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• W2023104402 startingPage "1774" @default.
• W2023104402 abstract "The dual nucleotide cofactor-specific enzyme, 3α-hydroxysteroid dehydrogenase (3α-HSD) from Pseudomonas sp. B-0831, is a member of the short-chain dehydrogenase/reductase (SDR) superfamily. Transient-phase kinetic studies using the fluorescence stopped-flow method were conducted with 3α-HSD to characterize the nucleotide binding mechanism. The binding of oxidized nucleotides, NAD+, NADP+ and nicotinic acid adenine dinucleotide (NAAD+), agreed well with a one-step mechanism, while that of reduced nucleotide, NADH, showed a two-step mechanism. This difference draws attention to previous characteristic findings on rat liver 3α-HSD, which is a member of the aldo-keto reductase (AKR) superfamily. Although functionally similar, AKRs are structurally different from SDRs. The dissociation rate constants associated with the enzyme–nucleotide complex formation were larger than the kcat values for either oxidation or reduction of substrates, indicating that the release of cofactors is not rate-limiting overall. It should also be noted that kcat for a substrate, cholic acid, with NADP+ was only 6% of that with NAD+, and no catalytic activity was detectable with NAAD+, despite the similar binding affinities of nucleotides. These results suggest that a certain type of nucleotide can modulate nucleotide-binding mode and further the catalytic function of the enzyme." @default.
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• W2023104402 date "2004-05-01" @default.
• W2023104402 modified "2023-10-03" @default.
• W2023104402 title "Transient-phase kinetic studies on the nucleotide binding to 3alpha-hydroxysteroid dehydrogenase from Pseudomonas sp. B-0831 using fluorescence stopped-flow procedures" @default.
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• W2023104402 doi "https://doi.org/10.1111/j.1432-1033.2004.04089.x" @default.
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