[Lactate dehydrogenase activity in the presence of certain structural analogs of the nicotinamide fragment of NAD].
The activity of lactate dehydrogenase from the cattle myocardium extract as well as of this enzyme crystalline form was studied in the presence of structural analogues of the nicotinamide fragment NAD-amide, diethyl amide and N-oxymethyl amide of nicotinic acid. It is shown that the rate of the reaction catalyzed with lactate dehydrogenase under the effect of amide and N-oxymethyl amide of nicotinic acid decreases to a different extent depending on their concentration. Nicotinic diethyl amide practically has no effect on the activity of lactate dehydrogenase. Ki for crystalline lactate dehydrogenase and myocardium lactate dehydrogenase in the presence of nicotinic amide is 0.23.10-3 and 1.13.10-3 M. respectively, in the presence of nicotinic N-oxymethyl amide-0.30.10-3 and 0.10.10-3 M.
D000818:Animals; D002417:Cattle; D007700:Kinetics; D007770:L-Lactate Dehydrogenase / Q000378:metabolism*; D009206:Myocardium / Q000201:enzymology*; D009243:NAD / Q000031:analogs & derivatives* / Q000494:pharmacology; D013329:Structure-Activity Relationship
D009243:NAD; D007770:L-Lactate Dehydrogenase
Aktivnost' laktatdegidrogenazy v prisutstvii nekororykh strukturnykh analogov nikotinamidnogo fragmenta NAD.