Abstract
The stereospecificity of the enzyme-dependent oxidation of alpha-[4R-2H]NADH has been determined for four dehydrogenases: two pro-R specific enzymes, pig heart malate dehydrogenase and yeast alcohol dehydrogenase; and two pro-S specific enzymes, rabbit muscle glycerol-3-phosphate dehydrogenase and Rhodopseudomonas spheroides 3-hydroxybutyrate dehydrogenase. In all cases, an enzyme-dependent and substrate-specific oxidation to alpha-NAD+ is observed with the stereochemistry of oxidation identical with that found for the oxidation of the correspondingly labeled beta-NADH. The ability of dehydrogenases from diverse sources to utilize alpha-NADH in a stereochemically competent fashion is discussed in relation to proposed interactions between the nicotinamide sugar moiety and active site residues or obligatory alignments of the pyridine and sugar moieties.
Highlights
The stereospecificity of the enzyme-dependent oxi- One readily available coenzyme analog with an altered dation of
The stereospecificity of oxidation of a-NADH has only been determined for yeast alcohol dehydrogenase, the same enzyme for which the stereochemistry of the 3-substituted analogs has been determined (4); the applicability of these results to dehydrogenases in general must be addressed
The suggestion has been made that the stereospecific preference of dehydrogenases is governed by specific stereoelectronic interactions between the orbitals of the furanose ring oxygen and the lone pair on the ring nitrogen of NADH when bound in the active site (5, 6)
Summary
The stereospecificity of the enzyme-dependent oxi- One readily available coenzyme analog with an altered dation of The stereospecificity of oxidation of a-NADH has only been determined for yeast alcohol dehydrogenase, the same enzyme for which the stereochemistry of the 3-substituted analogs has been determined (4); the applicability of these results to dehydrogenases in general must be addressed.
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