D
IPR014031

Beta-ketoacyl synthase, C-terminal

InterPro entry
Short nameKetoacyl_synth_C
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 C-terminal domain of beta-ketoacyl-ACP synthases. The active site is contained in a cleft between N-and C-terminal domains, with residues from both domains contributing to substrate binding and catalysis
[3]
. It is also found in polyketide synthases such as Non-reducing polyketide synthase nscA, reducing polyketide synthase FUB1, Phenolphthiocerol synthesis polyketide synthase type I Pks15/1 and related enzymes
[5, 4, 6]
.

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

3.The crystal structure of beta-ketoacyl-acyl carrier protein synthase II from Synechocystis sp. at 1.54 A resolution and its relationship to other condensing enzymes. Moche M, Dehesh K, Edwards P, Lindqvist Y. J. Mol. Biol. 305, 491-503, (2001). View articlePMID: 11152607

4.Identification of a 12-gene Fusaric Acid Biosynthetic Gene Cluster in Fusarium Species Through Comparative and Functional Genomics. Brown DW, Lee SH, Kim LH, Ryu JG, Lee S, Seo Y, Kim YH, Busman M, Yun SH, Proctor RH, Lee T. Mol. Plant Microbe Interact. 28, 319-32, (2015). View articlePMID: 25372119

5.Genome mining of a prenylated and immunosuppressive polyketide from pathogenic fungi. Chooi YH, Fang J, Liu H, Filler SG, Wang P, Tang Y. Org Lett 15, 780-3, (2013). View articlePMID: 23368997

6.Cooperation between a coenzyme A-independent stand-alone initiation module and an iterative type I polyketide synthase during synthesis of mycobacterial phenolic glycolipids. He W, Soll CE, Chavadi SS, Zhang G, Warren JD, Quadri LE. J Am Chem Soc 131, 16744-50, (2009). View articlePMID: 19799378

Cross References

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