[Effect of deuteration on methanol dehydrogenase activity in Methylophilus sp. B-7741].
We studied the effect of deuterium oxide present in the medium on the activity of methanol dehydrogenase (EC 1.1.99.8) from methylotrophic bacteria Methylophilus sp. B-7741. Methanol dehydrogenase activity in extracts of the biomass obtained in a highly deuterated medium (2H-enzyme) was 34-47% of enzyme activity in the control biomass, which depended on reaction conditions. The isotopic effects of substrate deuterium (methanol) for 1H-enzyme and 2H-enzyme were 1.37 +/- 0.05 and 1.38 +/- 0.01, respectively. We revealed for the first time the reverse isotopic effect of solvent deuterium in the reaction catalyzed by methanol dehydrogenase (0.80 +/- 0.02 and 0.60 +/- 0.01 for 1H-enzyme and 2H-enzyme, respectively).
Pshenichnikova
A B
AB
Lomonosov Moscow State Academy of Fine Chemical Technology, Moscow, 117571 Russia.
Nevo
A N
AN
Volkova
E V
EV
Skladnev
D A
DA
Shvets
V I
VI
D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D018533:Biomass; D003903:Deuterium; D007554:Isotopes; D020629:Methylophilus / Q000201:enzymology / Q000378:metabolism*; D013379:Substrate Specificity
D007554:Isotopes; D003903:Deuterium; D000429:Alcohol Oxidoreductases; C019641:alcohol dehydrogenase (acceptor)