spacer CRYSTAL STRUCTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN] SYNTHASE I FROM ESCHERICHIA COLI
UniProt
Accession P0A953search
Name FABB_ECOLI
Keywords Reference proteome, Lipid metabolism, Complete proteome, Cytoplasm, Transferase, 3D-structure, Fatty acid biosynthesis, Lipid biosynthesis, Acyltransferase, Direct protein sequencing, Fatty acid metabolism
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Polymers A B C D
 
Enzyme nomenclature
EC number 2.3.1.41 ExPASy BRENDA search
Polymers A, C, B, D
Name 3-oxoacyl-acyl-carrier-protein synthase, beta-ketoacyl-acyl-carrier-protein synthase I
Comment 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 2.3.1.179, 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].
spacer