CATH Classification

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 4NZS
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Crystal structure and biochemical characterization of beta-keto thiolase B from polyhydroxyalkanoate-producing bacterium Ralstonia eutropha H16
Kim, E.J., Son, H.F., Kim, S., Ahn, J.W., Kim, K.J.
Biochem.Biophys.Res.Commun.