CATH Classification

Domain Context

CATH Clusters

Superfamily NAD(P)-binding Rossmann-like Domain
Functional Family Polyketide synthase Pks12

Enzyme Information

2.3.1.41
Beta-ketoacyl-[acyl-carrier-protein] synthase I.
based on mapping to UniProt P96202
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)

P96202
PPSC_MYCTU
Mycobacterium tuberculosis H37Rv
Phthiocerol synthesis polyketide synthase type I PpsC

PDB Structure

PDB 4OKI
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Insights into the catalytic mechanism of the DH domain of the Mycobacterium tuberculosis polyketide synthase PpsC and architecture of the beta-carbon processing domains
Faille, A., Slama, N., Quemard, A., Mourey, L., Pedelacq, J.D.
To be Published