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Related Concept Videos

Enzyme Inhibition01:30

Enzyme Inhibition

93.3K
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.
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Enzymes02:34

Enzymes

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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...
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Enzyme Kinetics01:19

Enzyme Kinetics

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Enzymes speed up reactions by lowering the activation energy of the reactants. The speed at which the enzyme turns reactants into products is called the rate of reaction. Several factors impact the rate of reaction, including the number of available reactants. Enzyme kinetics is the study of how an enzyme changes the rate of a reaction.
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...
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Introduction to Enzyme Kinetics01:19

Introduction to Enzyme Kinetics

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Enzyme kinetics studies the rates of biochemical reactions. Scientists monitor the reaction rates for a particular enzymatic reaction at various substrate concentrations. Additional trials with inhibitors or other molecules that affect the reaction rate may also be performed.
The experimenter can then plot the initial reaction rate or velocity (Vo) of a given trial against the substrate concentration ([S]) to obtain a graph of the reaction properties. For many enzymatic reactions involving a...
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Introduction to Enzymes01:22

Introduction to Enzymes

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The use of enzymes by humans dates to 7000 BCE. Humans first used enzymes to ferment sugars and produce alcohol without knowing that this was an enzyme-catalyzed reaction. Wilhelm Kuhne coined the term 'enzyme' in 1877 from the Greek words ‘en’ meaning ‘in’ or ‘within’ and ‘zyme’ meaning ‘yeast.’
Most enzymes are proteins that speed up biochemical reactions without being consumed. Enzymes contain one or more active sites that...
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Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

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The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.
 
Most enzymes...
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Related Experiment Video

Updated: Feb 26, 2026

Measuring Lactase Enzymatic Activity in the Teaching Lab
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Measuring Lactase Enzymatic Activity in the Teaching Lab

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Practical problems in clinical enzymology.

J A Lott

    CRC Critical Reviews in Clinical Laboratory Sciences
    |December 1, 1977
    PubMed
    Summary
    This summary is machine-generated.

    Precise serum enzyme activity measurements require kinetic methods, ensuring readings are taken after the induction period and from the linear curve portion. Standardization of instruments and methods is crucial for accurate, comparable enzyme assays.

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    Area of Science:

    • Clinical Chemistry
    • Biochemistry
    • Enzymology

    Background:

    • Accurate determination of clinically significant serum enzyme activity is essential for diagnosis and monitoring.
    • Continuous monitoring (kinetic) methods offer precise enzyme activity measurements.
    • Current limitations include the lack of suitable enzyme standards and the need for careful method execution.

    Purpose of the Study:

    • To outline the critical parameters for precise serum enzyme activity determination using kinetic methods.
    • To highlight the importance of instrument standardization and calibration for accurate enzyme assays.
    • To discuss the role of emerging reference methods in improving interlaboratory comparability.

    Main Methods:

    • Utilizing continuous monitoring (kinetic) assays for serum enzyme activity.
    • Ensuring measurements are taken post-induction period and from the linear phase of the reaction curve.
    • Implementing instrument standardization and calibration using national standards for wavelength and absorbance accuracy.

    Main Results:

    • Precise enzyme activity determination is achievable with kinetic methods when specific procedural steps are followed.
    • Instrument standardization is paramount due to the current absence of reliable enzyme standards.
    • Emerging reference methods show promise for enhancing interlaboratory consistency.

    Conclusions:

    • Adherence to kinetic assay protocols, including proper timing and curve assessment, is vital for accurate serum enzyme activity.
    • Standardization of analytical instruments and methods is critical for reducing variability in enzyme assays.
    • The development and adoption of reference methods and enzyme standards will further improve the reliability and comparability of clinical enzyme measurements.