Abstract
Abstract Threonine deaminase (l-threonine hydro-lyase (deaminating), EC 4.2.1.16) has been purified from crude extracts of Bacillus subtilis. The enzyme in crude extracts and after crystallization yielded substrate saturation curves which were hyperbolic unless the inhibitor, isoleucine, was present. Sigmoid substrate saturation curves were obtained in the presence of isoleucine. In crude extracts, the enzyme was stabilized in phosphate buffer at room temperature by pyridoxal phosphate. Under these conditions, however, the enzyme was cold labile. After treatment with brushite during the purification procedure the enzyme was cold stable. The enzyme had a molecular weight of about 200,000 and could be dissociated into half-molecules by urea, guanidine, and sodium lauryl sulfate. Electron microscopy suggested a dimeric structure.
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