Beta-ketoacyl-ACP synthase

Beta-ketoacyl-ACP synthase

3-oxoacyl-ACP synthase, mitochondrial
Identifiers
Symbol OXSM
Entrez HUGO OMIM RefSeq UniProt EC number Locus 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 Pfam clan InterPro PROSITE PDOC00529
SCOP SUPERFAMILY 1kas
Beta-ketoacyl synthase, C-terminal domain
arabidopsis thaliana mitochondrial beta-ketoacyl acp synthase hexanoic acid complex
Identifiers
Symbol Ketoacyl-synt_C
Pfam Pfam clan InterPro PROSITE PDOC00529
SCOP SUPERFAMILY 1kas

In molecular biology, Beta-ketoacyl-ACP synthase 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

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References

This article incorporates text from the IPR014030

This article incorporates text from the IPR014031