Information on EC - beta-ketoacyl-[acyl-carrier-protein] synthase I

for references in articles please use BRENDA:EC2.3.1.41
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IUBMB Comments
This enzyme is responsible for the chain-elongation step of dissociated (type II) fatty-acid biosynthesis, i.e. the addition of two C atoms to the fatty-acid chain. Escherichia coli mutants that lack this enzyme are deficient in unsaturated fatty acids. The enzyme can use fatty acyl thioesters of ACP (C2 to C16) as substrates, as well as fatty acyl thioesters of Co-A (C4 to C16) . The substrate specificity is very similar to that of EC, beta-ketoacyl-ACP synthase II, with the exception that the latter enzyme is far more active with palmitoleoyl-ACP (C16Delta9) as substrate, allowing the organism to regulate its fatty-acid composition with changes in temperature [4,5].
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
3-ketoacyl-ACP synthase, 3-ketoacyl-acyl carrier protein synthase, 3-ketoacyl-acyl-carrier protein synthase I, 3-oxoacyl synthase, 3-oxoacyl-[acyl-carrier-protein] synthase, acyl-malonyl(acyl-carrier-protein)-condensing enzyme, B-ketoacyl-ACP synthase I, beta-ketoacyl ACP synthase I, beta-ketoacyl acyl carrier protein synthase, beta-ketoacyl acyl carrier protein synthase I, more
an acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = a 3-oxoacyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
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