Reference: Ahmed SI, et al. (1976) Purification and properties of threonine deaminase from Saccharomyces cerevisiae. Biochimie 58(1-2):225-32

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Abstract


Threonine deaminase (L-theonine hydro-lyase (deaminating), E.C. 4.2.1.16) has been purified to homogeneity from extracts of Saccharomyces cerevisiae. When purified 1200-fold, the enzyme is homogeneous by the criterion of sodium dodecyl sulfate-polyacrylamide electrophoresis. The reduced and alkylated protein has a molecular weight of approximately 50,000 daltons, one-fourth the value determined previously for the intact enzyme. The purified enzyme exhibits homotropic effects with the substrate; these effects are descresed in the presence of DL-allothreonine, a competitive inhibitor. Half-maximal velocity is achieved at 34 mM L-threonine in the absence of other effectors. L-isoleucine both stimulates at low (0.01-0.05 mM) concentrations and inhibits at high (0.1-1.0 mM) concentrations. Valine activates the enzyme in the absence of isoleucine ; in the presence of isoleucine it reverses inhibition.

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Journal Article | Research Support, U.S. Gov't, Non-P.H.S. | Research Support, U.S. Gov't, P.H.S.
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Ahmed SI, Bollon AP, Rogers SJ, Magee PT
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