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• W3087466986 abstract "1 Kinetic studies performed with naturally occurring pyridine nucleotides and their thioanalogues point to the existence of a ping-pong bi-bi mechanism for the NADH → TNAD+ and NADPH → (T)NAD+ reactions. Inhibition studies with NAD+ and NADP+, however, exclude this type of mechanism on the basis of the relations found. 2 A ternary complex mechanism is proposed in which the enzyme is first reduced to the fourequivalent reduced state by two moles of donor, before two moles of acceptor are bound to the reduced enzyme; the possibility of complex formation of the oxidised enzyme with NADP+ is included in the scheme. The kinetic patterns of the NADPH → TNAD+ reaction in the absence and presence of NADP+ can be explained by this mechanism. 3 The explanation of the kinetic patterns of the NADH → TNAD+ reaction can be given by slightly modifying the proposed mechanism in such a way that the sequence of addition of the first acceptor molecule and the second donor molecule is changed and assuming irreversible binding of the first acceptor molecule to the two-equivalent reduced enzyme. The high affinity of NAD+ for the reduced enzyme justifies the latter assumption. 4 The reduction of NADP+ and TNAD(P)+ proceeds due to the reversible binding of both substrates according to a rapid-equilibrium-random-bi-bi mechanism. The data of the reaction NADH → NADP+ and the NADP+ inhibition patterns of the reaction NADPH → TNADP+ are consistent with this mechanism." @default.
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• W3087466986 date "1971-12-01" @default.
• W3087466986 modified "2023-09-25" @default.
• W3087466986 title "Pyridine-Nucleotide Transhydrogenase. 5. Kinetic Studies on Transhydrogenase from Azotobacter vinelandii" @default.
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• W3087466986 doi "https://doi.org/10.1111/j.1432-1033.1971.tb19656.x" @default.
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