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    Prentice Hall c2002 1

    ENZYME

    1. Structure and properties

    2. Enzymes Classification

    3. Activities

    4. Enzyme Application

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    STRUCTURE AND PROPERTIES

    Enzyme = protein protein

    http://localhost/var/www/apps/conversion/tmp/scratch_1/protein.PPThttp://localhost/var/www/apps/conversion/tmp/scratch_1/protein.PPT
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    Hierarchical nature of protein

    structure stucture

    Primary structure(Amino acid sequence)

    Secondary structure -helix, -sheet

    Tertiary structure Three-dimensional structureformed by assembly of secondary structures

    Quaternary structure Structure formed by morethan one polypeptide chains

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    Catalyst- speeds up attainment of reaction

    equilibrium CATALYST

    Enzymatic reactions- 103to 1017faster than

    the corresponding uncatalyzed reactions

    Substrates- highly specific reactants forenzymes SPESIFICITY

    Properties of enzymes

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    Properties of enzymes (continued)

    Stereospecificity- many enzymes act upon

    only one stereoisomer of a substrate

    STEREOSPESIFICITY

    Reaction specificity - enzyme product yields

    are essentially 100% (there is no formation of

    wasteful byproducts)

    Active site- where enzyme reactions take place

    ACTIVE SITE

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    Enzyme Nomenclature and Classification

    Trivial named, based on existed ancient name;

    Examples: trypsin, pepsin, ptyalin, papain

    Systematic named, Based on the reaction theycatalyze, add suffix -ase. Examples: urease acts on

    urea, argininase on arginine, tyrosinase on tyrosine.

    International Commission on Enzymesnamed, Enzymes are classified into 6 classesbased on the kind of reaction they catalyze

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    The Six Classes of Enzymes

    1.Oxidoreductases(dehydrogenases)

    2.Transferases

    3. Hydrolases

    4. Lyases

    5. Isomerases

    6. Ligases (synthetases)

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    1.Oxidoreductases(dehydrogenases)

    Catalyze oxidation-reduction reactions

    EC 1.1.1.27

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    2.Transferases

    Catalyze group transfer reactions

    EC 2.6.1.2

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    3.Hydrolases

    Catalyze hydrolysis reactions where water is

    the acceptor of the transferred group

    EC 3.6.1.1

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    4. Lyases

    Catalyze lysis of a substrate, generating adouble bond in a nonhydrolytic, nonoxidative

    elimination (Synthasescatalyze the addition to

    a double bond, the reverse reaction of a lyase)

    EC 4.1.1.1

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    5. Isomerases

    Catalyze isomerization reactions

    EC 5.1.1.1

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    6. Ligases (synthetases)

    Catalyze ligation, or joining of two substrates

    Require chemical energy (e.g. ATP)

    EC 6.3.1.2

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