Malonate CoA-transferase
| Malonate CoA-transferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.8.3.3 | ||||||||
| CAS no. | 9026-18-0 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Malonate CoA-transferase (EC 2.8.3.3) is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme characterised from Pseudomonas ovalis are malonic acid and acetyl-CoA. Its products are malonyl-CoA and acetic acid. The reaction is the first step in the decarboxylation of malonic acid.[1][2][3] In Pseudomonas putida, this decarboxylation involves a multi-enzyme complex.[4]
This enzyme is a transferase, specifically a CoA-transferase. The systematic name of this enzyme class is acetyl-CoA:malonate CoA-transferase. This enzyme is also called malonate coenzyme A-transferase.[5]
References
- ↑ Hayaishi, O (July 1955). "Enzymatic decarboxylation of malonic acid". The Journal of Biological Chemistry. 215 (1): 125–36. doi:10.1016/S0021-9258(18)66022-3. 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.
- ↑ Janssen, Peter H.; Harfoot, C. G. (1992). "Anaerobic malonate decarboxylation by Citrobacter diversus". Archives of Microbiology. 157 (5): 471–474. doi:10.1007/BF00249107. PMID 1510573.
- ↑ Hu, Zhiyuan; Cha, Seung Hun; Chohnan, Shigeru; Lane, M. Daniel (2003). "Hypothalamic malonyl-CoA as a mediator of feeding behavior". Proceedings of the National Academy of Sciences. 100 (22): 12624–12629. doi:10.1073/pnas.1834402100. PMC 240668. PMID 14532332.
- ↑ Enzyme 2.8.3.3 at KEGG Pathway Database.
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