Jove
Visualize
お問い合わせ
JoVE
x logofacebook logolinkedin logoyoutube logo
JoVEについて
概要リーダーシップブログJoVEヘルプセンター
著者向け
出版プロセス編集委員会範囲と方針査読よくある質問投稿
図書館員向け
推薦の声購読アクセスリソース図書館諮問委員会よくある質問
研究
JoVE JournalMethods CollectionsJoVE Encyclopedia of Experimentsアーカイブ
教育
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab Manual教員リソースセンター教員サイト
利用規約
プライバシーポリシー
ポリシー

関連する概念動画

Induced-fit Model01:13

Induced-fit Model

Most chemical reactions in cells require enzymes—biological catalysts that speed up the reaction without being consumed or permanently changed. They reduce the activation energy needed to convert the reactants into products. Enzymes are proteins, that usually work by binding to a substrate—a reactant molecule that they act upon.
Enzymes exhibit substrate specificity, meaning that they can only bind to certain substrates. This is mainly determined by the shape and chemical characteristics of...
Catalysis02:50

Catalysis

The presence of a catalyst affects the rate of a chemical reaction. A catalyst is a substance that can increase the reaction rate without being consumed during the process. A basic comprehension of a catalysts’ role during chemical reactions can be understood from the concept of reaction mechanisms and energy diagrams.
Enzymes02:34

Enzymes

Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
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...
Catalysis01:27

Catalysis

Catalysis influences the rate of chemical reactions by providing an alternative reaction pathway with lower activation energy. A catalyst speeds up a reaction, but it is not consumed during the process. The fundamental principle of catalysis is the ability of a catalyst to alter the reaction mechanism, often introducing a more efficient pathway than the uncatalyzed process.In a catalyzed reaction, the catalyst participates directly in the reaction mechanism. It interacts with reactants to form...

こちらも読む

関連記事

共著者、ジャーナル、引用グラフによってこの研究に関連する記事。

並び替え
Same author

Protein-Solvent Interface Controls Proton-Coupled Reactivity in Cryptochrome 4a.

Journal of the American Chemical Society·2026
Same author

Extended Lagrangian molecular dynamics on vibronic surfaces in the nuclear-electronic orbital framework.

The Journal of chemical physics·2026
Same author

General Expression for Vibronic Coupling in Proton-Coupled Energy Transfer.

Journal of chemical theory and computation·2026
Same author

Capturing nuclear quantum effects in high-pressure superconducting hydrides and ice with nuclear-electronic orbital theory.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Proton-Coupled Electron and Energy Transfer in Molecular Triads.

Accounts of chemical research·2026
Same author

Nuclear-electronic orbital quasiclassical trajectory method for vibrational spectroscopy.

The Journal of chemical physics·2026

関連する実験動画

Updated: Jul 7, 2026

The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis
19:16

The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis

Published on: March 17, 2010

酵素触媒の視点

Stephen J Benkovic1, Sharon Hammes-Schiffer

  • 1Department of Chemistry, 152 Davey Laboratory, Pennsylvania State University, University Park, PA 16802, USA. sjb1@psu.edu

Science (New York, N.Y.)
|August 30, 2003
PubMed
まとめ

この研究は,酵素触媒の仮説を検証し,タンパク質の分子運動,特に二酸化葉酸還元酵素の動きが,触媒効率にどのように重要なかを強調しています. 保存された残留ネットワークは,酵素の構造と運動に影響を与え,進化とタンパク質工学に影響を与えます.

科学分野:

  • バイオケミストリー バイオケミストリー
  • 理論化学 理論化学について
  • 構造生物学 構造生物学とは

背景:

  • 酵素触媒は,生物学的プロセスにとって根本的なものです.
  • 酵素機構を説明するために,数多くの仮説が提案されています.
  • 酵素機能におけるタンパク質ダイナミクスの役割は,依然として活発な研究分野です.

研究 の 目的:

  • 酵素触媒の基礎的仮説を精査する.
  • タンパク質の分子運動が触媒特性に与える影響を調査する.
  • 酵素ダイナミクスの進化とエンジニアリングの影響を調査する.

主な方法:

  • 酵素触媒に関する生化学的および理論的視点の歴史的レビュー.
  • タンパク質内の分子運動の分析.
  • ディヒドロフォラート還元酵素を用いたケーススタディ.

主要な成果:

  • 酵素の触媒効率は,内部分子運動によって著しく影響を受けます.
  • 保存された残留物の結合ネットワークは,タンパク質の構造と動態を決定する.
  • ディヒドロフォラート還元酵素は,これらの結合ネットワークを実証するモデルとして機能します.

さらに関連する動画

Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization
11:16

Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization

Published on: July 11, 2012

Assaying Protein Kinase Activity with Radiolabeled ATP
08:05

Assaying Protein Kinase Activity with Radiolabeled ATP

Published on: May 26, 2017

関連する実験動画

Last Updated: Jul 7, 2026

The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis
19:16

The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis

Published on: March 17, 2010

Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization
11:16

Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization

Published on: July 11, 2012

Assaying Protein Kinase Activity with Radiolabeled ATP
08:05

Assaying Protein Kinase Activity with Radiolabeled ATP

Published on: May 26, 2017

結論:

  • タンパク質の分子運動は酵素触媒の不可欠な部分です.
  • 保存された残留ネットワークは,酵素の進化と機能において重要な役割を果たします.
  • これらのネットワークを理解することは,高度なタンパク質工学の可能性を秘めています.