关于Glu-68在乙醇脱氢酶中的作用
On the role of Glu-68 in alcohol dehydrogenase.
作者信息
Ryde U
机构信息
Department of Theoretical Chemistry, University of Lund, Sweden.
出版信息
Protein Sci. 1995 Jun;4(6):1124-32. doi: 10.1002/pro.5560040611.
Abstract
Theoretical computations (molecular dynamics and combined quantum chemical and molecular mechanical geometry optimizations) have been performed on horse liver alcohol dehydrogenase. The results provide evidence that Glu-68, a highly conserved residue located 0.47 nm from the catalytic zinc ion, may intermittently coordinate to the zinc ion. Structures with Glu-68 coordinated to the zinc ion are almost as stable as structures with Glu-68 at the crystal position and the barrier between the two configurations of Glu-68 is so low that it can readily be bypassed at room temperature. There is a cavity behind the zinc ion that seems to be tailored to allow such coordination of Glu-68 to the zinc ion. It is suggested that Glu-68 may facilitate the exchange of ligands in the substrate site by coordinating to the zinc ion when the old ligand dissociates.
摘要
已对马肝醇脱氢酶进行了理论计算（分子动力学以及量子化学与分子力学相结合的几何优化）。结果表明，位于距催化锌离子0.47纳米处的高度保守残基Glu-68可能会间歇性地与锌离子配位。Glu-68与锌离子配位的结构几乎与晶体位置上Glu-68的结构一样稳定，并且Glu-68两种构型之间的势垒很低，以至于在室温下很容易越过。锌离子后方有一个腔，似乎是为了使Glu-68能与锌离子进行这样的配位而形成的。有人提出，当旧配体解离时，Glu-68可能通过与锌离子配位来促进底物位点中配体的交换。
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本文引用的文献
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Structure of a triclinic ternary complex of horse liver alcohol dehydrogenase at 2.9 A resolution.分辨率为2.9埃的马肝醇脱氢酶三斜三元复合物的结构。
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