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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 1 H-NMR spectroscopy
The two diastereotopic protons at C4 of NAD(P)H are seen separately in 1 H-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 [ 2 H 6 ]ethanol was found to yield (4R)-[4- 2 H 1 ]NADPH and the oxidation of (4R)-[4- 2 H 1 ]NADH with 2-oxoglutarate to yield unlabelled [4- 1 H]NAD + . These results indicate that both enzymes are Re-face stereospecific at C4 of the pyridine nucleotides.
Max-Planck-Institut für terrestrische Mikrobiologie and Laboratorium für Mikrobiologie, Fachbereich Biologie der Philipps-Universität, Karl-von-Frisch-StraßeD-35043 MarburgGermany
Max-Planck-Institut für terrestrische Mikrobiologie and Laboratorium für Mikrobiologie, Fachbereich Biologie der Philipps-Universität, Karl-von-Frisch-StraßeD-35043 MarburgGermany
Max-Planck-Institut für terrestrische Mikrobiologie and Laboratorium für Mikrobiologie, Fachbereich Biologie der Philipps-Universität, Karl-von-Frisch-StraßeD-35043 MarburgGermany