Ksantin dehidrogenaza
(Preusmjereno sa stranice Ksantinska oksidoreduktaza)
Ksantin dehidrogenaza (EC 1.17.1.4, NAD+-ksantinska dehidrogenaza, ksantin-NAD+ oksidoreduktaza, ksantin/NAD+ oksidoreduktaza, ksantinska oksidoreduktaza) je enzim sa sistematskim imenom ksantin:NAD+ oksidoreduktaza.[1][2][3][4][5][6][7][8][9][10][11][12][13][14][15] Ovaj enzim katalizuje sledeću hemijsku reakciju
| Ksantin dehidrogenaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Identifikatori | |||||||||
| EC broj | 1.17.1.4 | ||||||||
| CAS broj | 9054-84-6 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Ovaj enzim deluje na više purina i aldehida, uključujući hipoksantin.
Reference uredi
- ↑ Battelli, M.G. and Lorenzoni, E. (1982). „Purification and properties of a new glutathione-dependent thiol:disulphide oxidoreductase from rat liver”. Biochem. J. 207: 133-138. PMID 6960894.
- ↑ Della Corte, E. and Stirpe, F. (1972). „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”. Biochem. J. 126: 739-745. PMID 4342395.
- ↑ Parzen, S.D. and Fox, A.S. (1964). „Purification of xanthine dehydrogenase from Drosophila melanogaster”. Biochim. Biophys. Acta 92: 465-471. PMID 14264879.
- ↑ Rajagopalan, K.V. and Handler, P. (1967). „Purification and properties of chicken liver xanthine dehydrogenase”. J. Biol. Chem. 242: 4097-4107. PMID 4294045.
- ↑ Smith, S.T., Rajagopalan, K.V. and Handler, P. (1967). „Purification and properties of xanthine dehydroganase from Micrococcus lactilyticus”. J. Biol. Chem. 242: 4108-4117. PMID 6061702.
- ↑ Ikegami, T. and Nishino, T. (1986). „The presence of desulfo xanthine dehydrogenase in purified and crude enzyme preparations from rat liver”. Arch. Biochem. Biophys. 247: 254-260. PMID 3459393.
- ↑ Engerson, T.D., McKelvey, T.G., Rhyne, D.B., Boggio, E.B., Snyder, S.J. and Jones, H.P. (1987). „Conversion of xanthine dehydrogenase to oxidase in ischemic rat tissues”. J. Clin. Invest. 79: 1564-1570. PMID 3294898.
- ↑ Saito, T., Nishino, T. and Tsushima, K. (1989). „Interconversion between NAD-dependent and O2-dependent types of rat liver xanthine dehydrogenase and difference in kinetic and redox properties between them”. Adv. Exp. Med. Biol. 253B: 179-183. PMID 2610112.
- ↑ Parschat, K., Canne, C., Hüttermann, J., Kappl, R. and 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: 151-165. PMID 11341925.
- ↑ Ichida, K., Amaya, Y., Noda, K., Minoshima, S., Hosoya, T., Sakai, O., Shimizu, N. and 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: 279-284. PMID 8224915.
- ↑ Enroth, C., Eger, B.T., Okamoto, K., Nishino, T., Nishino, T. and Pai, E.F. (2000). „Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion”. Proc. Natl. Acad. Sci. USA 97: 10723-10728. PMID 11005854.
- ↑ Truglio, J.J., Theis, K., Leimkuhler, S., Rappa, R., Rajagopalan, K.V. and Kisker, C. (2002). „Crystal structures of the active and alloxanthine-inhibited forms of xanthine dehydrogenase from Rhodobacter capsulatus”. Structure 10: 115-125. PMID 11796116.
- ↑ Hille, R. (1996). „The mononuclear molybdenum enzymes”. Chem. Rev. 96: 2757-2816. PMID 11848841.
- ↑ Taibi, G., Di Gaudio, F. and Nicotra, C.M. (2008). „Xanthine dehydrogenase processes retinol to retinoic acid in human mammary epithelial cells”. J. Enzyme Inhib. Med. Chem. 23: 317-327. PMID 18569334.
- ↑ Nishino, T., Okamoto, K., Eger, B.T., Pai, E.F. and Nishino, T. (2008). „Mammalian xanthine oxidoreductase - mechanism of transition from xanthine dehydrogenase to xanthine oxidase”. FEBS J. 275: 3278-3289. PMID 18513323.
Literatura uredi
- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
- Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.