[Study of the complex formation between alpha- and beta- forms of NAD-kinase and glutamate dehydrogenase and the effect of metabolites on enzyme interaction].
The alpha- and beta-forms of rabbit liver NAD kinase were found to differ significantly in terms of their ability to form complexes with glutamate dehydrogenase. The beta-form of the enzyme was shown to form a more stable complex with glutamate dehydrogenase (Kd = 1.5.10(-8) M), whereas the Kd value for the alpha-form is 2.9.10(-7) M. Using two independent methods, it was shown that in the absence of effectors 40% of the beta-form of NAD kinase and up to 20% of the alpha-form are bound to glutamate dehydrogenase. The substrates of NAD kinase markedly activate the complex formation only in the case of the alpha-form of the enzyme. The time needed for this process is also reduced in the presence of the substrates.
Telepneva
V I
VI
Voronina
O L
OL
Bulygina
E R
ER
D000818:Animals; D002417:Cattle; D005969:Glutamate Dehydrogenase / Q000378:metabolism*; D007527:Isoenzymes / Q000378:metabolism*; D008099:Liver / Q000201:enzymology; D009097:Multienzyme Complexes / Q000378:metabolism*; D010770:Phosphotransferases / Q000378:metabolism*; D017853:Phosphotransferases (Alcohol Group Acceptor); D011817:Rabbits; D013379:Substrate Specificity
D007527:Isoenzymes; D009097:Multienzyme Complexes; D005969:Glutamate Dehydrogenase; D010770:Phosphotransferases; D017853:Phosphotransferases (Alcohol Group Acceptor); C021844:NAD kinase
Izuchenie kompleksoobrazovaniia mezhdu alpha- i beta-formami NAD- kinazy i glutamatdegidrogenazoĭ i vliianiia metabolitov na vzaimodeĭstvie fermentov.