Re-face stereospecificity at C4 of NAD(P) for alcohol dehydrogenase from Methanogenium organophilum and for (R)-2-hydroxyglutarate dehydrogenase from Acidaminococcus fermentans as determined by 1H-NMR spectroscopy.
The two diastereotopic protons at C4 of NAD(P)H are seen separately in 1H-NMR spectra. This fact was used to determine the stereospecificity at C4 of NAD(P) for the NADP-dependent alcohol dehydrogenase from Methanogenium organophilum and for the NAD-dependent (R)-2-hydroxyglutarate dehydrogenase from Acidaminococcus fermentans. The reduction of NADP+ with [2H6]ethanol was found to yield (4R)-[4-2H1]NADPH and the oxidation of (4R)-[4-2H1]NADH with 2-oxoglutarate to yield unlabelled [4-1H]NAD+. These results indicate that both enzymes are Re-face stereospecific at C4 of the pyridine nucleotides.
Berk
H
H
Max-Planck-Institut für terrestrische Mikrobiologie, Marburg, Germany.
Buckel
W
W
Thauer
R K
RK
Frey
P A
PA
D000426:Alcohol Dehydrogenase / Q000737:chemistry / Q000378:metabolism*; D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D000595:Amino Acid Sequence; D001421:Bacteria, Anaerobic / Q000201:enzymology*; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D009249:NADP / Q000378:metabolism*; D011522:Protons; D013237:Stereoisomerism; D013379:Substrate Specificity
D011522:Protons; D009249:NADP; D000429:Alcohol Oxidoreductases; D000426:Alcohol Dehydrogenase; C023858:2-hydroxyglutarate dehydrogenase