Activation of a Mutationally Altered Form of the Escherichia coli Alkaline Phosphatase by Zinc

From the ¹ From the Department of Microbiology, Washington University School of Medicine, St. Louis, Missouri 63110

An alkaline phosphatase-negative mutant of Escherichia coli has been found to synthesize a cross-reacting material that is deficient in zinc. Addition of zinc ions to the purified inactive protein leads to enzyme with activity that is 20% that of wild type enzyme. Activation consists of the binding of metal to the dimer form of this protein and is accompanied by changes in the spectral properties of the enzyme. Phosphate ions greatly stimulate this activation and, in growing cultures of a constitutive strain of this mutant, are shown to suppress the phenotypic expression of the structural gene mutation.

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