ENZYME entry: EC 2.8.3.8
Accepted Name |
acetate CoA-transferase.
|
Reaction catalysed |
acetate + an acyl-CoA <=> a carboxylate + acetyl-CoA |
Comment(s) |
- The enzyme belongs to family I of CoA-transferases, which operate
with a ping-pong kinetic mechanism.
- The reaction takes place in two half-reactions and involves the
formation of a CoA thioester intermediate with a glutamate residue.
- Unlike EC 2.8.3.9, this enzyme exhibits maximal activity using
acetate as the CoA acceptor.
- Substrate range depends on the specific enzyme.
- Typical substrates include butanoyl-CoA and pentanoyl-CoA.
|
Cross-references |
BRENDA | 2.8.3.8 |
EC2PDB | 2.8.3.8 |
ExplorEnz | 2.8.3.8 |
PRIAM enzyme-specific profiles | 2.8.3.8 |
KEGG Ligand Database for Enzyme Nomenclature | 2.8.3.8 |
IUBMB Enzyme Nomenclature | 2.8.3.8 |
IntEnz | 2.8.3.8 |
MEDLINE | Find literature relating to 2.8.3.8 |
MetaCyc | 2.8.3.8 |
Rhea expert-curated reactions | 2.8.3.8 |
UniProtKB/Swiss-Prot |
|
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ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 2.8.3.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.8.-.-
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