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.
Keleti, T., Leoncini, R., Pagani, R., Marinello, E. (1987). 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. EUROPEAN JOURNAL OF BIOCHEMISTRY, 170(1-2), 179-183 [10.1111/j.1432-1033.1987.tb13684.x].
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
LEONCINI, ROBERTO;PAGANI, ROBERTO;MARINELLO, ENRICO
1987-01-01
Abstract
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.
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https://hdl.handle.net/11365/23558
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