Ureidoglycolate dehydrogenase
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| 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 | ||||||||
| |||||||||
In enzymology, an ureidoglycolate dehydrogenase (EC 1.1.1.154) is an enzyme that catalyzes the chemical reaction
- (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
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1WTJ and 1XRH.
References
- 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.
