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-ketoacyl-CoA thiolase |
Enzyme Information
| 2.3.1.9 |
Acetyl-CoA C-acetyltransferase.
based on mapping to UniProt Q0KBP1
2 acetyl-CoA = CoA + acetoacetyl-CoA.
-!- The enzyme, found in both eukaryotes and prokaryotes, catalyzes the Claisen condensation of an acetyl-CoA and an acyl-CoA (often another acetyl-CoA), leading to the formation of an acyl-CoA that is longer by two carbon atoms. -!- The reaction starts with the acylation of a nucleophilic cysteine at the active site, usually by acetyl-CoA but potentially by a different acyl-CoA, with concomitant release of CoA. -!- In the second step the acyl group is transferred to an acetyl-CoA molecule. -!- Cf. EC 2.3.1.16.
|
| 2.3.1.16 |
Acetyl-CoA C-acyltransferase.
based on mapping to UniProt Q0KBP1
Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.
-!- The enzyme, found in both eukaryotes and in prokaryotes, is involved in degradation pathways such as fatty acid beta-oxidation. -!- The enzyme acts on 3-oxoacyl-CoAs to produce acetyl-CoA and an acyl- CoA shortened by two carbon atoms. -!- The reaction starts with the acylation of a nucleophilic cysteine at the active site by a 3-oxoacyl-CoA, with the concomitant release of acetyl-CoA. -!- In the second step the acyl group is transferred to CoA. -!- Most enzymes have a broad substrate range for the 3-oxoacyl-CoA. -!- cf. EC 2.3.1.9.
|
UniProtKB Entries (1)
| Q0KBP1 |
BKTB_CUPNH
Cupriavidus necator H16
Beta-ketothiolase BktB
|
PDB Structure
| PDB | 4W61 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Coenzyme A-free activity, crystal structure, and rational engineering of a promiscuous beta-ketoacyl thiolase fromRalstonia eutropha.
J. Mol. Catal., B Enzym.
|
