From Wikipedia, the free encyclopedia
Beta-ketoacyl-acyl-carrier-protein synthase II
Identifiers
EC no. 2.3.1.179
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

In enzymology, a beta-ketoacyl-acyl-carrier-protein synthase II ( EC 2.3.1.179) 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.

References

  • 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): 5289–94. 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): 11949–56. 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): 4136–43. 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): 3263–5. 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): 3593–5. doi: 10.1128/jb.177.12.3593-3595.1995. 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.


From Wikipedia, the free encyclopedia
Beta-ketoacyl-acyl-carrier-protein synthase II
Identifiers
EC no. 2.3.1.179
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

In enzymology, a beta-ketoacyl-acyl-carrier-protein synthase II ( EC 2.3.1.179) 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.

References

  • 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): 5289–94. 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): 11949–56. 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): 4136–43. 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): 3263–5. 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): 3593–5. doi: 10.1128/jb.177.12.3593-3595.1995. 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.



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