D
IPR014030

Beta-ketoacyl synthase-like, N-terminal

InterPro entry
Short nameKetoacyl_synth_N
Overlapping
homologous
superfamilies
 
Thiolase-like (IPR016039)

Description

Beta-ketoacyl-ACP synthase
2.3.1.41
(KAS)
[1]
is the enzyme that catalyses the condensation of malonyl-ACP with the growing fatty acid chain. 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.

This entry represents the N-terminal domain of beta-ketoacyl-ACP synthases and polyketide synthases.

References

1.beta-Ketoacyl-ACP synthase I of Escherichia coli: nucleotide sequence of the fabB gene and identification of the cerulenin binding residue. Kauppinen S, Siggaard-Andersen M, von Wettstein-Knowles P. Carlsberg Res. Commun. 53, 357-70, (1988). PMID: 3076376

2.The multifunctional 6-methylsalicylic acid synthase gene of Penicillium patulum. Its gene structure relative to that of other polyketide synthases. Beck J, Ripka S, Siegner A, Schiltz E, Schweizer E. Eur. J. Biochem. 192, 487-98, (1990). View articlePMID: 2209605

Cross References

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