KINETIC-PROPERTIES OF TRIOSE-PHOSPHATE ISOMERASE FROM TRYPANOSOMA-BRUCEI-BRUCEI - A COMPARISON WITH THE RABBIT MUSCLE AND YEAST ENZYMES
KINETIC-PROPERTIES OF TRIOSE-PHOSPHATE ISOMERASE FROM TRYPANOSOMA-BRUCEI-BRUCEI - A COMPARISON WITH THE RABBIT MUSCLE AND YEAST ENZYMES
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DOI：
10.1111/j.1432-1033.1987.tb13388.x
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发表时间：
1987-10-01
期刊：
影响因子：
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通讯作者：
WIERENGA, RK
中科院分区：
文献类型：
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作者：
LAMBEIR, AM;OPPERDOES, FR;WIERENGA, RK
将布氏锥虫布氏丙糖磷酸异构酶的动力学特性与市售的兔肌肉酶和酵母酶的动力学特性以及鸡肌肉酶的已发表数据进行比较。以甘油醛3-磷酸为底物Km=0.25.+-。 0.05 mM 和 kcat = 3.7 倍。 105 分钟-1。以磷酸二羟基丙酮为底物Km=1.2.+-。 0.1 mM 和 kcat = 6.5 倍。 104 分钟-1。 0.1 M 离子强度下 Km 和 Vmax 的 pH 依赖性与针对酵母和鸡肌肉酶发表的结果一致。在离子强度低于 0.05 M 时，可以检测到锥虫酶特异的带电基团的作用，而酵母和兔肌肉酶中不存在该带电基团的作用。这种效应显着增加了 Km，而 Vmax 则略有提高。锥虫磷酸丙糖异构酶受硫酸根、磷酸根和砷酸根离子、2-磷酸乙醇酸和许多已记录的抑制剂的抑制，其浓度范围与其他磷酸丙糖异构酶相同。杀锥虫药物苏拉明以相同程度抑制布氏锥虫和兔肌肉磷酸丙糖异构酶，而酵母酶相对不受影响。
The kinetic properties of Trypanosoma brucei brucei triose-phosphate isomerase are compared with those of the commerically available rabbit muscle and yeast enzymes and with published data on the chicken muscle enzyme. With glyceraldehyde 3-phosphate as substrate Km = 0.25 .+-. 0.05 mM and kcat = 3.7 .times. 105 min-1. With dihydroxyacetone phosphate as substrate Km = 1.2 .+-. 0.1 mM and kcat = 6.5 .times. 104 min-1. The pH dependence of Km and Vmax at 0.1 M ionic strength is in agreement with the results published for the yeast and chicken muscle enzymes. At ionic strength below 0.05 M the effect of a charged group specific for the trypanosomal enzyme and absent from the yeast and rabbit muscle enzymes becomes detectable. This effect significantly increased Km whereas Vmax becomes slightly higher. Trypanosomal triose-phosphate isomerase is inhibited by sulphate, phosphate and arsenate ions, by 2-phosphoglycolate and a number of documented inhibitors in the same concentration range as are the other triose-phosphate isomerases. The trypanocidal drug, Suramin inhibits T. brucei and rabbit muscle triose-phosphate isomerase to the same extent while leaving the yeast enzyme relatively unaffected.