CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.47 | Peroxisomal Thiolase; Chain A, domain 1 |
|
3.40.47.10 | Thiolase/Chalcone synthase |
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 | 1F91 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structures of beta-ketoacyl-acyl carrier protein synthase I complexed with fatty acids elucidate its catalytic machinery.
Structure
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