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    L-1 Enzymes

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    Liyakath Ali
    1) Enzymes are protein catalysts that accelerate chemical reactions by lowering their activation energy. They convert substrates into products through specific biochemical reactions without being used up in the process. 2) Enzymes have specific structures that allow them to bind to substrates. They are classified based on the type of reaction they catalyze according to the International Union of Biochemistry and Molecular Biology system. 3) Key properties of enzymes include being highly specific catalysts, having optimal temperatures for activity, and not being used up in the reactions they catalyze. They play essential roles in all metabolic processes by facilitating individual reaction steps.

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    L-1 Enzymes

    Uploaded by

    Liyakath Ali
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    1) Enzymes are protein catalysts that accelerate chemical reactions by lowering their activation energy. They convert substrates into products through specific biochemical reactions without being used up in the process. 2) Enzymes have specific structures that allow them to bind to substrates. They are classified based on the type of reaction they catalyze according to the International Union of Biochemistry and Molecular Biology system. 3) Key properties of enzymes include being highly specific catalysts, having optimal temperatures for activity, and not being used up in the reactions they catalyze. They play essential roles in all metabolic processes by facilitating individual reaction steps.

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    1) Enzymes are protein catalysts that accelerate chemical reactions by lowering their activation energy. They convert substrates into products through specific biochemical reactions without being used up in the process. 2) Enzymes have specific structures that allow them to bind to substrates. They are classified based on the type of reaction they catalyze according to the International Union of Biochemistry and Molecular Biology system. 3) Key properties of enzymes include being highly specific catalysts, having optimal temperatures for activity, and not being used up in the reactions they catalyze. They play essential roles in all metabolic processes by facilitating individual reaction steps.

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    2 views3 pages

    L-1 Enzymes

    Uploaded by

    Liyakath Ali
    1) Enzymes are protein catalysts that accelerate chemical reactions by lowering their activation energy. They convert substrates into products through specific biochemical reactions without being used up in the process. 2) Enzymes have specific structures that allow them to bind to substrates. They are classified based on the type of reaction they catalyze according to the International Union of Biochemistry and Molecular Biology system. 3) Key properties of enzymes include being highly specific catalysts, having optimal temperatures for activity, and not being used up in the reactions they catalyze. They play essential roles in all metabolic processes by facilitating individual reaction steps.

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    of 3

    MIND NURTURE KRISHANA Page 1 of 3

    ENZYMES
    ❖ Definition
    • Enzyme are proteins that act as biological catalysts by accelerating chemical reactions. The molecules
    upon which enzymes may act are called substrates, and the enzyme converts the substrates into
    different molecules known as products. Almost all metabolic processes in the cell need enzyme catalysis
    in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to
    catalyze individual steps.
    • The study of enzymes is called enzymology
    • The enzyme term was invented by W. Kuhne in 1878.
    ❖ Structure of enzyme

    ❖ Properties of enzyme
    i) Physically, enzymes act as colloids or as high-molecular-weight compounds.
    ii) At a temperature below the boiling point of the water, enzymes are killed or inactivated.
    iii) Most enzymes in the liquid medium are inactivated at 60 degrees Celsius.
    iv) Extracting dried enzymes can withstand temperatures of 100 degrees Celsius to 120 degrees Celsius or even higher.
    Enzymes are, therefore, thermos labile.
    v) The optimum activity of each enzyme is always at a particular temperature, which typically varies from 25 degrees
    Celsius to 45 degrees Celsius. At 37 degrees Celsius, enzyme action is strongest and as temperatures rise above 60
    degrees Celsius, enzymes become inactive.
    vi) Enzymes are complex macromolecules with high molecular weight.
    vii) They catalyze biochemical reactions in a cell. They help in the breakdown of large molecules into smaller molecules or
    bring together two smaller molecules to form a larger molecule.
    viii) Enzymes do not start a reaction. However, they help in accelerating it.
    ix) Enzymes affect the rate of biochemical reaction and not the direction. Most of the enzymes have a high turnover
    number. Turnover number of an enzyme is the number of molecules of a substance that is acted upon by an enzyme
    per minute. High turnover number of enzymes increases the efficiency of the reaction.
    x) Enzymes are specific in action.
    xi) Enzymatic activity decreases with increase in temperature.
    xii) They show maximum activity at an optimum pH of 6 – 8.
    xiii) The velocity of enzyme increases with an increase in substrate concentration and then, ultimately reaches maximum
    velocity.
    xiv) In nature, all enzymes are proteins, but all proteins may not be enzymes.
    xv) Enzymes remain unchanged after a reaction and therefore can work again.
    xvi) They lowers the activation energy required for a chemical reaction to proceed.

