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3-oxoacyl-ACP synthase, mitochondrial

beta-ketoacyl synthase, KASI, K S
This gene encodes a beta-ketoacyl synthetase. The encoded enzyme is required for elongation of fatty acid chains in the mitochondria. Alternatively spliced transcript variants have been described.[provided by RefSeq, Feb 2009] (from NCBI)
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Top mentioned proteins: ACID, CAN, STEP, HAD, OUT
Papers on beta-ketoacyl synthase
OsKASI, a β-ketoacyl-[acyl carrier protein] synthase I, is involved in root development in rice (Oryza sativa L.).
Zhu et al., Ningbo, China. In Planta, Jul 2015
Map-based cloning revealed that the mutation occurred in a putative 3-oxoacyl-synthase, an ortholog of β-ketoacyl-[acyl carrier protein] synthase I (KASI) in Arabidopsis, thus designated as OsKASI.
Fatty acid biosynthesis in Pseudomonas aeruginosa is initiated by the FabY class of β-ketoacyl acyl carrier protein synthases.
Meredith et al., Cambridge, United States. In J Bacteriol, 2012
The prototypical type II fatty acid synthesis (FAS) pathway in bacteria utilizes two distinct classes of β-ketoacyl synthase (KAS) domains to assemble long-chain fatty acids, the KASIII domain for initiation and the KASI/II domain for elongation.
Pseudomonas aeruginosa directly shunts β-oxidation degradation intermediates into de novo fatty acid biosynthesis.
Meredith et al., Cambridge, United States. In J Bacteriol, 2012
We identified the fatty acid synthesis (FAS) initiation enzyme in Pseudomonas aeruginosa as FabY, a β-ketoacyl synthase KASI/II domain-containing enzyme that condenses acetyl coenzyme A (acetyl-CoA) with malonyl-acyl carrier protein (ACP) to make the FAS primer β-acetoacetyl-ACP in the accompanying article (Y.
Substrate recognition by β-ketoacyl-ACP synthases.
Tonge et al., Stony Brook, United States. In Biochemistry, 2012
In the priming KASIII enzymes the donor substrate is an acyl-CoA while in the elongating KASI and KASII enzymes the donor is an acyl-ACP.
Arabidopsis β-ketoacyl-[acyl carrier protein] synthase i is crucial for fatty acid synthesis and plays a role in chloroplast division and embryo development.
Xue et al., Shanghai, China. In Plant Cell, 2010
β-Ketoacyl-[acyl carrier protein] synthase I (KASI) catalyzes the elongation of de novo fatty acid (FA) synthesis.
The methoxymalonyl-acyl carrier protein biosynthesis locus and the nearby gene with the beta-ketoacyl synthase domain are involved in the biosynthesis of galbonolides in Streptomyces galbus, but these loci are separate from the modular polyketide synthase gene cluster.
Kwon et al., South Korea. In Fems Microbiol Lett, 2010
A multimodular polyketide synthase (PKS) was predicted to catalyze their biosynthesis, and a methoxymalonyl-acyl carrier protein (methoxymalonyl-ACP) was expected to be involved in the biosynthesis of galbonolide A. Cloning of a methoxymalonyl-ACP biosynthesis locus (galGHIJK) and the flanking regions has revealed that the locus is colocalized with beta-ketoacyl synthase (KAS)-related genes (orf3, 4, and 5), but separated from any multimodular PKS gene cluster in S. galbus.
Detection of microcystin-producing cyanobacteria in Missisquoi Bay, Quebec, Canada, using quantitative PCR.
Greer et al., Montréal, Canada. In Appl Environ Microbiol, 2010
Primers were designed for the beta-ketoacyl synthase (mcyD(KS)) and the first dehydratase domain (mcyD(DH)) of the mcyD gene, involved in microcystin synthesis.
Inhibitory effects of thioethers on fatty acid synthase and 3T3-L1 cells.
Tian et al., Beijing, China. In J Enzyme Inhib Med Chem, 2010
Inhibition kinetics, substrate protection analysis, and stoichiometric assay revealed that DATS interacted with both essential sulfhydryl groups on the acyl-carrier protein and beta-ketoacyl synthase domain of FAS to inactivate the enzyme.
ACTTS3 encoding a polyketide synthase is essential for the biosynthesis of ACT-toxin and pathogenicity in the tangerine pathotype of Alternaria alternata.
Akimitsu et al., Japan. In Mol Plant Microbe Interact, 2010
The 7,374-bp ORF encodes a polyketide synthase with putative beta-ketoacyl synthase, acyltransferase, methyltransferase, beta-ketoacyl reductase, and phosphopantetheine attachment site domains.
Structure of the human fatty acid synthase KS-MAT didomain as a framework for inhibitor design.
Rudolph et al., Basel, Switzerland. In J Mol Biol, 2010
We describe the high-resolution crystal structure of a large part of human FAS that encompasses the tandem domain of beta-ketoacyl synthase (KS) connected by a linker domain to the malonyltransferase (MAT) domain.
Slow onset inhibition of bacterial beta-ketoacyl-acyl carrier protein synthases by thiolactomycin.
Tonge et al., Stony Brook, United States. In J Biol Chem, 2010
Using enzyme kinetics and direct binding studies, TLM has been shown to bind preferentially to the acyl-enzyme intermediates of the KASI and KASII enzymes from Mycobacterium tuberculosis and Escherichia coli.
Cloning, expression, and characterization of the human mitochondrial beta-ketoacyl synthase. Complementation of the yeast CEM1 knock-out strain.
Smith et al., Oakland, United States. In J Biol Chem, 2005
characterization of the human mitochondrial beta-ketoacyl synthase
Structure and function of animal fatty acid synthase.
Wakil et al., Houston, United States. In Lipids, 2004
The FAS monomer (approximately 270 kDa) contains six catalytic activities and from the N-terminus the order is beta-ketoacyl synthase (KS), acetyl/malonyl transacylase (AT/MT), beta-hydroxyacyl dehydratase (DH), enoyl reductase (ER), beta-ketoacyl reductase (KR), acyl carrier protein (ACP), and thioesterase (TE).
Structural and functional organization of the animal fatty acid synthase.
Joshi et al., Oakland, United States. In Prog Lipid Res, 2003
Each subunit contains three N-terminal domains, the beta-ketoacyl synthase, malonyl/acetyl transferase and dehydrase separated by a structural core from four C-terminal domains, the enoyl reductase, beta-ketoacyl reductase, acyl carrier protein and thiosterase.
C-O bond formation by polyketide synthases.
Shen et al., Madison, United States. In Science, 2002
Polyketide synthases (PKSs) assemble the polyketide carbon backbone by sequential decarboxylative condensation of acyl coenzyme A (CoA) precursors, and the C-C bond-forming step in this process is catalyzed by the beta-ketoacyl synthase (KS) domain or subunit.
Mapping the genome of rapeseed (Brassica napus L.). I. Construction of an RFLP linkage map and localization of QTLs for seed glucosinolate content.
Röbbelen et al., Göttingen, Germany. In Theor Appl Genet, 1995
Using cDNA probes for the genes of acyl-carrier-protein (ACP) and β-ketoacyl-ACP-synthase I (KASI) we were able to map three and two loci, respectively, for these genes.
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