CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.10 | Roll |
|
3.10.129 | Thiol Ester Dehydrase; Chain A |
|
3.10.129.110 | Polyketide synthase dehydratase |
Domain Context
CATH Clusters
| Superfamily | Polyketide synthase dehydratase |
| Functional Family | Phthiocerol synthesis polyketide synthase type I PpsC |
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 | 4OOC |
| 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
To be Published
|
