplorEnz:EC:2.3.1.85 , IUBMB-ExplorEnz:EC:2.3.1.86


References

Chohnan98: Chohnan S, Fujio T, Takaki T, Yonekura M, Nishihara H, Takamura Y (1998). "Malonate decarboxylase of Pseudomonas putida is composed of five subunits." FEMS Microbiol Lett 169(1);37-43. PMID: 9851033

Dimroth97: Dimroth P, Hilbi H (1997). "Enzymic and genetic basis for bacterial growth on malonate." Mol Microbiol 25(1);3-10. PMID: 11902724

Hoenke97: Hoenke S, Schmid M, Dimroth P (1997). "Sequence of a gene cluster from Klebsiella pneumoniae encoding malonate decarboxylase and expression of the enzyme in Escherichia coli." Eur J Biochem 246(2);530-8. PMID: 9208947

Hoenke99: Hoenke S, Dimroth P (1999). "Formation of catalytically active acetyl-S-malonate decarboxylase requires malonyl-coenzyme A:acyl carrier protein transacylase as auxiliary enzyme [corrected]." Eur J Biochem 259(1-2);181-7. PMID: 9914491

Joshi71: Joshi VC, Wakil SJ (1971). "Studies on the mechanism of fatty acid synthesis. XXVI. Purification and properties of malonyl-coenzyme A--acyl carrier protein transacylase of Escherichia coli." Arch Biochem Biophys 1971;143(2);493-505. PMID: 4934182

KeatingeClay03: Keatinge-Clay AT, Shelat AA, Savage DF, Tsai SC, Miercke LJ, O'Connell JD, Khosla C, Stroud RM (2003). "Catalysis, specificity, and ACP docking site of Streptomyces coelicolor malonyl-CoA:ACP transacylase." Structure 11(2);147-54. PMID: 12575934

Koo99: Koo JH, Kim YS (1999). "Functional evaluation of the genes involved in malonate decarboxylation by Acinetobacter calcoaceticus." Eur J Biochem 266(2);683-90. PMID: 10561613

Kremer01: Kremer L, Nampoothiri KM, Lesjean S, Dover LG, Graham S, Betts J, Brennan PJ, Minnikin DE, Locht C, Besra GS (2001). "Biochemical characterization of acyl carrier protein (AcpM) and malonyl-CoA:AcpM transacylase (mtFabD), two major components of Mycobacterium tuberculosis fatty acid synthase II." J Biol Chem 276(30);27967-74. PMID: 11373295

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

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

Szafranska02: Szafranska AE, Hitchman TS, Cox RJ, Crosby J, Simpson TJ (2002). "Kinetic and mechanistic analysis of the malonyl CoA:ACP transacylase from Streptomyces coelicolor indicates a single catalytically competent serine nucleophile at the active site." Biochemistry 41(5);1421-7. PMID: 11814333

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

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 Fri Jul 31, 2015, biocyc14.