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Enzymes and Catalysis

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30 Questions

What is the primary function of an enzyme?

To increase the rate of a chemical reaction

What is the characteristic of enzyme-substrate binding according to the induced fit model?

The substrate induces a change in the enzyme's conformation

What is the purpose of the active site in an enzyme-catalyzed reaction?

To bind to the substrate by noncovalent interactions

Why is the lock-and-key model less likely to be an effective catalyst?

The ES complex may be too stable, reducing the thermodynamic benefit

What is the term for the energy required to reach the transition state from the ground state of the reactants?

Activation energy

What is the characteristic of enzyme-catalyzed reactions?

They are 103-1020 times faster than uncatalyzed reactions

What is the primary function of the transition state?

To represent an unstable arrangement of atoms in which chemical bonds are being formed or broken

What is the advantage of inducing a fit in the induced fit model?

It reduces the distance to the transition state

What is the characteristic of most enzymes?

They are proteins

What is the term for the reactant in an enzyme-catalyzed reaction?

Substrate

What is the characteristic of competitive inhibition?

Km increases

What is the effect of uncompetitive inhibition on Vmax?

Decreases

What is the characteristic of non-competitive inhibition?

Vmax decreases, Km remains the same

What is the effect of adding more substrate in competitive inhibition?

Overcomes the inhibition

What type of inhibition occurs when the inhibitor binds only to the ES complex?

Uncompetitive

What is the effect of non-competitive inhibition on Km?

Remains the same

What is the characteristic of irreversible inhibition?

Forms a stable covalent bond with the enzyme

What is the effect of uncompetitive inhibition on the ES complex?

Decreases the formation of ES

What is the result of irreversible inhibition of acetylcholinesterase (AChE)?

Death by paralysis

What is the difference between reversible and irreversible inhibition?

Reversible inhibition can be overcome by adding more substrate, while irreversible inhibition cannot

What is the primary purpose of studying Enzyme Kinetics?

To understand various properties of enzymes such as substrate specificity and affinity

What is the unit of measurement for Turnover Number (Kcat)?

sec-1

What does a small KM value indicate?

The enzyme requires only a small amount of substrate to become saturated

What is the purpose of Lineweaver-Burk plots?

To accurately determine Vmax and KM from experimental data

What is the result of excessive heat on enzyme function?

Enzyme becomes completely nonfunctional

What type of inhibitor binds to the active site of E, competing with S?

Competitive inhibitor

What is the definition of Vmax?

The maximum reaction rate reached when the enzyme is completely saturated with substrate

What is the significance of Km in enzyme kinetics?

It gives us information on enzyme affinity for the substrate

What is the definition of catalytic efficiency?

The ratio of Kcat to Km

What is the effect of pH on enzyme function?

Enzymes work best within a particular range of pH

Test your knowledge of enzymes, biological molecules that catalyze chemical reactions, and their properties, including stereospecificity and activation energy. Learn about the role of proteins and RNA in enzymatic activity.

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