Beta-ketoacyl-acyl-carrier-protein synthase II

From Wikipedia, the free encyclopedia
Jump to navigation Jump to search
Beta-ketoacyl-acyl-carrier-protein synthase II
EC number
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

In enzymology, a beta-ketoacyl-acyl-carrier-protein synthase II (EC is an enzyme that catalyzes the chemical reaction

(Z)-hexadec-11-enoyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] (Z)-3-oxooctadec-13-enoyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein]

Thus, the two substrates of this enzyme are (Z)-hexadec-11-enoyl-[acyl-carrier-protein] and malonyl-[acyl-carrier-protein], whereas its 3 products are (Z)-3-oxooctadec-13-enoyl-[acyl-carrier-protein], CO2, and 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 (Z)-hexadec-11-enoyl-[acyl-carrier-protein]:malonyl-[acyl-carrier-pr otein] C-acyltransferase (decarboxylating). Other names in common use include KASII, KAS II, FabF, 3-oxoacyl-acyl carrier protein synthase I, and beta-ketoacyl-ACP synthase II. This enzyme participates in fatty acid biosynthesis.


  • D'Agnolo G, Rosenfeld IS, Vagelos PR (1975). "Multiple forms of beta-ketoacyl-acyl carrier protein synthetase in Escherichia coli". J. Biol. Chem. 250 (14): 5289&ndash, 94. PMID 237914.
  • Garwin JL, Klages AL, Cronan JE Jr (1980). "Structural, enzymatic, and genetic studies of beta-ketoacyl-acyl carrier protein synthases I and II of Escherichia coli". J. Biol. Chem. 255 (24): 11949&ndash, 56. PMID 7002930.
  • Price AC, Rock CO, White SW (2003). "The 1.3-Angstrom-resolution crystal structure of beta-ketoacyl-acyl carrier protein synthase II from Streptococcus pneumoniae". J. Bacteriol. 185 (14): 4136&ndash, 43. doi:10.1128/JB.185.14.4136-4143.2003. PMC 164876. PMID 12837788.
  • Garwin JL, Klages AL, Cronan JE Jr (1980). "Beta-ketoacyl-acyl carrier protein synthase II of Escherichia coli Evidence for function in the thermal regulation of fatty acid synthesis". J. Biol. Chem. 255 (8): 3263&ndash, 5. PMID 6988423.
  • Magnuson K, Carey MR, Cronan JE Jr (1995). "The putative fabJ gene of Escherichia coli fatty acid synthesis is the fabF gene". J. Bacteriol. 177 (12): 3593&ndash, 5. PMC 177068. PMID 7768872.
  • Neidhardt, F.C. (Ed.), Escherichia coli and Salmonella: Cellular and Molecular Biology, 2nd ed., vol. 1, ASM Press, Washington, DC, 1996, p. 612-636.