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 2AQ7
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Structure-Activity Relationships at the 5-Position of Thiolactomycin: An Intact (5R)-Isoprene Unit Is Required for Activity against the Condensing Enzymes from Mycobacterium tuberculosis and Escherichia coli
Kim, P., Zhang, Y.M., Shenoy, G., Nguyen, Q.A., Boshoff, H.I., Manjunatha, U.H., Goodwin, M.B., Lonsdale, J., Price, A.C., Miller, D.J., Duncan, K., White, S.W., Rock, C.O., Barry III, C.E., Dowd, C.S.
J.Med.Chem.