Related Experiment Video

Updated: Aug 14, 2026

Defining Substrate Specificities for Lipase and Phospholipase Candidates
08:59

Defining Substrate Specificities for Lipase and Phospholipase Candidates

Published on: November 23, 2016

Substrate specificity and modifications of the active centre of elastase-like neutral proteinases from horse blood

A Koj, J Chudzik, A Dubin

    The Biochemical Journal
    |February 1, 1976
    PubMed

    More Related Videos

    The Determination of Protease Specificity in Mouse Tissue Extracts by MALDI-TOF Mass Spectrometry: Manipulating PH to Cause Specificity Changes09:47

    The Determination of Protease Specificity in Mouse Tissue Extracts by MALDI-TOF Mass Spectrometry: Manipulating PH to Cause Specificity Changes

    Published on: May 25, 2018

    Quantifying the Modulation of Elastase Enzyme Activity Through Colorimetric Analysis04:30

    Quantifying the Modulation of Elastase Enzyme Activity Through Colorimetric Analysis

    Published on: January 17, 2025

    Related Concept Videos

    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...
    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...
    Ligand Binding and Linkage00:49

    Ligand Binding and Linkage

    Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence 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...
    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...
    Allosteric Proteins-ATCase01:19

    Allosteric Proteins-ATCase

    Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
    Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...