3-oxoadipate CoA-transferase
| 3-oxoadipate CoA-transferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.8.3.6 | ||||||||
| CAS no. | 9026-16-8 | ||||||||
| 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 | ||||||||
| |||||||||
3-oxoadipate CoA-transferase (EC 2.8.3.6) is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme characterised from Pseudomonas fluorescens are β-ketoadipic acid and succinyl-CoA. Its products are 3-oxoadipyl-CoA and succinic acid.[1] This reaction is part of the degradation of several aromatic compounds which proceed via β-ketoadipic acid.[2][3]
This enzyme is a transferases, specifically a CoA-transferases. The systematic name of this enzyme class is succinyl-CoA:3-oxoadipate CoA-transferase. Other names in common use include 3-oxoadipate coenzyme A-transferase, and 3-oxoadipate succinyl-CoA transferase.[4]
References
- ↑ Katagiri, Masayuki; Hayaishi, Osamu (1957). "Enzymatic degradation of β-ketoadipic acid". Journal of Biological Chemistry. 226: 439–448. doi:10.1016/S0021-9258(18)64844-6. PMID 13428776.
- ↑ Kaschabek, Stefan R.; Kuhn, Bernd; MüLler, Dagmar; Schmidt, Eberhard; Reineke, Walter (2002). "Degradation of Aromatics and Chloroaromatics by Pseudomonas sp. Strain B13: Purification and Characterization of 3-Oxoadipate:Succinyl-Coenzyme A (CoA) Transferase and 3-Oxoadipyl-CoA Thiolase". Journal of Bacteriology. 184 (1): 207–215. doi:10.1128/JB.184.1.207-215.2002. PMC 134768. PMID 11741862.
- ↑ GöBel, Markus; Kassel-Cati, Kerstin; Schmidt, Eberhard; Reineke, Walter (2002). "Degradation of Aromatics and Chloroaromatics by Pseudomonas sp. Strain B13: Cloning, Characterization, and Analysis of Sequences Encoding 3-Oxoadipate:Succinyl-Coenzyme A (CoA) Transferase and 3-Oxoadipyl-CoA Thiolase". Journal of Bacteriology. 184 (1): 216–223. doi:10.1128/JB.184.1.216-223.2002. PMC 134769. PMID 11741863.
- ↑ Enzyme 2.8.3.6 at KEGG Pathway Database.
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