1) Isoenzymes are: a) Inactive forms of enzymes; b) multiple forms of the enzyme; c) multienzyme systems; d) enzyme precursors. 2) The speed of the enzymatic reaction depends on: a) enzyme concentration; b) molecular weight of the enzyme; c) molecular heterogeneity of the enzyme; d) molecular weight of the substrate. 3) Zymogen is: a) Enzyme poison b) Enzyme modulator c) Enzyme precursor d) Enzyme inhibitor 4) Non-competitive inhibition is the inhibition of an enzymatic reaction caused by the addition of an inhibitor: a) to the substrate; b) to the enzyme -substrate complex; c) to zymogen. d) there is no correct answer 8) The Michaelis-Menten equation. The Km for the Enzyme "A" for the substrate "B" was determined to be 500mu M. When the substrate "B"concentration was set to 180 juM, the initial rate of the reaction was found to be 45.0mu mol/(mLast s) What is Vmax for Enzyme "A" under these conditions?

Question

1) Isoenzymes are: a) Inactive forms of enzymes; b) multiple forms of the enzyme; c) multienzyme systems; d) enzyme precursors. 2) The speed of the enzymatic reaction depends on: a) enzyme concentration; b) molecular weight of the enzyme; c) molecular heterogeneity of the enzyme; d) molecular weight of the substrate. 3) Zymogen is: a) Enzyme poison b) Enzyme modulator c) Enzyme precursor d) Enzyme inhibitor 4) Non-competitive inhibition is the inhibition of an enzymatic reaction caused by the addition of an inhibitor: a) to the substrate; b) to the enzyme -substrate complex; c) to zymogen. d) there is no correct answer 8) The Michaelis-Menten equation. The Km for the Enzyme "A" for the substrate "B" was determined to be 500mu M. When the substrate "B"concentration was set to 180 juM, the initial rate of the reaction was found to be 45.0mu mol/(mLast s) What is Vmax for Enzyme "A" under these conditions?

Answer 1

1) Isoenzymes are:b) multiple forms of the enzyme.Isoenzymes, also known as isozymes, are different forms of the same enzyme that catalyze the same reaction but have different amino acid sequences and structural properties. They are produced by different genes and can have different kinetic properties, tissue distribution, and regulatory mechanisms.2) The speed of the enzymatic reaction depends on:a) enzyme concentration.The speed of an enzymatic reaction, also known as the reaction rate, is primarily determined by the concentration of the enzyme. The higher the enzyme concentration, the faster the reaction rate, as there are more active sites available for the substrate to bind to.3) Zymogen is:c) Enzyme precursor.A zymogen, also known as a proenzyme, is an inactive precursor of an enzyme that requires a specific activation step to become an active enzyme. This activation step often involves the cleavage of a peptide bond within the zymogen, resulting in the formation of the active enzyme.4) Non-competitive inhibition is the inhibition of an enzymatic reaction caused by the addition of an inhibitor:b) to the enzyme-substrate complex.In non-competitive inhibition, the inhibitor binds to an allosteric site on the enzyme, which is a site other than the active site. This binding causes a conformational change in the enzyme, reducing its activity. The inhibitor can bind to the enzyme-substrate complex, preventing the substrate from being converted into the product.8) To determine the Vmax for Enzyme "A" under the given conditions, we can use the Michaelis-Menten equation:V = (Vmax \* [S]) / (Km + [S])Where:V is the initial rate of the reaction,Vmax is the maximum reaction rate,[S] is the substrate concentration, andKm is the Michaelis constant.Given:V = 45.0 μmol/(mL\*s)[S] = 180 μMKm = 500 μMWe can rearrange the equation to solve for Vmax:Vmax = (V \* Km) / [S]Substituting the given values:Vmax = (45.0 μmol/(mL\*s) \* 500 μM) / 180 μMVmax = 125 μmol/(mL\*s)Therefore, the Vmax for Enzyme "A" under these conditions is 125 μmol/(mL\*s).

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