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Related Concept Videos

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 Enzymes01:22

Introduction to Enzymes

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 bind the substrates and convert them into products. Many enzymes also...
Introduction to Enzyme Kinetics01:19

Introduction to Enzyme Kinetics

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...
Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

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.
Turnover Number and Catalytic Efficiency01:19

Turnover Number and Catalytic Efficiency

The turnover number of an enzyme is the maximum number of substrate molecules it can transform per unit time. Turnover numbers for most enzymes range from 1 to 1000 molecules per second. Catalase has the known highest turnover number, capable of converting up to 2.8×106 molecules of hydrogen peroxide into water and oxygen per second. Lysozyme has the lowest known turnover number of half a molecule per second.
Chymotrypsin is a pancreatic enzyme that breaks down proteins during digestion. The...
Introduction To Enzymes01:22

Introduction To Enzymes

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 bind the substrates and convert them into products. Many enzymes also...

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Related Experiment Video

Updated: Jun 21, 2026

Multi-enzyme Screening Using a High-throughput Genetic Enzyme Screening System
08:10

Multi-enzyme Screening Using a High-throughput Genetic Enzyme Screening System

Published on: August 8, 2016

Reliability of elements and systems in enzymology.

S D Varfolomeev, I V Berezin

    Molekuliarnaia Biologiia
    |July 1, 1976
    PubMed
    Summary
    This summary is machine-generated.

    Reliability principles describe enzyme stability and aging. Exponential laws govern "all-or-nothing" inactivation, while normal laws apply to gradual breakdowns, offering quantitative stability criteria.

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    Measuring Enzymatic Stability by Isothermal Titration Calorimetry
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    Multi-enzyme Screening Using a High-throughput Genetic Enzyme Screening System
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    Benchtop Immobilized Metal Affinity Chromatography, Reconstitution and Assay of a Polyhistidine Tagged Metalloenzyme for the Undergraduate Laboratory
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    Benchtop Immobilized Metal Affinity Chromatography, Reconstitution and Assay of a Polyhistidine Tagged Metalloenzyme for the Undergraduate Laboratory

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    Measuring Enzymatic Stability by Isothermal Titration Calorimetry
    08:37

    Measuring Enzymatic Stability by Isothermal Titration Calorimetry

    Published on: March 26, 2019

    Area of Science:

    • Biochemistry
    • Enzymology
    • Biophysics

    Background:

    • Enzyme and polyenzyme system stability are crucial for biological processes.
    • Understanding aging and inactivation mechanisms is essential for predicting system longevity.
    • Reliability theory offers a framework for quantifying system stability.

    Purpose of the Study:

    • To apply reliability theory concepts to describe enzyme and polyenzyme system stability and aging.
    • To model inactivation processes using established reliability laws.
    • To propose quantitative criteria for assessing enzyme system stability.

    Main Methods:

    • Modeling enzyme inactivation using exponential reliability laws for "all-or-nothing" processes.
    • Modeling systems with gradual breakdowns and latent error accumulation using normal reliability laws.
    • Analyzing parallel and sequential enzyme systems to determine factors influencing mean operational time.

    Main Results:

    • Exponential reliability law accurately describes inactivation of individual enzymes and systems operating on an "all-or-nothing" principle.
    • In parallel enzyme systems, mean operation time is dictated by the most stable enzyme.
    • In sequential systems, mean operation time is limited by the most labile enzyme.
    • Normal reliability law characterizes systems aging via latent error accumulation and gradual breakdowns.
    • Combined exponential and normal reliability laws can describe complex systems.
    • Mean time for continuous functioning is proposed as a key quantitative stability criterion.

    Conclusions:

    • Reliability theory provides a robust framework for quantitatively assessing enzyme and polyenzyme system stability and aging.
    • Different inactivation mechanisms (all-or-nothing vs. gradual) necessitate distinct reliability models (exponential vs. normal).
    • The arrangement of enzymes (parallel vs. sequential) significantly impacts system stability and mean operational time.
    • Experimental validation using hydrogenase activity enzymes, isolated chloroplasts, and blue-green algae supports the theoretical models.