関連する実験動画

Updated: Aug 10, 2026

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity
14:27

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity

Published on: August 19, 2013

サブストラット安定化:ヒトの2つの酵素の遺伝子制御された相互関係

M L Greene, J A Boyle, J E Seegmiller

    Science (New York, N.Y.)
    |February 6, 1970
    PubMed
    まとめ

    5-フォスフォリボシル-1-ピロホスファートは,ヒポキサンチン・グアニン・フォスフォリボシルトランスフェラーゼが欠けている個体で蓄積します. この基板はアデニンフォスフォリボシルトランスフェラーゼを安定させ,これらの個体における酵素活性の増加を説明する可能性がある.

    さらに関連する動画

    Identification of Kinase-substrate Pairs Using High Throughput Screening11:13

    Identification of Kinase-substrate Pairs Using High Throughput Screening

    Published on: August 29, 2015

    Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins10:54

    Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins

    Published on: May 30, 2025

    関連する概念動画

    Allosteric Regulation01:08

    Allosteric Regulation

    Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
    Enzyme Inhibition01:30

    Enzyme Inhibition

    Inhibitors are molecules that reduce enzyme activity by binding to the enzyme. In a normally functioning cell, enzymes are regulated by a variety of inhibitors. Drugs and other toxins can also inhibit enzymes. Some inhibitors bind to the enzyme’s active site, while others inhibit enzymatic activity by binding to other sites on the protein structure.
    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...
    Allosteric Regulation01:08

    Allosteric Regulation

    Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
    Regulation of Metabolism01:19

    Regulation of Metabolism

    Cellular needs and conditions vary from cell to cell and change within individual cells over time. For example, the required enzymes and energetic demands of stomach cells are different from those of fat storage cells, skin cells, blood cells, and nerve cells. Furthermore, a digestive cell works much harder to process and break down nutrients during the time that closely follows a meal compared with many hours after a meal. As these cellular demands and conditions vary, so do the amounts and...
    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...