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Quinone Reductases

Authors
  • Ross, D.
  • Siegel, D.
Type
Book
Journal
Comprehensive Toxicology
Publication Date
Jan 01, 2010
Pages
207–218
Identifiers
DOI: 10.1016/B978-0-08-046884-6.00411-5
ISBN: 978-0-08-046884-6
Source
Elsevier
Keywords
License
Unknown

Abstract

Quinone reductases are a large group of enzymes that catalyze the reduction of quinones. NQO1 and NQO2 are the major mammalian quinone reductases that catalyze the reduction of quinones to hydroquinones. Both NQO1 and NQO2 are FAD-containing homodimers with similar catalytic mechanism and overlapping substrate specificities; however, major differences have been observed between the two enzymes in the utilization of reduced pyridine nucleotide cofactors and inhibitors. NQO1 and NQO2 undergo similar ARE/Nrf2-mediated transcriptional regulation and both enzymes have been shown to protect mice against chemical carcinogenesis. In humans single nucleotide polymorphisms have been discovered in both the NQO1 and NQO2 genes resulting in lower levels of functional proteins. In addition to reducing quinones to hydroquinones, NQO1 and NQO2 have been shown to perform additional antioxidant functions as well as protein–protein interactions involving the tumor suppressor p53. In cancer treatment NQO1 and NQO2 have been utilized as molecular targets because of the high levels of these enzymes in many human cancers in combination with their ability to bioactivate a wide-range of quinone antitumor drugs.

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