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 |
Enzyme Information
| 2.3.1.179 |
Beta-ketoacyl-[acyl-carrier-protein] synthase II.
based on mapping to UniProt P0AAI5
(Z)-hexadec-11-enoyl-[acyl-carrier-protein] + malonyl-[acyl-carrier- protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-carrier-protein] + CO(2) + [acyl-carrier-protein].
-!- Involved in the dissociated (or type II) fatty acid biosynthesis system that occurs in plants and bacteria. -!- While the substrate specificity of this enzyme is very similar to that of EC 2.3.1.41, it differs in that palmitoleoyl-ACP is not a good substrate of EC 2.3.1.41 but is an excellent substrate of this enzyme. -!- The fatty-acid composition of Escherichia coli changes as a function of growth temperature, with the proportion of unsaturated fatty acids increasing with lower growth temperature. -!- Controls the temperature-dependent regulation of fatty-acid composition, with mutants lacking this acivity being deficient in the elongation of palmitoleate to cis-vaccenate at low temperatures.
|
UniProtKB Entries (1)
| P0AAI5 |
FABF_ECOLI
Escherichia coli K-12
3-oxoacyl-[acyl-carrier-protein] synthase 2
|
PDB Structure
| PDB | 1B3N |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structure of the complex between the antibiotic cerulenin and its target, beta-ketoacyl-acyl carrier protein synthase.
J.Biol.Chem.
|
