Enzymatic oxidation of some non-phosphorylated derivatives of dihydronicotinamide
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Regulation: Quinone reductase 2: From classical role in detoxification to emerging role as a novel regulator of cellular activities
2021, Encyclopedia of Biological Chemistry: Third EditionDiscovery of potent 4-aminoquinoline hydrazone inhibitors of NRH:quinoneoxidoreductase-2 (NQO2)
2019, European Journal of Medicinal ChemistryCitation Excerpt :NQO2 is a FAD-containing protein capable of oxidizing a variety of analogues of dihydronicotinamide. It is a structural analogue of NAD(P)H:quinone oxidoreductase 1 (NQO1, DT-diaphorase, EC.1.6.99.2) and while the two enzymes have similar properties there are major functional differences [10–12]. In particular, the two enzymes catalyse the reduction of various quinones into hydroquinones [12–15].
Evaluation of analogues of furan-amidines as inhibitors of NQO2
2018, Bioorganic and Medicinal Chemistry LettersNon-symmetrical furan-amidines as novel leads for the treatment of cancer and malaria
2016, European Journal of Medicinal ChemistryCharacterization of cofactors, substrates and inhibitor binding to flavoenzyme quinone reductase 2 by automated supramolecular nano-electrospray ionization mass spectrometry
2012, International Journal of Mass SpectrometryCitation Excerpt :QR1 and QR2 are closely related [2], since they share 59% (cDNA) and 44% (protein) similarity in their sequences, with the interesting difference that QR1 has a 43 amino acid longer C-terminus than QR2 [3]. Due to this particular fact, QR2 does not recognize NADH and NADPH as co-substrates but rather natural compounds possibly derived from those, such as N-ribosyl- or N-methyl-dihydronicotinamide [4,5]. Secondly, two papers are absolutely crucial in understanding the role of QR1 and QR2 in animals.
In silico identification and biochemical evaluation of novel inhibitors of NRH:quinone oxidoreductase 2 (NQO2)
2010, Bioorganic and Medicinal Chemistry Letters