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    Enzymology Syllabus

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    Kamlesh Sahu
    This document outlines the syllabus for an enzymology course. It introduces key enzymology concepts like holoezymes, cofactors, and enzyme specificity. It discusses different enzyme catalysis mechanisms and examples like chymotrypsin and ribonuclease. The syllabus covers enzyme kinetics including the Michaelis-Menten equation and different types of inhibition. It also addresses methods to study enzyme structure and regulation through feedback, induction, repression and allosteric effects. The course appears to provide an overview of historical foundations, catalytic mechanisms, kinetics, inhibition studies and regulation of enzymatic reactions.

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    Enzymology Syllabus

    Uploaded by

    Kamlesh Sahu
    179 views1 page
    This document outlines the syllabus for an enzymology course. It introduces key enzymology concepts like holoezymes, cofactors, and enzyme specificity. It discusses different enzyme catalysis mechanisms and examples like chymotrypsin and ribonuclease. The syllabus covers enzyme kinetics including the Michaelis-Menten equation and different types of inhibition. It also addresses methods to study enzyme structure and regulation through feedback, induction, repression and allosteric effects. The course appears to provide an overview of historical foundations, catalytic mechanisms, kinetics, inhibition studies and regulation of enzymatic reactions.

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    Enzymology Syllabus

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    This document outlines the syllabus for an enzymology course. It introduces key enzymology concepts like holoezymes, cofactors, and enzyme specificity. It discusses different enzyme catalysis mechanisms and examples like chymotrypsin and ribonuclease. The syllabus covers enzyme kinetics including the Michaelis-Menten equation and different types of inhibition. It also addresses methods to study enzyme structure and regulation through feedback, induction, repression and allosteric effects. The course appears to provide an overview of historical foundations, catalytic mechanisms, kinetics, inhibition studies and regulation of enzymatic reactions.

    Copyright:

    © All Rights Reserved
    Download as DOCX, PDF, TXT or read online from Scribd
    Download as docx, pdf, or txt
    179 views1 page

    Enzymology Syllabus

    Uploaded by

    Kamlesh Sahu
    This document outlines the syllabus for an enzymology course. It introduces key enzymology concepts like holoezymes, cofactors, and enzyme specificity. It discusses different enzyme catalysis mechanisms and examples like chymotrypsin and ribonuclease. The syllabus covers enzyme kinetics including the Michaelis-Menten equation and different types of inhibition. It also addresses methods to study enzyme structure and regulation through feedback, induction, repression and allosteric effects. The course appears to provide an overview of historical foundations, catalytic mechanisms, kinetics, inhibition studies and regulation of enzymatic reactions.

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    © All Rights Reserved
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    Enzymology Syllabus

    Introduction: Historical perspectives; General characteristics; Nomenclature and classification;


    Introduction to the following terms with examples – Holoenzyme, apoenzyme, cofactors,
    coenzymes, prosthetic groups, metalloenzymes, turnover number, enzyme activity units (I.U and
    Katal), and specific activity. Multienzyme systems and multifunctional enzymes with specific
    examples and significance. Enzyme specificity: Types of specificity; three-point attachment theory to
    explain stereospecificity; Lock-and-key hypothesis; Induced- fit hypothesis; Hypothesis involving
    strain or transition-state stabilization. Enzyme Catalysis: Role of NAD+/NADP+, FMN/FAD, coenzyme
    A, thiamine pyrophosphate, pyridoxal phosphate, lipoic acid, biocytin, Vitamin B12 Coenzyme, and
    tetrahydrofolate coenzymes in enzyme catalysis; Common features of active sites; Reaction co-
    ordinate diagram; Proximity & orientation, acid-base catalysis, and covalent catalysis; Mechanism of
    action of chymotrypsin, ribonuclease, carboxypeptidase, and lysozyme

    Enzyme assay: Introduction; Kinetic and coupled enzyme assays. Enzyme Kinetics: Factors affecting
    enzyme activity; Arrhenius plot; Derivation of Michaelis-Menten equation for unisubstrate reactions;
    Km and its significance; Kcat/Km and its importance; Measurement of Km and Vmax by Lineweaver-
    Burk plot and other linear transformations of MM equation; Bi-substrate reactions: Sequential and
    ping-pong mechanisms with examples and determination of Km and Vmax for each substrate
    (derivations excluded); Use of initial velocity studies, product-inhibition studies and isotope
    exchange at equilibrium for determining the kinetic mechanism of a bisubstrate reaction.

    Methods of studying fast reactions: A brief account of rapid mixing techniques, flash photolysis and
    relaxation methods. Enzyme inhibition: Reversible (competitive, non- competitive, and
    uncompetitive) and irreversible (affinity labels and suicide inhibitors) enzyme inhibitors;
    Determination of Ki. Investigation of active site structure: Methods for identification of binding and
    catalytic sites- Trapping the enzyme-substrate complex, use of substrate analogues, chemical
    modification of amino acid side chains in enzymes, enzyme modification by proteases and effect of
    changing pH.

    Enzyme regulation: Coarse and fine control of enzyme activity; Enzyme induction & Repression;
    Feed back inhibition; Allosteric enzymes with aspartate transcarbamoylase as an example;
    Concerted and sequential models for action of allosteric enzymes; Negative and Positive
    Cooperativity; Hill plot; Scatchard plot; Regulation by reversible and irreversible covalent
    modification of enzymes; Isoenzymes. Ribozyme and Abzyme

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