THE l -CYSTEINE DESULFHYDRASE OF ESCHERICHIA COLI

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Abstract
Cysteine desulfhydrase of E. coli was resolved with respect to pyridoxal-phosphate by grinding the bacterial cells with alumina. The enzyme preparation thus prepared is unaffected by adenosine-5-phosphate, and biotin, but is inhibited by alpha-ketoglutarate, tryptophan, glutamic acid, alanine and tris (hydroxymethyl) aminomethane. Optimum pH of the enzyme is 7.8; the optimum temperatrue, 40[degree]C. A Michaelis constant of 1.76 x 10-2 M/L was derived for enzymatic action at pH 7.8 and 40[degree]C.