ENZYMOLOGY PT. 1

    Cards (85)

    • Apoenzyme is the protein part of the enzyme without the cofactor necessary for catalysis
    • Activator is an affecter molecule that increases the catalytic activity of an enzyme when it binds to a specific site
    • Inhibitor is a substance that diminishes the rate of a chemical reaction
    • Catalytic activity is the property of a catalyst that is measured by the catalyzed rate of conversion of a specified chemical reaction procured in a specified assay system
    • Coenzyme combines with apoenzymes to form compounds called holoenzyme
    • Enzyme is a protein that catalyzes chemical reactions without being destroyed, altered, and consumed.
    • Properties of enzyme
      1. Specific for substrate
      2. Normally confined within cells unless allowed to roam bloodstream
      3. Appear in serum after cellular injury and degradation of cell
    • Isoenzymes are a group of related enzymes catalyzing the same reaction but are different in structure, and physical, biochemical, and immunological properties.
    • International unit is the unit used in quantifying amount of enzyme needed in converting one micromole of substrate per minute.
    • Substrate is the reactant in a catalyzed reaction
    • Product is the substance produced by the enzyme-catalyzed conversion of a substrate
    • Active site is the specific portion of enzyme that binds on the substrate
    • An active site is a water free cavity
    • Allosteric site is the other cavity which may bind regulatory molecules
    • An allosteric site can either bind an activator molecule or an inhibitor molecule
    • In the Emil Fisher's Lock and Key theory of enzymes, enzymes have rigid active sites that means one kind of substrate can only fit an enzyme
    • In Kochland's Induced Fit Theory it states that an enzyme has a flexible active site and changes based on the substrate that is to bind to it.
    • Enzymes catalyze the chemical reaction by lowering the activation energy of the reaction.
    • Activation energy is the minimum energy needed to start a reaction and convert the substrate into products.
    • Transition state is the molecular intermidiate between substrate and its product thru which the reaction passes.
    • The movement of energy in chemical reactions is downward or downhill. High energy reactants going to the lower energy of the product.
    • Absolute specificity is when an enzyme combines only with one substrate and catalyzes only one reaction.
    • Group specificity is when an enzyme can bind to all substrate within a chemical group
    • Bond specificity is when an enzyme will only bind to a substrate that has a specific chemical bond present within its structure.
    • Stereoisomers are enzymes that bonds with substrates that have the same formula but differ in the orientation of molecules
    • Michaelis Menten Kinetics states that the rate of enzyme-catalyzed reaction is proportional to the concentration of the substrate.
    • According to the Michaelis Menten Kinetics, If the reaction has reached its maximum velocity there will no longer be any further reaction to occur.
    • Formula for Michaelis Menten Kinetics
      v=v=\frac{V_\text{max }[{S}]}{K_{{M}}+[{S}]}
    • The value of Km represents the substrate concentration required for half of the maximal velocity (Vmax) of an enzymatic reaction.
    • The value of Vmax represents the maximum possible rate at which an enzyme catalyzes a reaction under given conditions.
    • The Zero Order Reaction is when the rate of a reaction is independent of the concentration of the reactants. It Depends on the concentration of the Enzymes present to react.
    • First-order reaction is where the rate of reaction is directly proportional to the substrate concentration. This means the more substrate, the faster the reaction.
    • Second-Order Reactions are reactions that depend on two reacting species. The rate of this type of reaction depends on both concentrations of the reactant molecules. The reaction quadruples in rate
    • Oxidoreductases are enzymes that catalyze the transfer of electrons from one molecule to another. Typically from an oxidant to a reductant.
    • Oxidoreductases usually requires cofactors such as NADPH, FAD, or NADP
    • Hydroxylases add hydroxyl groups to a substrate.
    • Oxidases are enzymes where the oxygen molecule is the hydrogen or electron acceptor.
    • Peroxidases are enzymes that catalyzes reduction of hydrogen peroxide and organic hydroperoxides
    • Reductase enzymes catalyzes reduction reactions
    • Oxygenases are enzymes that catalyzes incorporation of intramolecular oxygen into organic substrates
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