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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
Author(s) -
Berk Holger,
Buckel Wolfgang,
Thauer Rudolf K.,
Frey Perry A.
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01292-6
Subject(s) - stereospecificity , nad+ kinase , alcohol dehydrogenase , chemistry , yield (engineering) , dehydrogenase , stereochemistry , glycerol 3 phosphate dehydrogenase , cofactor , nucleotide , enzyme , biochemistry , catalysis , materials science , metallurgy , gene
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 (4 R )‐[4‐ 2 H 1 ]NADPH and the oxidation of (4 R )‐[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.