Enzyme

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     1. Oxidoreductases
        1.17 Acting on CH or CH2 groups
            1.17.1 With NAD+ or NADP+ as acceptor
ID:1.17.1.4
Description:Xanthine dehydrogenase.
Alternative Name: Xanthine/NAD(+) oxidoreductase.
Xanthine-NAD oxidoreductase.
Xanthine oxidoreductase.
NAD-xanthine dehydrogenase.
Prosite: PDOC00484;
PDB:
PDBScop
Cath: 1.10.150.120; 3.30.365.10; 3.30.390.50; 3.30.43.10; 3.30.43.30; 3.30.465.10; 3.90.1170.50; 3.10.20.30;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.17.1.4
BRENDA Enzyme Link: BRENDA 1.17.1.4
KEGG Enzyme Link: KEGG1.17.1.4
BioCyc Enzyme Link: BioCyc 1.17.1.4
ExPASy Enzyme Link: ExPASy1.17.1.4
EC2PDB Enzyme Link: EC2PDB 1.17.1.4
ExplorEnz Enzyme Link: ExplorEnz 1.17.1.4
PRIAM enzyme-specific profiles Link: PRIAM 1.17.1.4
IntEnz Enzyme Link: IntEnz 1.17.1.4
MEDLINE Enzyme Link: MEDLINE 1.17.1.4
MSA:

1.17.1.4;

Phylogenetic Tree:

1.17.1.4;

Uniprot:
M-CSA:
RHEA:24670 H2O + hypoxanthine + NAD(+) = H(+) + NADH + xanthine
RULE(radius=1) [*:1]-[n+;H0:2]1:[cH;+0:3]:[cH;+0:4]:[cH;+0:5]:[c;H0;+0:6](-[*:7]):[cH;+0:8]:1.[*:9]:[cH;+0:10]:[n;H0;+0:11]:[*:12]1:[*:13]:[nH;+0:14]:[*:15]:[n;H0;+0:16]:1.[OH2;+0:17]>>[*:1]-[N;H0;+0:2]1-[CH;+0:3]=[CH;+0:4]-[CH2;+0:5]-[C;H0;+0:6](-[*:7])=[CH;+0:8]-1.[*:9]:[c;H0;+0:10](=[O;H0;+0:17]):[nH;+0:11]:[*:12]1:[*:13]:[n;H0;+0:14]:[*:15]:[nH;+0:16]:1
Reaction
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References

TitleAuthorsDatePubMed ID
Crystal structures of the active and alloxanthine-inhibited forms of xanthine dehydrogenase from Rhodobacter capsulatus.Truglio JJ, Theis K, Leimkühler S, Rappa R, Rajagopalan KV, Kisker C2002 Jan11796116
Purine catabolism in Escherichia coli and function of xanthine dehydrogenase in purine salvage.Xi H, Schneider BL, Reitzer L2000 Oct10986234

RHEA:16669 H2O + NAD(+) + xanthine = H(+) + NADH + urate
RULE(radius=1) [*:1]-[n+;H0:2]1:[cH;+0:3]:[cH;+0:4]:[cH;+0:5]:[c;H0;+0:6](-[*:7]):[cH;+0:8]:1.[*:9]:[n;H0;+0:10]:[cH;+0:11]:[*:12].[OH2;+0:13]>>[*:1]-[N;H0;+0:2]1-[CH;+0:3]=[CH;+0:4]-[CH2;+0:5]-[C;H0;+0:6](-[*:7])=[CH;+0:8]-1.[*:9]:[nH;+0:10]:[c;H0;+0:11](:[*:12])=[O;H0;+0:13]
Reaction
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References

TitleAuthorsDatePubMed ID
Cloning of the cDNA encoding human xanthine dehydrogenase (oxidase): structural analysis of the protein and chromosomal location of the gene.Ichida K, Amaya Y, Noda K, Minoshima S, Hosoya T, Sakai O, Shimizu N, Nishino T1993 Nov 158224915
Purification and properties of a new glutathione-dependent thiol:disulphide oxidoreductase from rat liver.Battelli MG, Lorenzoni E1982 Oct 16960894
Purification and properties of xanthine dehydroganase from Micrococcus lactilyticus.Smith ST, Rajagopalan KV, Handler P1967 Sep 256061702
The regulation of rat liver xanthine oxidase. Involvement of thiol groups in the conversion of the enzyme activity from dehydrogenase (type D) into oxidase (type O) and purification of the enzyme.Corte ED, Stirpe F1972 Feb4342395
Purification and properties of chicken liver xanthine dehydrogenase.Rajagopalan KV, Handler P1967 Sep 254294045
The presence of desulfo xanthine dehydrogenase in purified and crude enzyme preparations from rat liver.Ikegami T, Nishino T1986 Jun3459393
Conversion of xanthine dehydrogenase to oxidase in ischemic rat tissues.Engerson TD, McKelvey TG, Rhyne DB, Boggio EB, Snyder SJ, Jones HP1987 Jun3294898
Interconversion between NAD-dependent and O2-dependent types of rat liver xanthine dehydrogenase and difference in kinetic and redox properties between them.Saito T, Nishino T, Tsushima K19892610112
Xanthine dehydrogenase processes retinol to retinoic acid in human mammary epithelial cells.Taibi G, Di Gaudio F, Nicotra CM2008 Jun18569334
Mammalian xanthine oxidoreductase - mechanism of transition from xanthine dehydrogenase to xanthine oxidase.Nishino T, Okamoto K, Eger BT, Pai EF, Nishino T2008 Jul18513323
PURIFICATION OF XANTHINE DEHYDROGENASE FROM DROSOPHILA MELANOGASTER.PARZEN SD, FOX AS1964 Dec 2314264879
The Mononuclear Molybdenum Enzymes.Hille R1996 Nov 711848841
Crystal structures of the active and alloxanthine-inhibited forms of xanthine dehydrogenase from Rhodobacter capsulatus.Truglio JJ, Theis K, Leimkühler S, Rappa R, Rajagopalan KV, Kisker C2002 Jan11796116
Xanthine dehydrogenase from Pseudomonas putida 86: specificity, oxidation-reduction potentials of its redox-active centers, and first EPR characterization.Parschat K, Canne C, Hüttermann J, Kappl R, Fetzner S2001 Jan 1211341925
Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion.Enroth C, Eger BT, Okamoto K, Nishino T, Nishino T, Pai EF2000 Sep 2611005854