A kinetic method for distinguishing whether an enzyme has one or two active sites for two different substrates. Rat liver L-threonine dehydratase has a single active site for threonine and serine.
We have elaborated a kinetic method which allows us to evaluate whether a Michaelis-Menten-type enzyme acting on two different substrates has one or two active sites. This method has been used with the rat liver L-threonine dehydratase, which catalyzes the dehydrative deamination of both serine and threonine. The experimental data can be fitted to the theoretical plot obtained for the case of a single active site.
D000818:Animals; D001665:Binding Sites; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008297:Male; D008433:Mathematics; D051381:Rats; D011919:Rats, Inbred Strains; D012694:Serine / Q000378:metabolism*; D013379:Substrate Specificity; D013912:Threonine / Q000378:metabolism*; D013913:Threonine Dehydratase / Q000378:metabolism*
D013912:Threonine; D012694:Serine; D013913:Threonine Dehydratase