Any feedback?
Please rate this page

BRENDA support

show all | hide all No of entries

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

for references in articles please use BRENDA:EC2.3.1.41
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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].
Specify your search results
Select one or more organisms in this record: ?
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
condensing enzyme, beta-ketoacyl synthase, kas i, beta-ketoacyl-acp synthase, beta-ketoacyl synthetase, 3-ketoacyl-acyl carrier protein synthase, 3-ketoacyl-acp synthase, beta-ketoacyl-acp synthase i, beta-ketoacyl-acyl carrier protein synthase i, oskasi, more
an acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = a 3-oxoacyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
show the reaction diagram