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首页> 外文期刊>Journal of Molecular Biology >A structural basis for substrate selectivity and stereoselectivity in octopine dehydrogenase from Pecten maximus.
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A structural basis for substrate selectivity and stereoselectivity in octopine dehydrogenase from Pecten maximus.

机译：最大果胶中章鱼碱脱氢酶中底物选择性和立体选择性的结构基础。

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摘要

Octopine dehydrogenase [N(2)-(D-1-carboxyethyl)-L-arginine:NAD(+) oxidoreductase] (OcDH) from the adductor muscle of the great scallop Pecten maximus catalyzes the reductive condensation of l-arginine and pyruvate to octopine during escape swimming. This enzyme, which is a prototype of opine dehydrogenases (OpDHs), oxidizes glycolytically born NADH to NAD(+), thus sustaining anaerobic ATP provision during short periods of strenuous muscular activity. In contrast to some other OpDHs, OcDH uses only l-arginine as the amino acid substrate. Here, we report the crystal structures of OcDH in complex with NADH and the binary complexes NADH/l-arginine and NADH/pyruvate, providing detailed information about the principles of substrate recognition, ligand binding and the reaction mechanism. OcDH binds its substrates through a combination of electrostatic forces and size selection, which guarantees that OcDH catalysis proceeds with substrate selectivity and stereoselectivity, giving rise to a second chiral centerand exploiting a "molecular ruler" mechanism.
机译：来自扇贝大花蜜最大内收肌的章鱼碱脱氢酶[N（2）-（D-1-羧乙基）-L-精氨酸：NAD（+）氧化还原酶]（OcDH）催化L-精氨酸和丙酮酸的还原缩合反应逃生游泳过程中的章鱼碱。这种酶是阿片脱氢酶（OpDHs）的原型，可将糖酵解的NADH氧化为NAD（+），从而在短时间内剧烈的肌肉活动中维持厌氧ATP的供应。与某些其他OpDH相比，OcDH仅使用1-精氨酸作为氨基酸底物。在这里，我们报告与NADH复杂的OcDH的晶体结构和二元复合物NADH / 1-精氨酸和NADH /丙酮酸盐，提供有关底物识别，配体结合和反应机理的详细信息。 OcDH通过静电力和大小选择的组合来结合其底物，从而确保OcDH催化以底物选择性和立体选择性进行，从而产生第二个手性中心并利用“分子尺”机制。

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