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the binding of a compound to an enzyme is observed to slow down or stop the rate of the reaction catalyzed by the enzyme. increasing the substrate concentration reduces the inhibitory effects of this compound. which of the following could account for this observation? the compound forms a covalent bond with one of the amino acid residues needed for enzyme activity is a competitive inhibitor is a negative allosteric regulator reduces disulfide bonds, causing the enzyme molecules to partially unfold

Respuesta :

In the particular case given in the question, the compound is a competitive inhibitor.

Describes enzyme-substrate reactions.

Enzymes are biocatalysts. Like other catalysts, it can lower the activation energy and drive the reaction in the desired direction. Because their activity depends on protein folding, they are usually sensitive to the temperature, pH, and salt concentration of the environment in which they work. The substrate enters the active site of the enzyme to form the enzyme-substrate complex. A reaction then takes place, converting the substrate to a product and forming an enzyme-product complex. Now the product is  released from the active site of the enzyme.

First, an increase in substrate concentration leads to an increase in the rate of enzyme-catalyzed reactions. This rate increase plateaus when the enzyme molecules become saturated with substrate. The rate of enzyme-catalyzed reactions increases with increasing concentrations of the enzyme.

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