Open AccessA kinetic method for distinguishing whether an enzyme has one or two active sites for two different substrates
Author(s) -
KELETI Tamás,
LEONCINI Roberto,
PAGANI Roberto,
MARINELLO Enrico
Publication year - 1987
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1987.tb13684.x
Subject(s) - deamination , active site , threonine , enzyme , serine , chemistry , dehydratase , biochemistry , kinetic energy , stereochemistry , physics , quantum mechanics
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.