The lock and key model of substrate binding and enzymatic catalysis explains: Wh
ID: 67656 • Letter: T
Question
The lock and key model of substrate binding and enzymatic catalysis explains: Which of the following statements about inhibitors of enzyme-catalyzed reactions is TRUE? Which of the following amino acid residues are often involved in proton transfers in enzyme-catalyzed reactions? Write 'T' if the statement is true and 'F' if the statement is false. Almost all irreversible enzyme inhibitors bind noncovalently to the enzyme. Coenzymes or cofactors are irreversibly changed during catalysis. Non-catalyzed biochemical reactions always occur at physiological useful timescales. Feedback regulation of a metabolic pathway can either be activation or inhibition. Catalysis affect the thermodynamics of a chemical reaction. A mutation causing an amino acid change in an enzyme that affects the turnover number k_cat will always affect the K_M a well, Electrostatic catalysis proceeds via covalent bonding interactions. A Lineweaver-Burk plot can be used to determine K_M using initial-rate data for an enzyme-catalyzed reaction. Covalent modification can either activate inhibit enzymes.Explanation / Answer
7). The lock and key model of substrate binding and enzymatic catalysis explain
A. Substrate specificity
Lock and key model of enzyme catalysis hypothesizes that the substrate possesses specific geometrical shape that exactly fits into the groove of enzyme. This theory does not include the structural changes that occur after substrate binding, and also fails to explain transition states.
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