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Partial Purification and Properties of a Highly Specific Trehalose Phosphate Phosphatase from Mycobacterium smegmatis

Department of Biochemistry, The University of Texas Medical School, San Antonio, Texas 78229

ABSTRACT

A specific trehalose phosphate phosphatase was purified approximately 50-fold from Mycobacterium smegmatis. The enzyme had a pH optimum of about 7.0 and was stimulated by Mg²⁺. The optimum concentration of Mg²⁺ was about 1.5 x 10^–3M. Of other divalent cations tested, only Co²⁺ showed some activity. The K_m for trehalose phosphate was found to be about 1.5 x 10^–3M. The enzyme showed slight activity toward mannose-6-P and fructose-6-P but was inactive on a large number of other phosphorylated compounds. Citrate was a competitive inhibitor of the enzyme both with respect to trehalose phosphate concentration and Mg²⁺ concentration. This inhibition appears to be due to chelation of Mg²⁺ by this compound. Ethylenediaminetetraacetic acid and NaF were also inhibitors of the enzyme, but these inhibitions were noncompetitive.

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