Reference: Betz JL, et al. (1971) Threonine deaminases from Saccharomyces cerevisiae mutationally altered in regulatory properties. Biochemistry 10(10):1818-24

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Abstract


Two mutants of Saccharomyces cereoisiae resistant to 5 x 10^-3 M thiaisoleucine were found to have threonine deaminases 10- and 100-fold less sensitive than the wild type to L-isoleucine as inhibitor. The apparent affinity for L-threonine as substrate, L-valine as activator, and L-isoleucine as activator was unchanged. Reversal of the isoleucine inhibition required higher concentrations of valine in the mutants as compared to the wild type. The enzyme was shown to exhibit cooperativity with respect to substrate in the absence of effecors, and with respect to activators as well. The kinetics of activation by valine or by isoleucine may be described by a modification of the allosteric equation of Monod, Wyman, and Changeux (1965, J. Mol. Biol. 12, 88). A tentative model for the interactions of the enzyme with its substrate and effectors, with two sorts of sites able to bind isoleucine or valine, is proposed. This model accounts for the activation as well as the inhibition by isoleucine.

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Journal Article
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Betz JL, Hereford LM, Magee PT
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