Malonate CoA-transferase
| malonate CoA-transferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.8.3.3 | ||||||||
| CAS no. | 9026-18-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a malonate CoA-transferase (EC 2.8.3.3) is an enzyme that catalyzes the chemical reaction
- acetyl-CoA + malonate acetate + malonyl-CoA
Thus, the two substrates of this enzyme are acetyl-CoA and malonate, whereas its two products are acetate and malonyl-CoA.
This enzyme belongs to the family of transferases, specifically the CoA-transferases. The systematic name of this enzyme class is acetyl-CoA:malonate CoA-transferase. This enzyme is also called malonate coenzyme A-transferase. This enzyme participates in beta-alanine metabolism and propanoate metabolism.
References
[edit]- Hayaishi O (July 1955). "Enzymatic decarboxylation of malonic acid". The Journal of Biological Chemistry. 215 (1): 125–36. PMID 14392148.
- Takamura Y, Kitayama Y (1981). "Purification and some properties of malonate decarboxylase from Pseudomonas ovalis: an oligomeric enzyme with bifunctional properties". Biochem. Int. 3: 483–491.
