Biology:Xanthine dehydrogenase
Generic protein structure example |
xanthine dehydrogenase | |||||||||
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Bos taurus | |||||||||
Identifiers | |||||||||
EC number | 1.17.1.4 | ||||||||
CAS number | 9054-84-6 | ||||||||
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 | ||||||||
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Xanthine dehydrogenase, also known as XDH, is a protein that, in humans, is encoded by the XDH gene.[1][2]
Function
Xanthine dehydrogenase belongs to the group of molybdenum-containing hydroxylases involved in the oxidative metabolism of purines. The enzyme is a homodimer. Xanthine dehydrogenase can be converted to xanthine oxidase by reversible sulfhydryl oxidation or by irreversible proteolytic modification.[1]
Xanthine dehydrogenase catalyzes the following chemical reaction:
The three substrates of this enzyme are xanthine, NAD+, and H2O, whereas its three products are urate, NADH, and H+.
This enzyme participates in purine metabolism.
Nomenclature
This enzyme belongs to the family of oxidoreductases, to be specific, those acting on CH or CH2 groups 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.
Clinical significance
Defects in xanthine dehydrogenase cause xanthinuria, may contribute to adult respiratory stress syndrome, and may potentiate influenza infection through an oxygen metabolite-dependent mechanism.[1] It has been shown that patients with lung adenocarcinoma tumors which have high levels of XDH gene expression have lower survivals.[3][4] Addiction to XDH protein has been used to target NSCLC tumors and cell lines in a precision oncology manner.[4]
See also
- Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain
- MOCOS
- Xanthine oxidase
References
- ↑ 1.0 1.1 1.2 "Entrez Gene: XDH xanthine dehydrogenase". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7498.
- ↑ "Cloning of the cDNA encoding human xanthine dehydrogenase (oxidase): structural analysis of the protein and chromosomal location of the gene". Gene 133 (2): 279–84. November 1993. doi:10.1016/0378-1119(93)90652-J. PMID 8224915.
- ↑ "Acquired xanthine dehydrogenase expression shortens survival in patients with resected adenocarcinoma of lung". Tumour Biology 33 (5): 1727–32. October 2012. doi:10.1007/s13277-012-0431-2. PMID 22678977.
- ↑ 4.0 4.1 "Genomic signatures defining responsiveness to allopurinol and combination therapy for lung cancer identified by systems therapeutics analyses". Molecular Oncology 13 (8): 1725–1743. May 2019. doi:10.1002/1878-0261.12521. PMID 31116490.
Further reading
- "Purification and properties of a new glutathione-dependent thiol:disulphide oxidoreductase from rat liver". The Biochemical Journal 207 (1): 133–8. October 1982. doi:10.1042/bj2070133. PMID 6960894.
- "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". The Biochemical Journal 126 (3): 739–45. February 1972. doi:10.1042/bj1260739. PMID 4342395.
- "Purification of xanthine dehydrogenase from Drosophila melanogaster". Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects 92 (3): 465–71. December 1964. doi:10.1016/0926-6569(64)90006-9. PMID 14264879.
- "Purification and properties of chicken liver xanthine dehydrogenase". The Journal of Biological Chemistry 242 (18): 4097–107. September 1967. doi:10.1016/S0021-9258(18)95784-4. PMID 4294045.
- "Purification and properties of xanthine dehydroganase from Micrococcus lactilyticus". The Journal of Biological Chemistry 242 (18): 4108–17. September 1967. doi:10.1016/S0021-9258(18)95785-6. PMID 6061702.
- "Xanthine dehydrogenase from Pseudomonas putida 86: specificity, oxidation-reduction potentials of its redox-active centers, and first EPR characterization". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1544 (1–2): 151–65. January 2001. doi:10.1016/S0167-4838(00)00214-4. PMID 11341925.
- "Cloning of the cDNA encoding human xanthine dehydrogenase (oxidase): structural analysis of the protein and chromosomal location of the gene". Gene 133 (2): 279–84. November 1993. doi:10.1016/0378-1119(93)90652-J. PMID 8224915.
- "Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion". Proceedings of the National Academy of Sciences of the United States of America 97 (20): 10723–8. September 2000. doi:10.1073/pnas.97.20.10723. PMID 11005854. Bibcode: 2000PNAS...9710723E.
- "Crystal structures of the active and alloxanthine-inhibited forms of xanthine dehydrogenase from Rhodobacter capsulatus". Structure 10 (1): 115–25. January 2002. doi:10.1016/S0969-2126(01)00697-9. PMID 11796116.
