[The interaction of pyridine-adenine-dinucleotides containing a hydrazide group with swine muscle lactate dehydrogenase].
Hydrazide group of 4-substituted NAD analogues is shown to interact with functional groups of substrate-binding site in double complexes with pig muscle lactate dehydrogenase (isoenzyme M4). The lactic acid residue, which is structurally incorporated into NAD analogue, improves slightly the binding of dinucleotide, while 2,2,6,6-tetramethylpiperidine-1-oxyl residue considerably decreases the firmless of binding. The comparison of the inhibitory ability of oxamate, incotinic acid hydraxide and their spin-labelled derivatives indicates the restricted and stiff sizes of a substrate-binding site.
D000818:Animals; D001665:Binding Sites; D055598:Chemical Phenomena; D002621:Chemistry; D007527:Isoenzymes; D007700:Kinetics; D007770:L-Lactate Dehydrogenase; D009132:Muscles / Q000201:enzymology; D009243:NAD / Q000031:analogs & derivatives*; D013552:Swine
D007527:Isoenzymes; D009243:NAD; D007770:L-Lactate Dehydrogenase
Vzaimodeĭstvie piridin-adenin-dinukleotidov, soderzhashchikh gidrazidnuiu gruppu, s laktatdegidrogenazoĭ myshts svin'i