Matula M, Mitchell M, Elbein A D
J Bacteriol. 1971 Jul;107(1):217-22. doi: 10.1128/jb.107.1.217-222.1971.
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 Mg(2+). The optimum concentration of Mg(2+) was about 1.5 x 10(-3)m. Of other divalent cations tested, only Co(2+) showed some activity. The K(m) for trehalose phosphate was found to be about 1.5 x 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 Mg(2+) concentration. This inhibition appears to be due to chelation of Mg(2+) by this compound. Ethylenediaminetetraacetic acid and NaF were also inhibitors of the enzyme, but these inhibitions were noncompetitive.
从耻垢分枝杆菌中纯化出一种特定的海藻糖磷酸磷酸酶，纯化倍数约为50倍。该酶的最适pH约为7.0，受Mg(2+)刺激。Mg(2+)的最适浓度约为1.5×10(-3)m。在测试的其他二价阳离子中，只有Co(2+)表现出一定活性。发现海藻糖磷酸的K(m)约为1.5×10(-3)m。该酶对甘露糖-6-磷酸和果糖-6-磷酸表现出轻微活性，但对大量其他磷酸化化合物无活性。柠檬酸在海藻糖磷酸浓度和Mg(2+)浓度方面都是该酶的竞争性抑制剂。这种抑制作用似乎是由于该化合物对Mg(2+)的螯合作用。乙二胺四乙酸和NaF也是该酶的抑制剂，但这些抑制作用是非竞争性的。
