Yeast glutathione reductase
作者： Gary Moroff , Raymond S. Ochs , Karl G. Brandt
DOI: 10.1016/0003-9861(76)90232-0
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摘要: Abstract Yeast glutathione reductase catalyzes a pyridine nucleotide transhydrogenase reaction using either NADPH or NADH as the electron donor and thionicotinamideadenine dinucleotide phosphate acceptor. Competitive substrate inhibition of by (Ki = 11 μM) is observed when donor. thionicotinamide-adenine 58 with The turnover numbers two reactions are similar equal to about 1% number for NADPH-dependent reduction oxidized catalyzed enzyme. kinetics analyzed in terms pingpong mechanism. It concluded that results from formation abortive complexes reduced form enzyme With donor, apparent Michaelis constant sensitive ionic composition assay medium. data interpreted support existence general nucleotide-binding site at active separate binding glutathione.
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