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曼氏血吸虫三磷酸甘油醛异构酶:一个潜在药物和疫苗靶点的生化特性分析。

Triose phosphate isomerase from the blood fluke Schistosoma mansoni: biochemical characterisation of a potential drug and vaccine target.

机构信息

School of Biological Sciences, Queen's University Belfast, Medical Biology Centre, 97 Lisburn Road, Belfast BT9 7BL, UK.

出版信息

FEBS Lett. 2013 Nov 1;587(21):3422-7. doi: 10.1016/j.febslet.2013.09.022. Epub 2013 Sep 23.

DOI:10.1016/j.febslet.2013.09.022
PMID:24070897
Abstract

The glycolytic enzyme triose phosphate isomerase from Schistosoma mansoni is a potential target for drugs and vaccines. Molecular modelling of the enzyme predicted that a Ser-Ala-Asp motif which is believed to be a helminth-specific epitope is exposed. The enzyme is dimeric (as judged by gel filtration and cross-linking), resistant to proteolysis and highly stable to thermal denaturation (melting temperature of 82.0 °C). The steady-state kinetic parameters are high (Km for dihydroxyacetone phosphate is 0.51 mM; Km for glyceraldehyde 3-phosphate is 1.1 mM; kcat for dihydroxyacetone phosphate is 7800 s(-1) and kcat for glyceraldehyde 3-phosphate is 6.9s(-1)).

摘要

曼氏血吸虫糖酵解酶磷酸丙糖异构酶是药物和疫苗的潜在靶点。对该酶的分子建模预测,一个丝氨酸-丙氨酸-天冬氨酸基序(被认为是一种寄生虫特异性表位)暴露在外。该酶是二聚体(通过凝胶过滤和交联判断),具有抗蛋白水解和对热变性(熔点为 82.0°C)高度稳定的特性。稳态动力学参数较高(二羟丙酮磷酸的 Km 为 0.51mM;甘油醛 3-磷酸的 Km 为 1.1mM;二羟丙酮磷酸的 kcat 为 7800s(-1),甘油醛 3-磷酸的 kcat 为 6.9s(-1))。

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