- "The Mononuclear Molybdenum Enzymes". Chemical Reviews 96 (7): 2757–2816. November 1996. doi:10.1021/cr950061t. PMID 11848841.
- "The physiology of endothelial xanthine oxidase: from urate catabolism to reperfusion injury to inflammatory signal transduction". Microcirculation 9 (3): 161–75. July 2002. doi:10.1038/sj.mn.7800136. PMID 12080414.
- "Molecular cloning, tissue expression of human xanthine dehydrogenase". Biochemical and Biophysical Research Communications 215 (1): 429. October 1995. doi:10.1006/bbrc.1995.2482. PMID 7575623.
- "Assignment of human xanthine dehydrogenase gene to chromosome 2p22". Genomics 23 (1): 289–91. September 1994. doi:10.1006/geno.1994.1498. PMID 7829092.
- "Mapping of the gene for human xanthine dehydrogenase (oxidase) (XDH) to band p23 of chromosome 2". Cytogenetics and Cell Genetics 68 (1–2): 52–3. 1994. doi:10.1159/000133887. PMID 7956358.
- "The human gene for xanthine dehydrogenase (XDH) is localized on chromosome band 2q22". Cytogenetics and Cell Genetics 68 (1–2): 61–3. 1994. doi:10.1159/000133890. PMID 7956361.
- "Molecular cloning, tissue expression of human xanthine dehydrogenase". Biochemical and Biophysical Research Communications 199 (2): 998–1004. March 1994. doi:10.1006/bbrc.1994.1328. PMID 8135849.
- "Cloning of the cDNA encoding human xanthine dehydrogenase (oxidase): structural analysis of the protein and chromosomal location of the gene". Gene 133 (2): 279–84. November 1993. doi:10.1016/0378-1119(93)90652-J. PMID 8224915.
- "Regulation of xanthine dehydrogenase in rat liver in response to peroxisome proliferators". Biochemical and Biophysical Research Communications 195 (2): 751–7. September 1993. doi:10.1006/bbrc.1993.2109. PMID 8373410.
- "Molecular cloning and characterization of the human xanthine dehydrogenase gene (XDH)". Genomics 34 (2): 173–80. June 1996. doi:10.1006/geno.1996.0262. PMID 8661045.
- "Cloning and expression in vitro of human xanthine dehydrogenase/oxidase". The Biochemical Journal 315 (Pt 1): 235–9. April 1996. doi:10.1042/bj3150235. PMID 8670112.
- "Xanthine oxidase/dehydrogenase is present in human placenta". Placenta 17 (5–6): 361–5. 1996. doi:10.1016/S0143-4004(96)90061-2. PMID 8829220.
- "Xanthine oxidase in human skeletal muscle following eccentric exercise: a role in inflammation". The Journal of Physiology 498 (Pt 1): 239–48. January 1997. doi:10.1113/jphysiol.1997.sp021855. PMID 9023782.
- "Identification of two mutations in human xanthine dehydrogenase gene responsible for classical type I xanthinuria". The Journal of Clinical Investigation 99 (10): 2391–7. May 1997. doi:10.1172/JCI119421. PMID 9153281.
- "Expression of xanthine oxidase activity in human endothelial cells as a function of cell density". Biochemical Society Transactions 25 (3): 532S. August 1997. doi:10.1042/bst025532s. PMID 9388748.
- "Detection of xanthine oxidase in human plasma". The Medical Journal of Malaysia 53 (1): 70–5. March 1998. PMID 10968141.
- "Nuclear factor Y activates the human xanthine oxidoreductase gene promoter". FEBS Letters 480 (2–3): 84–8. September 2000. doi:10.1016/S0014-5793(00)01909-8. PMID 11034305.
- "Carcinogenic aristolochic acids upon activation by DT-diaphorase form adducts found in DNA of patients with Chinese herbs nephropathy". Carcinogenesis 23 (4): 617–25. April 2002. doi:10.1093/carcin/23.4.617. PMID 11960915.
- "Ultrastructural localization of xanthine oxidoreductase activity in isolated rat liver cells". Acta Histochemica 104 (1): 29–37. 2002. doi:10.1078/0065-1281-00629. PMID 11993848.
- "Xanthine oxidoreductase and xanthine oxidase in human cornea". Histology and Histopathology 17 (3): 755–60. 2003. doi:10.14670/HH-17.755. PMID 12168784.
External links
- Overview of all the structural information available in the PDB for UniProt: P47989 (Xanthine dehydrogenase/oxidase) at the PDBe-KB.
Original source: https://en.wikipedia.org/wiki/Xanthine dehydrogenase.
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