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Xanthine oxidase and xanthine dehydrogenase
Author(s) -
Hille Russ,
Nishino Takeshi
Publication year - 1995
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.9.11.7649415
Subject(s) - xanthine dehydrogenase , xanthine oxidase , biochemistry , dehydrogenase , flavin group , enzyme , xanthine , chemistry , nad+ kinase , purine , biology
Xanthine oxidase and xanthine dehy‐drogenase are enzymes involved in the metabolism of purines and pyrimidines in various organisms. Their relationship to one another has been the subject of considerable debate, primarily because of their proposed roles in ischemia/reperfasion damage in tissues. Differences in the kinetics and oxidation‐reduction behavior of the two forms are accounted for by the presence in the dehydrogenase of a binding site for NAD + , as well as a substantially lower reduction potential for the flavin FADH7FADH2 couple of the dehydrogenase relative to the oxidase. This review presents recent advances of our understanding of the biochemistry and molecular biology of these systems, including a model for the overall morphology of xanthine oxidizing enzymes. The evidence that the two enzymes represent alternate forms of the same gene product, in some cases reversibly interconvertible between one another, is discussed.—Hille, R., Nishino, T. Xanthine oxidase and xanthine dehydrogenase. FASEB JT. 9, 995‐1003 (1995)