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A specific trehalose phosphate phosphatase was purified approximately 50-fold fromMycobacterium smegmatis . The enzyme had ap H optimum of about 7.0 and was stimulated by Mg2+ . The optimum concentration of Mg2+ was about 1.5 × 10−3 m . Of other divalent cations tested, only Co2+ showed some activity. TheK m for trehalose phosphate was found to be about 1.5 × 10−3 m . 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.

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