MCQ on Enzyme Kinetics







Enzyme kinetics studies the speed of enzyme-catalyzed reactions. It explores factors influencing reaction rates: substrate concentration, enzyme activity, and temperature. Michaelis-Menten equation models this, defining Vmax (maximum rate) and Km (substrate concentration at half Vmax). Enzyme inhibitors also impact kinetics, crucial in understanding various biological processes and drug development. Please use this MCQ on Enzyme Kinetics to understand the concept.

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Enzymes are biological catalysts that:

The specific substance on which an enzyme acts is called:

The active site of an enzyme is:

Enzyme kinetics is the study of:

The maximum rate of an enzyme-catalyzed reaction is known as:

The Michaelis-Menten equation describes the relationship between:

The Km value in enzyme kinetics represents:

The turnover number (kcat) of an enzyme is defined as:

Which type of inhibition occurs when an inhibitor binds to the active site of an enzyme and competes with the substrate?

Non-competitive inhibition differs from competitive inhibition in that it:

The Lineweaver-Burk plot is a graphical representation of the Michaelis-Menten equation. What is the slope of this plot?

An enzyme-catalyzed reaction follows Michaelis-Menten kinetics. What happens to the reaction rate if the substrate concentration is much higher than Km?

Allosteric enzymes differ from Michaelis-Menten enzymes in that they:

The Hill coefficient (n) in enzyme kinetics measures:

A Lineweaver-Burk plot is linear with a slope of 0.1. What is the value of Km?

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