Beta-ketoacyl-ACP synthase I

This article is about the specific variant of the enzyme type I. For the function and the enzyme in general, see Beta-ketoacyl-ACP synthase.

3-oxoacyl-[acyl-carrier-protein] synthase I
Identifiers
EC no.	2.3.1.41
CAS no.	9077-10-5
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 / QuickGO
Search PMC articles PubMed articles NCBI proteins

In enzymology, a beta-ketoacyl-acyl-carrier-protein synthase I (EC 2.3.1.41) is an enzyme that catalyzes the chemical reaction

an acyl-acyl-carrier-protein + malonyl-acyl-carrier-protein $\rightleftharpoons$ a 3-oxoacyl-acyl-carrier-protein + CO₂ + acyl-carrier-protein

Thus, the two substrates of this enzyme are acyl-acyl-carrier-protein and malonyl-acyl-carrier-protein, whereas its 3 products are 3-oxoacyl-acyl-carrier-protein, CO₂, and acyl carrier protein. This enzyme participates in fatty acid biosynthesis. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups.

Nomenclature

The systematic name of this enzyme class is acyl-[acyl-carrier-protein]:malonyl-[acyl-carrier-protein] C-acyltransferase (decarboxylating).

Other names in common use include:

• beta-ketoacyl-ACP synthase I,
• beta-ketoacyl synthetase,
• beta-ketoacyl-ACP synthetase,
• beta-ketoacyl-acyl carrier protein synthetase,
• beta-ketoacyl-[acyl carrier protein] synthase,
• beta-ketoacylsynthase,
• condensing enzyme (CE),
• 3-ketoacyl-acyl carrier protein synthase,
• fatty acid condensing enzyme,
• acyl-malonyl(acyl-carrier-protein)-condensing enzyme,
• acyl-malonyl acyl carrier protein-condensing enzyme,
• beta-ketoacyl acyl carrier protein synthase,
• 3-oxoacyl-[acyl-carrier-protein] synthase,
• 3-oxoacyl:ACP synthase I,
• KASI,
• KAS I,
• FabF1, and
• FabB.

References

• Alberts AW, Majerus PW, Vagelos PR (1969). "Acetyl-CoA acyl carrier protein transacylase". Lipids. Methods in Enzymology. Vol. 14. pp. 50–53. doi:10.1016/S0076-6879(69)14009-4. ISBN 978-0-12-181871-5.
• Prescott DJ, Vagelos PR (1972). "Acyl carrier protein". Advances in Enzymology and Related Areas of Molecular Biology. Vol. 36. pp. 269–311. doi:10.1002/9780470122815.ch8. ISBN 9780470122815. PMID 4561013.
• Toomey RE, Wakil SJ (Mar 1966). "Studies on the mechanism of fatty acid synthesis. XVI. Preparation and general properties of acyl-malonyl acyl carrier protein-condensing enzyme from Escherichia coli". The Journal of Biological Chemistry. 241 (5): 1159–65. doi:10.1016/S0021-9258(18)96816-X. PMID 5327099.
• D'Agnolo G, Rosenfeld IS, Vagelos PR (Jul 1975). "Multiple forms of beta-ketoacyl-acyl carrier protein synthetase in Escherichia coli". The Journal of Biological Chemistry. 250 (14): 5289–94. doi:10.1016/S0021-9258(19)41179-4. PMID 237914.
• Garwin JL, Klages AL, Cronan JE (Dec 1980). "Structural, enzymatic, and genetic studies of beta-ketoacyl-acyl carrier protein synthases I and II of Escherichia coli". The Journal of Biological Chemistry. 255 (24): 11949–56. doi:10.1016/S0021-9258(19)70226-9. PMID 7002930.
• Wang H, Cronan JE (Aug 2004). "Functional replacement of the FabA and FabB proteins of Escherichia coli fatty acid synthesis by Enterococcus faecalis FabZ and FabF homologues". The Journal of Biological Chemistry. 279 (33): 34489–95. doi:10.1074/jbc.M403874200. PMID 15194690.
• Neidhardt, F.C. (Ed.), Escherichia coli and Salmonella: Cellular and Molecular Biology, 2nd ed., vol. 1, ASM Press, Washington, DC, 1996, p. 612-636.