Contributions of Valine-292 in the Nicotinamide Binding Site of Liver Alcohol Dehydrogenase and Dynamics to Catalysis

Jon K. Rubach; S. Ramaswamy; Bryce V. Plapp

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Contributions of Valine-292 in the Nicotinamide Binding Site of Liver Alcohol Dehydrogenase and Dynamics to Catalysis

机译：缬氨酸-292在肝脏酒精脱氢酶烟酰胺结合位点的贡献及其动力学

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The participation of Val-292 in catalysis by alcohol dehydrogenase and the involvement of dynamics were investigated.

机译：研究了Val-292在乙醇脱氢酶催化中的参与以及动力学的参与。

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《Biochemistry》 |2001年第42期|共9页
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Jon K. Rubach; S. Ramaswamy; Bryce V. Plapp;
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1. Contributions of Valine-292 in the Nicotinamide Binding Site of Liver Alcohol Dehydrogenase and Dynamics to Catalysis [J] . Jon K. Rubach, S. Ramaswamy, Bryce V. Plapp Biochemistry . 2001,第42期

机译：缬氨酸-292在肝脏酒精脱氢酶烟酰胺结合位点的贡献及其动力学
2. Amino Acid residues in the nicotinamide binding site contribute to catalysis by horse liver alcohol dehydrogenase(,). [J] . Rubach JK, Plapp BV Biochemistry . 2003,第10期

机译：烟酰胺结合位点中的氨基酸残基有助于马肝醇脱氢酶的催化作用。
3. Contribution of Global Dynamics to Catalysis by Horse Liver Alcohol Dehydrogenase [J] . Plapp Bryce, Shanmuganatham Karthik, Wallace Rachel, Protein Science: A Publication of the Protein Society . 2017,第Suppla1期

机译：全球动态对马肝脱氢酶催化的贡献
4. Investigating Catalysis-Linked Dynamics and Measuring Kinetic Isotope Effects in Yeast Alcohol Dehydrogenase Using Time-Resolved ESI-MS with H/D Exchange [C] . Peter Liuni, Derek J. Wilson American Society for Mass Spectrometry Conference on Mass Spectrometry and Allied Topics . 2013

机译：使用H / D兑MS调查酵母醇脱氢酶在酵母醇脱氢酶中测量动力学同位素效应
5. Dynamics of catalysis by liver alcohol dehydrogenase [D] . Rubach, Jon Kieran. 2002

机译：肝酒精脱氢酶催化动力学
6. Effects of Cavities at the Nicotinamide Binding Siteof Liver Alcohol Dehydrogenase on Structure Dynamics and Catalysis [O] . Atsushi Yahashiri, †, Jon K. Rubach, -1

机译：烟酰胺结合部位空洞的影响酒精脱氢酶对结构动力学和催化的影响
7. Substrate specificity and stereoselectivity of horse liver alcohol dehydrogenase. Kinetic evaluation of binding and activation parameters controlling the catalytic cycles of unbranched, acyclic secondary alcohols and ketones as substrates of the native and active-site-specific Co(II)-substituted enzyme [O] . Hans W. ADOLPH, Patrik MAURER, Helga SCHNEIDER-BERNLOHR, 1991

机译：马肝醇脱氢酶的底物特异性和立体选择性。控制非分支，无环次级醇和酮的催化循环的结合和活化参数的动力学评价为天然和有效位点特异性CO（II） - 取出的酶的基材

Contributions of Valine-292 in the Nicotinamide Binding Site of Liver Alcohol Dehydrogenase and Dynamics to Catalysis

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