Xanthine dehydrogenase

From Wikipedia, the free encyclopedia

In enzymology, a xanthine dehydrogenase (EC 1.17.1.4) is an enzyme that catalyzes the chemical reaction

xanthine + NAD⁺ + H₂O $\rightleftharpoons$ urate + NADH + H⁺

The 3 substrates of this enzyme are xanthine, NAD⁺, and H₂O, whereas its 3 products are urate, NADH, and H⁺.

This enzyme belongs to the family of oxidoreductases, specifically those acting on CH or CH2 group with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is xanthine:NAD+ oxidoreductase. Other names in common use include NAD+-xanthine dehydrogenase, xanthine-NAD+ oxidoreductase, xanthine/NAD+ oxidoreductase, and xanthine oxidoreductase. This enzyme participates in purine metabolism.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2E1Q and 2E3T.

[edit] References

IUBMB entry for 1.17.1.4
BRENDA references for 1.17.1.4 (Recommended.)
PubMed references for 1.17.1.4
PubMed Central references for 1.17.1.4
Google Scholar references for 1.17.1.4
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PARZEN SD, FOX AS (1964). "PURIFICATION OF XANTHINE DEHYDROGENASE FROM DROSOPHILA MELANOGASTER". Biochim. Biophys. Acta. 92: 465–71. PMID 14264879.
Rajagopalan KV, Handler P (1967). "Purification and properties of chicken liver xanthine dehydrogenase". J. Biol. Chem. 242: 4097–107. PMID 4294045.
Smith ST, Rajagopalan KV, Handler P (1967). "Purification and properties of xanthine dehydroganase from Micrococcus lactilyticus". J. Biol. Chem. 242: 4108–17. PMID 6061702.
Parschat K, Canne C, Huttermann J, Kappl R, Fetzner S (2001). "Xanthine dehydrogenase from Pseudomonas putida 86: specificity, oxidation-reduction potentials of its redox-active centers, and first EPR characterization". Biochim. Biophys. Acta. 1544: 151–65. PMID 11341925.
N, Nishino T (1993). "Cloning of the cDNA encoding human xanthine dehydrogenase (oxidase): structural analysis of the protein and chromosomal location of the gene". Gene. 133: 279–84. doi:10.1016/0378-1119(93)90652-J. PMID 8224915.
Enroth C, Eger BT, Okamoto K, Nishino T, Nishino T, Pai EF (2000). "Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion". Proc. Natl. Acad. Sci. U. S. A. 97: 10723–8. doi:10.1073/pnas.97.20.10723. PMID 11005854.
C (Camb). "Crystal structures of the active and alloxanthine-inhibited forms of xanthine dehydrogenase from Rhodobacter capsulatus". S Structure.: 115–25. PMID 11796116.
Hille R (1996). "The Mononuclear Molybdenum Enzymes". Chem. Rev. 96: 2757–2816. doi:10.1021/cr950061t. PMID 11848841.