1989
DOI: 10.1021/bi00440a049
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Mitochondrial nicotinamide nucleotide transhydrogenase: NADPH binding increases and NADP binding decreases the acidity and susceptibility to modification of cysteine-893

Abstract: The mitochondrial nicotinamide nucleotide transhydrogenase is a dimeric enzyme of monomer Mr 110,000. It is located in the inner mitochondrial membrane and catalyzes hydride ion transfer between NAD(H) and NADP(H) in a reaction that is coupled to proton translocation across the inner membrane. The amino acid sequence and the nucleotide binding sites of the enzyme have been determined [Yamaguchi, M., Hatefi, Y., Trach, K., & Hoch, J.A. (1988) J. Biol. Chem. 263, 2761-2767; Wakabayashi, S., & Hatefi, Y. (1987) B… Show more

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Cited by 25 publications
(8 citation statements)
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“…Further, the B-face is more exposed to solvent, consistent with biochemical data requiring direct hydride ion transfer between the 4A position of NAD(H) and the 4B position of NADP(H) 1,2 . Chemical modification 10,11 and site-directed mutagenesis data [12][13][14][15][16][17] are in agreement with the observed binding of NADP. Based on these mutagenesis studies, and homology of the E. coli NADP(H) binding domain with classical nucleotide binding folds, a model has been proposed for the structure of the E. coli domain with bound NADP(H) 17 .…”
Section: Non-classical Binding Of Nadpsupporting
confidence: 81%
“…Further, the B-face is more exposed to solvent, consistent with biochemical data requiring direct hydride ion transfer between the 4A position of NAD(H) and the 4B position of NADP(H) 1,2 . Chemical modification 10,11 and site-directed mutagenesis data [12][13][14][15][16][17] are in agreement with the observed binding of NADP. Based on these mutagenesis studies, and homology of the E. coli NADP(H) binding domain with classical nucleotide binding folds, a model has been proposed for the structure of the E. coli domain with bound NADP(H) 17 .…”
Section: Non-classical Binding Of Nadpsupporting
confidence: 81%
“…The modification of cysteine residues in transhydrogenases has been studied both with the E. coli enzyme [29,30] and with the bovine enzyme [33][34][35][36]. Comparisons are difficult to make, since the residue corresponding to βCys-260 in E. coli transhydrogenase (residue 834 in the bovine enzyme) is the only conserved cysteine residue located in a domain composed of a sequence of about 12 conserved residues.…”
Section: Discussionmentioning
confidence: 99%
“…Specific activity (mol AcPyAD or AcPyADP reduced/min/mg protein) is expressed per mg of bovine or R. rubrum domain I where one or the other was present. The NADPH 3 AcPyAD activity of purified bovine transhydrogenase is 30 -32 mol AcPyAD reduced (min ⅐ mg) Ϫ1 (Yamaguchi and Hatefi, 1993 chi and Hatefi, 1989). As seen in Table II, NEM had no inhibitory effect on the R. rubrum ␣1 subunit but inhibited the bovine domain III.…”
Section: Table Imentioning
confidence: 96%
“…Also, similar to the intact bovine enzyme, addition of NADPH but not NADH stimulated the NEM inhibition. In the bovine transhydrogenase, it was shown that the reason for this augmentation of the NEM inactivation rate is that in the presence of NADPH, the effective pK a of Cys 893 is lowered from 9.1 to 8.7 (Yamaguchi and Hatefi, 1989). Not shown in Table II is the inhibitory effect of palmitoyl-CoA (Rydström, 1972).…”
Section: Table Imentioning
confidence: 99%