Diaminohydroxyphosphoribosylaminopyrimidine deaminase
From Wikipedia, the free encyclopedia
In enzymology, a diaminohydroxyphosphoribosylaminopyrimidine deaminase (EC 3.5.4.26) is an enzyme that catalyzes the chemical reaction
- 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + H2O
5-amino-6-(5-phosphoribosylamino)uracil + NH3
Thus, the two substrates of this enzyme are 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine and H2O, whereas its two products are 5-amino-6-(5-phosphoribosylamino)uracil and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine 2-aminohydrolase. This enzyme participates in riboflavin metabolism.
Contents |
[edit] Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 2B3Z, 2D5N, 2G6V, 2HXV, 2O7P, and 2OBC.
[edit] References
- IUBMB entry for 3.5.4.26
- BRENDA references for 3.5.4.26 (Recommended.)
- PubMed references for 3.5.4.26
- PubMed Central references for 3.5.4.26
- Google Scholar references for 3.5.4.26
- Burrows RB, Brown GM (1978). "Presence of Escherichia coli of a deaminase and a reductase involved in biosynthesis of riboflavin". J. Bacteriol. 136: 657–67. PMID 30756.
[edit] External links
-
- The CAS registry number for this enzyme class is 68994-19-4.
[edit] Gene Ontology (GO) codes
 |
This hydrolase article is a stub. You can help Wikipedia by expanding it. |
