Which Statement About The Binding Of Enzymes And Substrates Is Correct?

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Which of the following statements about the combustion of glucose with oxygen to form water and carbon dioxide C6H12O6 6 O2 6 CO2 6 H2O is correct. The Þrst step is the binding of substrate to the enzyme which occurs because of highly speciÞc interactions between the substrate and the side chains and backbone groups of the amino acids making up the active site.

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Competitive inhibition occurs when the substrate and the inhibitor compete for the same active site on the enzyme.

Which statement about the binding of enzymes and substrates is correct?. B resembles the active site of general acid-base enzymes. As the enzyme and substrate come together their interaction causes a mild shift in the enzymes structure that confirms an ideal binding arrangement between the enzyme and the substrate. Decrease off rate for enzyme substrate binding.

The inhibition is thus due to substrate analogue. C is complementary to a specific ligand. The process by which a substrate adopts the correct binding conformation before entering an active site.

Which statements about the two different models proposed to explain enzyme specificity is CORRECT. What isare the effects of a molecule binding to an allosteric site on an enzyme. Which of the following statements is false with respect to an enzymes ability to catalyse a reaction.

D contains amino acids without sidechains. When substrate molecules bind to the active site of the enzyme the enzyme undergoes a slight change in shape. A Substrate molecules bind to the active site of the enzyme only by weak bonds such as hydrogen bonds or hydrophobic attraction.

Substrate molecules fit into the active site of an enzyme like a key fits into a lock. Substrate molecules bind to the active site of the enzyme only by weak bonds such as hydrogen bonds or hydrophobic attraction. Two important models have been developed to describe the binding process.

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Which statement about the binding of enzymes and substrates is correct. In synthetic and organic chemistry the substrate is the chemical of interest that. B When substrate molecules bind to the active site of the enzyme the enzyme undergoes a slight change in shape.

E None of the above are correct. B The enzyme undergoes a covalent modification when bound to substrate in the Lock and Key Model. The substrate has a specific binding-site.

Which statement about the binding of enzymes and substrates is correct. The enzyme now cannot act upon the substrate and reaction products are not formed. C resembles the transition-state structure of the normal enzyme-substrate complex.

The organic molecule concerned is required. The substrate binding-site on the enzyme is a mirror image of the substrate. The binding of two substrates in the active site provides the correct orientation for them to react to form a product.

The rate of the reactions that are catalyzed by the enzymes would double. Some enzymes covalently bind a non-protein organic molecule to the active site. A is less stable when binding to an enzyme than the normal substrate.

Which of the following statements are correct about noncompetitive inhibitors. Competitive inhibition occurs when a substrate competes with an enzyme for binding to an inhibitor protein. A The substrate changes shape when enzyme binds in the Lock and Key Model.

Which statement about the binding of enzymes and substrates is correct. Which one of the following statements about the induced-fit model for the binding of a substrate to an enzyme is NOT correct. They prevent the substrate from binding to the enzyme They bind to a site other than the active site of the enzyme They cause the enzyme to change shape.

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When substrate molecules bind to the active site of the enzyme the enzyme undergoes a slight change in shape. C Substrate molecules fit into the active site of an enzyme like a key fits into a lock. The active site can provide heat from the environment that raises the energy content of the substrate.

The enzyme binds a cofactor that interacts with the substrate to facilitate the reaction. Substrate molecules fit into the active site of an enzyme like a key fits into a lock. The active site of the enzyme can provide a microenvironment with a different pH that facilitates the reaction.

A competitive inhibitor is usually chemically similar to the normal substrate and therefore fits into the active site of an enzyme and binds with it. When substrate molecules bind to the active site of the enzyme the enzyme undergoes a slight change in shape. The active site of an enzyme differs from an antibody-antigen binding site in that the enzyme active site.

D stabilizes the transition state for the normal enzyme-substrate complex. In chemistry a substrate is typically the chemical species being observed in a chemical reaction which reacts with a reagent to generate a productIt can also refer to a surface on which other chemical reactions are performed or play a supporting role in a variety of spectroscopic and microscopic techniques. Substrate molecules fit into the active site of an enzyme like a key fits into a lock.

Which of the following statements about different types of enzyme inhibition are correct. Hence action of an enzyme may be reduced or inhibited. The binding of two substrates in the active site provides the correct orientation for them to react to form a product.

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This dynamic binding maximizes the enzymes ability to catalyze its reaction. B catalyzes a chemical reaction. When substrate molecules bind to the active site of the enzyme the enzyme undergoes a slight change in shape.

The binding of substrate to enzyme induces a conformational change in the enzyme. A contains modified amino acids.

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