Succinyl-CoA:(R)-benzylsuccinate CoA-transferase
| Succinyl-CoA:(R)-benzylsuccinate CoA-transferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.8.3.15 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
In enzymology, a succinyl-CoA:(R)-benzylsuccinate CoA-transferase (EC 2.8.3.15) is an enzyme that catalyzes the chemical reaction
- succinyl-CoA + (R)-2-benzylsuccinate succinate + (R)-2-benzylsuccinyl-CoA
Thus, the two substrates of this enzyme are succinyl-CoA and (R)-2-benzylsuccinate, whereas its two products are succinate and (R)-2-benzylsuccinyl-CoA.
This enzyme belongs to the family of transferases, specifically the CoA-transferases. The systematic name of this enzyme class is succinyl-CoA:(R)-2-benzylsuccinate CoA-transferase. This enzyme is also called benzylsuccinate CoA-transferase. This enzyme participates in benzoate degradation via coa ligation.
References
[edit]- Leutwein C, Heider J (2001). "Succinyl-CoA:(R)-benzylsuccinate CoA-transferase: an enzyme of the anaerobic toluene catabolic pathway in denitrifying bacteria". J. Bacteriol. 183 (14): 4288–95. doi:10.1128/JB.183.14.4288-4295.2001. PMC 95319. PMID 11418570.
- Leutwein C, Heider J. "Anaerobic toluene-catabolic pathway in denitrifying Thauera aromatica: activation and beta-oxidation of the first intermediate, (R)-(+)-benzylsuccinate". Microbiology. 145: 3265–71. doi:10.1099/00221287-145-11-3265. PMID 10589736.
- Leuthner B, Heider J (2000). "Anaerobic toluene catabolism of Thauera aromatica: the bbs operon codes for enzymes of beta oxidation of the intermediate benzylsuccinate". J. Bacteriol. 182 (2): 272–7. doi:10.1128/JB.182.2.272-277.2000. PMC 94273. PMID 10629170.
- Heider J (2001). "A new family of CoA-transferases". FEBS Lett. 509 (3): 345–9. doi:10.1016/S0014-5793(01)03178-7. PMID 11749953.
