In enzymology, an ureidoglycolate dehydrogenase (EC 1.1.1.154) is an enzyme that catalyzes the chemical reaction
| ureidoglycolate dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.154 | ||||||||
| CAS no. | 62213-62-1 | ||||||||
| 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 | ||||||||
| |||||||||
- (S)-ureidoglycolate + NAD(P)+ oxalurate + NAD(P)H + H+
The 3 substrates of this enzyme are (S)-ureidoglycolate, NAD+, and NADP+, whereas its 4 products are oxalurate, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-ureidoglycolate:NAD(P)+ oxidoreductase. This enzyme participates in purine metabolism.
Structural studies edit
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1WTJ and 1XRH.
References edit
- van der Drift C, van Helvoort PE, Vogels GD (1971). "S-ureidoglycolate dehydrogenase: purification and properties". Arch. Biochem. Biophys. 145 (2): 465–9. doi:10.1016/S0003-9861(71)80006-1. PMID 4399430.