    ❖ IUB and MB Classification (IUBMB-International union of biochemistry and molecular biology)


    ➢ Trivial Names of Enzymes
    • The name of an enzyme: Usually ends in –ase. Identifies the reacting substance. For example, sucrase
    catalyzes the reaction of sucrose. Describes the function of the enzyme. For example, oxidases catalyze
    oxidation. Could be a common name, particularly for the digestion enzymes such as pepsin and trypsin.
    MIND NURTURE KRISHANA Page 2 of 3

    ➢ IUB Classification of Enzymes


    Enzymes are classified according to the reaction they catalyze.
    Class Reactions catalyzed
    i) Oxidoreductases Oxidation-reduction
    ii) Transferases Transfer groups of atoms
    iii) Hydrolases Hydrolysis
    iv) Lyases Add atoms/remove atoms to/from a double bond
    v) Isomerases Rearrange atoms
    vi) Ligases Use ATP to combine molecules

    ➢ Systematic Name
    • According to the International union Of Biochemistry an enzyme name has two parts: -First part is the
    name of the substrates for the enzyme. -Second part is the type of reaction catalyzed by the
    enzyme.This part ends with the suffix “ase”. Example: Lactate dehydrogenase
    ❖ EC number
    • Enzymes are classified into six different groups according to the reaction being catalyzed. The
    nomenclature was determined by the Enzyme Commission in 1961 (with the latest update having
    occurred in 1992), hence all enzymes are assigned an “EC” number. The classification does not take into
    account amino acid sequence (ie, homology), protein structure, or chemical mechanism.
    ➢ EC numbers
    • EC numbers are four digits, for example a.b.c.d, where “a” is the class, “b” is the subclass, “c” is the sub-
    subclass, and “d” is the sub-sub-subclass. The “b” and “c” digits describe the reaction, while the “d” digit is
    used to distinguish between different enzymes of the same function based on the actual substrate in the
    reaction. Example: for Alcohol:NAD+ oxidoreductase EC number is 1.1.1.1
    EC Tree
    1 Oxidoreductases
    1.1 Acting on the CH-OH group of donors
    1.1.1 With NAD+ or NADP+ as acceptor
    1.1.1.1 alcohol dehydrogenase
    ➢ The Six Classes
    EC 1. Oxidoreductases
    EC 2. Transferases
    EC 3. Hydrolases
    EC 4. Lyases
    EC 5. Isomerases
    EC 6. Ligases
    EC 1. Oxidoreductases
    • Catalyze the transfer of hydrogen or oxygen atoms or electrons from one substrate to another.
    • Since these are ‘redox’ reactions, an electron donor/acceptor is also required to complete the reaction.
    • AH2 +B → A+ BH2
    • Ex. Oxidases, Dehydrogenases, Reductases.

    EC 2. Transferases
    • Catalyze group transfer reactions, excluding oxidoreductases (which transfer hydrogen or oxygen and
    are EC 1).
    • These are of the general form: A-X + B ↔ BX + A
    • Ex: Transaminases (transfer amino group), Kinases (transfer Phosphate group)
    MIND NURTURE KRISHANA Page 3 of 3

    EC 3. Hydrolases
    • Catalyze hydrolytic reactions.
    • A-X + H2O ↔ X-OH + A-H
    • Ex: lipases, esterases, Amylases, peptidases/proteases, etc.
    EC 4. Lyases
    • Catalyze non-hydrolytic (covered in EC 3) removal of functional groups from substrates, often creating a
    double bond in the product; or the reverse reaction, ie, addition of function groups across a double
    bond.
    • A-X +B-Y → A=B + X-Y
    • Ex: Decarboxylases, Aldolases, Dehydrases, Deaminases, Synthases, etc.
    EC 5. Isomerases
    • Catalyzes isomerization reactions, including epimerizations and cis-trans isomerizations.
    • A →A’
    • Ex: Isomerases (Cis-Trans), Epimerases (D—L)
    EC 6. Ligases
    • Catalyzes the synthesis of various (mostly C-X) bonds, coupled with the breakdown of energy- containing
    substrates, usually ATP .
    • A+B+ ATP → A-B+ ADP+iP
    • Ex: Synthetases, Carboxylases

    ❖ Enzyme Specificity
    • The ability of an enzyme to select a specific substrate from a range of chemically similar compounds is known as
    specificity. Since the enzyme and substrate exhibit complementary structural and conformational properties,
    specificity is a molecular identification process. Different enzymes exhibit different levels of substrate specificity.
    • The specificity that enzymes show to the reactions they catalyse is one of the characteristics that makes them so
    useful as diagnostic and research tools. Only a selected few enzymes can catalyse a single reaction or they have
    perfect specificity.
    • There are usually four different categories of specificity:
    i) Absolute specificity – The enzyme catalyses only one reaction.
    ii) Group specificity – The enzyme acts only on molecules having specific functional groups, like phosphate,
    amino, and methyl groups.
    iii) Linkage specificity – The enzyme acts on a specific type of chemical bond regardless of the remaining
    molecular structure.
    iv) Stereochemical specificity – The enzyme acts on a certain optical or steric isomer.

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