肝臓アルコールの脱水酸化酵素におけるヒドリド転送:量子力学,運動同位体効果,酵素運動の役割

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Updated: Jul 21, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

S R Billeter1, S P Webb, P K Agarwal

  • 1Department of Chemistry, 152 Davey Laboratory, Pennsylvania State University, University Park, Pennsylvania 16802, USA.

Journal of the American Chemical Society
|November 8, 2001
PubMed
まとめ

肝アルコール脱水素酶 (LADH) 量子ダイナミクスは,水素トンネリングが鍵であることを明らかにします. 酵素の動きは,VAL-203の相互作用と同様に,反応速度と酵素活性に大きな影響を与えます.

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Induced-fit Model01:13

Induced-fit Model

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Enzyme Inhibition

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Enzymes02:34

Enzymes

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Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes a mild...
Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes a mild...
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Transition State Theory

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