The stereospecificity of oxidation of alpha-[4R-2H]NADH by dehydrogenases

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 R...

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Bibliographic Details
Published in:The Journal of biological chemistry 1986-09, Vol.261 (26), p.12209-12212
Main Author: Oppenheimer, N J
Format: Article
Language:English
Subjects:
Alcohol Dehydrogenase
Alcohol Oxidoreductases - metabolism
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Glycerolphosphate Dehydrogenase - metabolism
Hydroxybutyrate Dehydrogenase - metabolism
Magnetic Resonance Spectroscopy
Malate Dehydrogenase - metabolism
Myocardium - enzymology
NAD - metabolism
Oxidoreductases
Oxidoreductases - metabolism
Rabbits
Stereoisomerism
Swine
Yeasts - enzymology
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Summary: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.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)67225-4