(acyl-carrier-protein) S-malonyltransferase

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[acyl-carrier-protein] S-malonyltransferase
Identifiers
EC number 2.3.1.39
CAS number 37257-17-3
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO

In enzymology, a [acyl-carrier-protein] S-malonyltransferase (EC 2.3.1.39) is an enzyme that catalyzes the chemical reaction

malonyl-CoA + [acyl-carrier-protein] \rightleftharpoons CoA + malonyl-[acyl-carrier-protein]

Thus, the two substrates of this enzyme are malonyl-CoA and acyl carrier protein, whereas its two products are CoA and malonyl-acyl-carrier-protein.

This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is malonyl-CoA:[acyl-carrier-protein] S-malonyltransferase. Other names in common use include malonyl coenzyme A-acyl carrier protein transacylase, malonyl transacylase, malonyl transferase, malonyl-CoA-acyl carrier protein transacylase, [acyl carrier protein]malonyltransferase, MAT, FabD, malonyl-CoA:acyl carrier protein transacylase, malonyl-CoA:ACP transacylase, MCAT, and malonyl-CoA:AcpM transacylase. This enzyme participates in fatty acid biosynthesis.

Structural studies[edit]

As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes 1NM2, 2CUY, 2G1H, 2G2O, 2G2Y, 2G2Z, 2H1Y, 2PFF, 2QC3, and 2QJ3.

References[edit]

  • Alberts AW, Majerus PW and Vagelos PR (1969). "Acetyl-CoA acyl carrier protein transacylase". Methods Enzymol. Methods in Enzymology 14: 50–53. doi:10.1016/S0076-6879(69)14009-4. ISBN 978-0-12-181871-5. 
  • Prescott DJ, Vagelos PR (1972). "Acyl carrier protein". Adv. Enzymol. Relat. Areas. Mol. Biol. 36: 269–311. PMID 4561013. 
  • 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. 
  • 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. 143 (2): 493–505. doi:10.1016/0003-9861(71)90234-7. PMID 4934182. 
  • 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. doi:10.1074/jbc.M103687200. PMID 11373295. 
  • O'Connell JD 3rd Khosla C, Stroud RM (2003). "Catalysis, specificity, and ACP docking site of Streptomyces coelicolor malonyl-CoA:ACP transacylase". Structure. 11 (2): 147–54. doi:10.1016/S0969-2126(03)00004-2. PMID 12575934. 
  • 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. doi:10.1021/bi012001p. PMID 11814333.