nhibitor always binds to the allosteric site of an enzyme
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Solved in 2 steps
- true or false 1. Conformational changes happen in an enzyme when the substrate binds to the active site. 2. Covalent bond stabilizes the binding of the substrate and the active site.the amino acid glutamic acid is at the active site of an enzyme. Normally the enzyme is active at pH 7. at pH 4 (higher concentration of H+), the enzyme is inactive. Explain there observationsAn enzyme won't function if the active site is the incorrect shape. What part of the amino acid has the most effect on the shape of the enzyme? O R group O carboxyl group O amine group O the peptide bonds
- You are observing an enzyme driven reaction. To the reaction mixture you add a chemical X which inhibits the reaction. If you add more substrate, the reaction rate approaches the Vmax of the uninhibited reaction. Furthermore, the structure of X is similar to the natural substrate. What kind of inhibitor is X?Assume that an inhibitor (I) can bind to an enzyme and is modified by the enzyme. The modified inhibitor (I*) is then permanently associated with the active site of the enzyme, thus inhibiting the enzyme activity. Such inhibitors are called: Suicide substrates Transition-state analogs Both A and B Neither A nor Bwhich answer choice is correct im confused... thxSubstrates bind to an enzymes site
- Allosteric enzymes allow the rate of reactions to control the activity. For example, the production of Product (P) can stop or limit the activity of enzyme 1 via _____________________________.The formation of a peptide bond between two amino acids is an example of a(n) _____ reaction.How does the structure of an enzyme affect its function in a cell? this should be an original thought, not Google’s. 3-4 sentences
- A transition-state analog— resembles the active site of general acid-base enzymes. is less stable when binding to an enzyme than the normal substrate. stabilizes the transition state for the normal enzyme-substrate complex. reacts more rapidly with an enzyme than the normal transition state intermediate. resembles the transition-state structure of the normal substrate in the enzyme-substrate complex.Which amino acid is NOT one that may be targeted for phosphorylation to modulate the activity of an enzyme? A) Ser B) Thr C) Tyr D) His E) AlaA competitive inhibitor binds to the - active site of theenzyme - a substrate -N termininus of the enzyme -more than one of these