Allosteric enzymes and their regulation
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This document discusses allosteric enzymes and their regulation. Allosteric enzymes have additional sites called allosteric sites that regulate enzyme activity. Enzyme activity can be activated or inhibited by metabolites interacting with these allosteric sites, known as allosteric regulation. There are two main models that explain allosteric regulation: the concerted model and sequential model. Allosteric regulation can be homotropic, where the substrate regulates the enzyme, or heterotropic, where a non-substrate regulatory molecule activates or inhibits the enzyme. Examples of each type of allosteric regulation are given.
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The term allosteric has been introduced by the two Noble Laureates JACOB AND MONOD to denote an enzyme site different from the active site which non competitively bands molecule other than the substrate and may influence the enzyme activity.
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All cleave peptide bonds, by a similar mechanism of action. They differ in their specificity and regulation.
Serine proteases include:
the pancreatic proteases: trypsin, chymotrypsin and elastase,
various tissue/intracellular proteases such as leukocyte elastase
enzymes of the blood clotting cascade
some enzymes of complement system
Many serine proteases are synthesized as inactive precursors (zymogens) which are activated by proteolysis
Methods of enzyme isolation and purification
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Enzymes.pptx
Enzymes are proteins that act as biological catalysts, regulating the rate of chemical reactions in living organisms. They accelerate reactions by lowering the activation energy without being consumed in the process. Enzymes are highly specific and each enzyme catalyzes only one type of reaction. They are affected by factors like temperature, pH, and substrate concentration. The active site of the enzyme binds specifically to substrates and catalyzes the conversion of substrates to products. Enzymes play essential roles in processes like digestion, cellular metabolism, and protection against pathogens.
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Enzymes are protein catalysts that accelerate chemical reactions in living organisms. They facilitate reactions by lowering the activation energy needed. Enzymes achieve specificity through their active sites, which are complementary in shape and chemical properties to their substrates. Factors like temperature, pH, and inhibitors can impact an enzyme's activity. There are several mechanisms of enzyme action and regulation, including competitive and non-competitive inhibition, as well as allosteric regulation through effectors binding at distinct sites. Precise control of enzymes is crucial for metabolic processes in cells and organisms.
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This document discusses various ways that enzyme activity can be regulated. It describes how enzyme levels and activity can be increased or decreased through different mechanisms, including substrate availability, product accumulation, allosteric effectors, covalent modification, genetic controls, zymogens, isozymes, and modulator proteins. A key example discussed is allosteric regulation, where binding of an allosteric effector at a site other than the active site can increase or decrease an enzyme's catalytic efficiency. Phosphorylation is provided as a common example of covalent regulation, where the addition of phosphate groups can alter an enzyme's activity.
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This document discusses allosteric enzymes, which have an additional regulatory site besides the active site. Allosteric enzymes are often oligomeric and have quaternary structure. The binding of effectors like allosteric inhibitors or activators at the regulatory site causes a conformational change that increases or decreases the enzyme's activity. Key metabolic enzymes are often regulated allosterically, allowing feedback inhibition that efficiently controls biochemical pathways. Examples of allosterically regulated enzymes include aspartate transcarbamylase and HMG-CoA reductase.
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Allosteric enzymes and their regulation
- 2. CONTENTS Introduction Allosteric regulation Models of allosteric regulation Sigmoid curve of allosteric regulation Types of allosteric regulation Allosteric inhibition
- 3. INTRODUCTION Enzymes: biocatalysts synthesized by living cells, protein in nature ,colloidal,thermolabile in character and specific in their action .they are known as catalyst of life which accelerates the rate of reaction Allosteric enzymes: enzymes which possess additional sites known as allosteric sites besides active site are known as allosteric enzymes the allosteric sites are unique places on enzyme molecules and allosteric enzymes can have one or more allosteric sites
- 4. ALLOSTERIC REGULATION Enzyme activity can be activated or inhibited through non covalent interaction of enzyme with metabolites other than substrates this form of control is termed as allosteric regulation. Allosteric proteins contain distinct regulatory sites and multiple functional sites
- 5. MODELS OF ALLOSTERIC REGULATION Two main models have been proposed to explain enzyme allostery Concerted model Sequential model
- 9. TYPES OF ALLOSTERIC REGULATION Homotropic Heterotropic
- 10. HOMOTROPIC A homotropic allosteric modulator is a substrate for its target enzyme as well as the regulatory molecule of the enzyme’s activity.it is typically an activator of enzyme For example: O2 is a homotropc modulator of haemoglobin
- 11. HETEROTROPIC A heterotropic allosteric modulator is a regulatory molecule that is not enzyme’s substrate it may be either an activator or inhibitor of enzyme For example:H+,CO2 are heterotropic allosteric modulators of enzyme
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