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首页> 外文期刊>Journal of Molecular Biology >Structural Enzymology of Li(+)-sensitive/Mg(2+)-dependent Phosphatases.
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Structural Enzymology of Li(+)-sensitive/Mg(2+)-dependent Phosphatases.

机译：Li（+）敏感/ Mg（2+）依赖性磷酸酶的结构酶学。

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Li(+)-sensitive/Mg(2+)-dependent phosphatases have attracted considerable attention since they have been proposed as targets for lithium therapy in the treatment of manic-depressive patients. The members of this enzyme superfamily display low levels of sequence identity while possessing a common fold and active site. Extensive structural and biochemical data demonstrate the direct involvement of two metal ions in catalysis, and show that lithium exerts its inhibitory action by blocking the products at the active site. By exploiting the different inhibitory properties of magnesium and calcium, we have been able to solve the X-ray structures of the Li(+)-sensitive/Mg(2+)-dependent 3'-phosphoadenosine-5'-phosphatase in complex with its substrate and with its products. The structural comparison of these complexes provides a 3D picture of the different stages of the catalytic cycle. This gives new insights into the understanding of the biological function of this group of enzymes and their lithium inhibition, and should assist in the design of improved inhibitors of therapeutic value.
机译：Li（+）敏感/ Mg（2+）依赖性磷酸酶已经引起了相当大的关注，因为它们已被提议作为躁狂抑郁症患者锂治疗的靶标。该酶超家族的成员显示低水平的序列同一性，同时具有共同的折叠和活性位点。大量的结构和生化数据表明，两种金属离子直接参与了催化作用，并表明锂通过在活性位点阻断产物发挥其抑制作用。通过利用镁和钙的不同抑制特性，我们已经能够解决Li（+）-敏感/ Mg（2 +）-依赖性3'-磷酸腺苷-5'-磷酸酶与X射线复合的结构它的基材及其产品。这些配合物的结构比较提供了催化循环不同阶段的3D图片。这为了解这一类酶的生物学功能及其对锂的抑制作用提供了新的见识，并应有助于设计治疗价值更高的抑制剂。

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