Beta-ketoacyl-ACP synthase

3-oxoacyl-ACP synthase, mitochondrial
Identifiers
Symbol OXSM
Entrez 54995
HUGO 26063
OMIM 610324
RefSeq NM_017897
UniProt Q9NWU1
Other data
EC number 2.3.1.41
Locus Chr. 3 p24.2
Beta-ketoacyl synthase, N-terminal domain

the crystal structure of beta-ketoacyl-[acyl carrier protein] synthase ii from streptococcus pneumoniae, triclinic form
Identifiers
Symbol ketoacyl-synt
Pfam PF00109
Pfam clan CL0046
InterPro IPR014030
PROSITE PDOC00529
SCOP 1kas
SUPERFAMILY 1kas
Beta-ketoacyl synthase, C-terminal domain

arabidopsis thaliana mitochondrial beta-ketoacyl acp synthase hexanoic acid complex
Identifiers
Symbol Ketoacyl-synt_C
Pfam PF02801
Pfam clan CL0046
InterPro IPR014031
PROSITE PDOC00529
SCOP 1kas
SUPERFAMILY 1kas

In molecular biology, Beta-ketoacyl-ACP synthase EC 2.3.1.41, is an enzyme involved in fatty acid synthesis. It results in the formation of acetoacetyl ACP.

It is the enzyme that catalyses the condensation of malonyl-ACP with the growing fatty acid chain.[1] It is found as a component of a number of enzymatic systems, including fatty acid synthetase (FAS), which catalyses the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH; the multi-functional 6-methysalicylic acid synthase (MSAS) from Penicillium patulum,[2] which is involved in the biosynthesis of a polyketide antibiotic; polyketide antibiotic synthase enzyme systems; Emericella nidulans multifunctional protein Wa, which is involved in the biosynthesis of conidial green pigment; Rhizobium nodulation protein nodE, which probably acts as a beta-ketoacyl synthase in the synthesis of the nodulation Nod factor fatty acyl chain; and yeast mitochondrial protein CEM1. The condensation reaction is a two-step process: first the acyl component of an activated acyl primer is transferred to a cysteine residue of the enzyme and is then condensed with an activated malonyl donor with the concomitant release of carbon dioxide.

Beta-ketoacyl synthase contains two protein domains. The active site is located between the N- and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine. Residues from both domains contribute to substrate binding and catalysis[3]

See also

External links

References

  1. Kauppinen S, Siggaard-Andersen M, von Wettstein-Knowles P (1988). "beta-Ketoacyl-ACP synthase I of Escherichia coli: nucleotide sequence of the fabB gene and identification of the cerulenin binding residue". Carlsberg Res. Commun. 53 (6): 357–70. doi:10.1007/bf02983311. PMID 3076376.
  2. Beck J, Ripka S, Siegner A, Schiltz E, Schweizer E (September 1990). "The multifunctional 6-methylsalicylic acid synthase gene of Penicillium patulum. Its gene structure relative to that of other polyketide synthases". Eur. J. Biochem. 192 (2): 487–98. doi:10.1111/j.1432-1033.1990.tb19252.x. PMID 2209605.
  3. Huang W, Jia J, Edwards P, Dehesh K, Schneider G, Lindqvist Y (1998). "Crystal structure of beta-ketoacyl-acyl carrier protein synthase II from E.coli reveals the molecular architecture of condensing enzymes.". EMBO J 17 (5): 1183–91. doi:10.1093/emboj/17.5.1183. PMC 1170466. PMID 9482715.

This article incorporates text from the public domain Pfam and InterPro IPR014030

This article incorporates text from the public domain Pfam and InterPro IPR014031

This article is issued from Wikipedia - version of the Saturday, April 04, 2015. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.