CATH Classification

Domain Context

CATH Clusters

Superfamily 3.40.47.10
Functional Family 3-oxoacyl-[acyl-carrier-protein] synthase I

Enzyme Information

2.3.1.41
Beta-ketoacyl-[acyl-carrier-protein] synthase I.
based on mapping to UniProt P0A953
Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl- [acyl-carrier-protein] + CO(2) + [acyl-carrier-protein].
-!- 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. -!- Can use fatty acyl thioesters of ACP (C(2) to C(16)) as substrates, as well as fatty acyl thioesters of Co-A (C(4) to C(16)). -!- The substrate specificity is very similar to that of EC 2.3.1.179 with the exception that the latter enzyme is far more active with palmitoleoyl-ACP (C(16)-Delta(9)) as substrate, allowing the organism to regulate its fatty-acid composition with changes in temperature.

UniProtKB Entries (1)

P0A953
FABB_ECOLI
Escherichia coli K-12
3-oxoacyl-[acyl-carrier-protein] synthase 1

PDB Structure

PDB 2VBA
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structure-Assisted Discovery of an Aminothiazole Derivative as a Lead Molecule for Inhibition of Bacterial Fatty-Acid Synthesis.
Pappenberger, G., Schulz-Gasch, T., Kusznir, E., Mueller, F., Hennig, M.
Acta Crystallogr.,Sect.D
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