Scribd Logo
Upload

Welcome to Scribd!

  • 295 views

    Allosteric Enzyme

    Uploaded by

    Ahmed Imran
    Allosteric enzymes have additional sites called allosteric sites that are distinct from the active site. Effectors that bind to these allosteric sites can positively or negatively influence the enzyme's activity. There are two main models that describe allosteric regulation: the concerted model where the enzyme exists in tense and relaxed states, and the sequential model which accounts for different protein conformations. Allosteric enzymes exhibit sigmoidal kinetics curves rather than standard michaelis-menten hyperbolic curves.

    Copyright:

    © All Rights Reserved
    Download as PPTX, PDF, TXT or read online from Scribd

    Allosteric Enzyme

    Uploaded by

    Ahmed Imran
    295 views22 pages
    Allosteric enzymes have additional sites called allosteric sites that are distinct from the active site. Effectors that bind to these allosteric sites can positively or negatively influence the enzyme's activity. There are two main models that describe allosteric regulation: the concerted model where the enzyme exists in tense and relaxed states, and the sequential model which accounts for different protein conformations. Allosteric enzymes exhibit sigmoidal kinetics curves rather than standard michaelis-menten hyperbolic curves.

    Original Description:

    enzyme

    Copyright

    © © All Rights Reserved

    Available Formats

    PPTX, PDF, TXT or read online from Scribd

    Did you find this document useful?

    Is this content inappropriate?

    Allosteric enzymes have additional sites called allosteric sites that are distinct from the active site. Effectors that bind to these allosteric sites can positively or negatively influence the enzyme's activity. There are two main models that describe allosteric regulation: the concerted model where the enzyme exists in tense and relaxed states, and the sequential model which accounts for different protein conformations. Allosteric enzymes exhibit sigmoidal kinetics curves rather than standard michaelis-menten hyperbolic curves.

    Copyright:

    © All Rights Reserved
    Download as PPTX, PDF, TXT or read online from Scribd
    Download as pptx, pdf, or txt
    295 views22 pages

    Allosteric Enzyme

    Uploaded by

    Ahmed Imran
    Allosteric enzymes have additional sites called allosteric sites that are distinct from the active site. Effectors that bind to these allosteric sites can positively or negatively influence the enzyme's activity. There are two main models that describe allosteric regulation: the concerted model where the enzyme exists in tense and relaxed states, and the sequential model which accounts for different protein conformations. Allosteric enzymes exhibit sigmoidal kinetics curves rather than standard michaelis-menten hyperbolic curves.

    Copyright:

    © All Rights Reserved
    Download as PPTX, PDF, TXT or read online from Scribd
    Download as pptx, pdf, or txt
    of 22

    ALLOSTERIC ENZYME

    Muhammad Wajid
    Allosteric Enzyme:

     Some of the enzyme possess additional sites, known as


    allosteric sites (Greek; allo-other) besides the active
    sites

     Such enzyme are known as allosteric enzyme

     The allosteric sites are unique places on enzyme


    molecules

     Allosteric enzymes have one or more allosteric sites


    History:

     The term allosteric has been introduced by the two


    Noble laureates, Monod and Jacob, to denote an
    enzyme site, different from the active site

     These allosteric sites non-competitively binds molecule


    other than the substrate and may influence the
    enzyme activity
    Properties of enzyme:

     Allosteric enzyme have one or more allosteric sites

     Allosteric sites are binding sites distinct from an


    enzyme active site or substrate binding site

     Effector may be positive or negative, this effector


    regulate the enzyme activity

     The enzyme activity is increased when a positive


    allosteric effector binds at the allosteric site known as
    activator site
    Conti….
     Negative allosteric effector bind at the allosteric site
    called inhibitor site and inhibit the enzyme activity

     Binding to allosteric sites alter the activity of the


    enzyme, this is called cooperative binding

     Allosteric enzymes are also generally larger and


    more complex than simple enzymes

     Most of them have two or more polypeptide chains or


    subunits
    Model of allosteric regulation:

     Two main model have been proposed to describe the


    mechanistic basis of enzyme allostery

     Concerted model :

     Proposed by Monod, Wyman and Changeux .


