show all | hide all No of entries

Information on EC - very-long-chain 3-oxoacyl-CoA synthase

for references in articles please use BRENDA:EC2.3.1.199
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
This is the first component of the elongase, a microsomal protein complex responsible for extending palmitoyl-CoA and stearoyl-CoA (and modified forms thereof) to very-long-chain acyl CoAs. Multiple forms exist with differing preferences for the substrate, and thus the specific form expressed determines the local composition of very-long-chain fatty acids [6,7]. For example, the FAE1 form from the plant Arabidopsis thaliana accepts only 16 and 18 carbon substrates, with oleoyl-CoA (18:1) being the preferred substrate , while CER6 from the same plant prefers substrates with chain length of C22 to C32 [4,8]. cf. EC, very-long-chain 3-oxoacyl-CoA reductase, EC, very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] dehydratase, and EC, very-long-chain enoyl-CoA reductase
Specify your search results
Select one or more organisms in this record: ?
Word Map
The enzyme appears in viruses and cellular organisms
fatty acid elongase, elovl1, elovl7, 3-ketoacyl-coa synthase, acyl-coa elongase, fatty acid elongase 1, beta-ketoacyl-coa synthase, fa elongase, fae1 kcs, fatty acid elongation1, more
a very-long-chain acyl-CoA + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
show the reaction diagram
Select items on the left to see more content.