Related Experiment Video

Updated: Aug 12, 2026

Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions
13:00

Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions

Published on: April 4, 2014

A quenched-flow study of the reaction catalysed by creatine kinase

Y Engelborghs, A Marsh, H Gutfreund

    The Biochemical Journal
    |October 1, 1975
    PubMed

    More Related Videos

    Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes09:42

    Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

    Published on: January 16, 2016

    Quantification of Bacterial Histidine Kinase Autophosphorylation Using a Nitrocellulose Binding Assay09:17

    Quantification of Bacterial Histidine Kinase Autophosphorylation Using a Nitrocellulose Binding Assay

    Published on: January 11, 2017

    Related Concept Videos

    Enzyme Kinetics01:19

    Enzyme Kinetics

    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...
    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...
    Fast Reactions01:27

    Fast Reactions

    Fast reactions occurring in times shorter than the time needed to mix reactants pose a unique challenge for investigation. In a liquid-phase continuous-flow system, reactants A and B are swiftly pushed into the mixing chamber, where mixing occurs within 1 ms. The reaction mixture then flows through an observation tube, and one measures light absorption to determine species concentrations at various points of the tube. This method is most appropriate when relatively large volumes of reactants...