     Sequential model:

     Proposed by Koshland, Nemethy and Allous


    Concerted model:
     According to the model used (concerted model) to
    study allosteric enzymes, they exists in two
    conformational states:
     T (tense) and R (relaxed) state

     Allosteric activator favour ‘R’ state of the enzyme


     Allosteric inhibitors favour ‘T’ state of the enzyme
     In the absence of the allosteric modulator an
    allosteric enzyme follows the hyperbolic kinetics R =
    Relax (active)
    Sequential model:

     Cooperativity by assuming that the enzyme/protein


    molecule affinity is relative and changes as substrates
    bind

     Unlike the concerted model, the sequential model


    accounts for different species of the protein molecule
    Sigmoid curve of allosteric enzyme:
    Allosteric Enzyme Kinetics: Sigmoid Curve instead of
    Hyperbola.

    Figure: Sigmoid Curve Of Allosteric Enzyme (Initial


    Reaction Rate Vs. Concentration Of Substrate)
    Allosteric modulator:

     There are two types of allosteric modulators

     Homotropic modulator

     Heterotropic Modulator
    Homotropic modulator:
     A homotropic allosteric modulator is a substrate for its
    target enzyme, as well as a regulatory molecule of
    the enzyme's activity

     It is typically an activator of the enzyme

     For example, O2 is a homotropic allosteric


    modulator of hemoglobin
    Heterotropic modulator:

     A heterotropic allosteric modulator is a regulatory


    molecule that is not also the enzyme's substrate
     It may be either an activator or an inhibitor of the
    enzyme
     For example, H +, CO2, and 2,3-
    bisphosphoglycerate are heterotropic allosteric
    modulators of hemoglobin
     2,3-BPG binds to an allosteric site on hemoglobin,
    the affinity for oxygen of all subunits decreases
    Enzyme Specificity:

     Enzymes are highly specific in nature, interacting with


    one or few substrates and catalyzing only one type
    of chemical reaction

     Substrate specificity is due to complete fitting of


    active site and substrate

     Example: Oxido-reductase do not catalyze hydrolysis


    reactions and hydrolase do not catalyze reaction
    involving oxidation and reduction
    Types of Enzyme Specificity:

     Bond Specificity

     Group Specificity

     Substrate Specificity

     Optical/Stereo Specificity

     Dual Specificity
    Bond Specificity:

     In this type, enzyme acts on substrates that are similar


    in structure and contain the same type of bond

     Example : Amylase which acts on α-1-4 glycosidic,


    bond in starch, dextrin and glycogen, shows bond
    specificity

     Lipase hydrolyze the ester bonds in different


    triglycerides
    Group Specificity:

     In this type of specificity, the enzyme is specific not


    only to the type of bond but also to the structure
    surrounding it
     Example: Pepsin is an endopeptidases enzyme, that
    hydrolyzes central peptide bonds in which the amino
    group belongs to aromatic amino acids e.g. phenyl
    alanine, tyrosine and tryptophan
     Trypsin is an endopeptidases enzyme, that hydrolyzes
    central peptide bonds in which the amino group
    belongs to basic amino acids e.g. arginine, lysine and
    Histidine
    Conti…

     Chymotrypsin is an endopeptidases enzyme, that


    hydrolyzes central peptide bonds in which the
    carboxyl group belongs to aromatic amino acids
     Amino peptidase is an exopeptidases that hydrolyzes
    peripheral peptide bond at amino terminal (end) of
    the polypeptide chain
     Carboxy peptidase is an exopeptidases that
    hydrolyzes peripheral peptide bond at carboxyl
    terminal (end) of the polypeptide chain
    Substrate Specificity:

     In this type of specificity, the enzymes acts only on


    one substrate
     Example : Uricase ,which acts only on uric acid, shows
    substrate specificity
     Maltase , which acts only on maltose, shows substrate
    specificity
     Sucrase, which acts only on sucrose
     Arginase, which acts only on arginine
    Types of substrate specificity:

     There are two types of substrate specificity

     Absolute specificity

     Relative specificity

     Absolute specificity is comparatively rare such as


    urease which catalyses hydrolysis of urea
    Optical/Stereo-specificity:

     In this type of specificity , the enzyme is not specific to


    substrate but also to its optical configuration
     Example: D amino acid oxidase acts only on D amino
    acids
     L amino acid oxidase acts only on L amino acids
     α- glycosidase which acts only on α- glycosidic bond,
    which is present in starch, glycogen, and dextrin
     ß- glycosidase which acts only on β- glycosidic bond,
    which is present in cellulose
    Dual Specificity:

     The enzyme may act on two substrates by one


    reaction type

     Example: Xanthine oxidase enzyme acts on xanthine


    and hypoxanthine (two substrates) by oxidation (one
    reaction type)

    You might also like