Phenylglyoxylate dehydrogenase (acylating)
| phenylglyoxylate dehydrogenase (acylating) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.2.1.58 | ||||||||
| CAS no. | 205510-78-7 | ||||||||
| 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, phenylglyoxylate dehydrogenase (acylating; EC 1.2.1.58) is an enzyme that catalyzes the chemical reaction
The three substrates of this enzyme are phenylglyoxylic aicd, coenzyme A, and oxidised nicotinamide adenine dinucleotide (NAD+). Its products are benzoyl-CoA, carbon dioxide, reduced NADH, and a proton.[1][2]
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is phenylglyoxylate:NAD+ oxidoreductase. It has 3 cofactors: FAD, Thiamin diphosphate, and Iron-sulfur.
References
- ^ Enzyme 1.2.1.58 at KEGG Pathway Database.
- ^ Hirsch W, Schagger H, Fuchs G (1998). "Phenylglyoxylate:NAD+ oxidoreductase (CoA benzoylating), a new enzyme of anaerobic phenylalanine metabolism in the denitrifying bacterium Azoarcus evansii". Eur. J. Biochem. 251 (3): 907–15. doi:10.1046/j.1432-1327.1998.2510907.x. PMID 9490067.