Join thousands of students who trust us to help them ace their exams!Watch the first video
Multiple Choice
The image at right shows which of the following aspects of enzymatic catalysis?
A
The induced fit model of substrate binding
B
Covalent modification of the enzyme
C
Allosteric inhibition of enzyme activity
D
The Michaelis-Menten saturation curve
Verified step by step guidance
1
Understand the concept of enzymatic catalysis and the different models of substrate binding. The induced fit model suggests that the enzyme undergoes a conformational change upon substrate binding to better accommodate the substrate.
Review the concept of covalent modification of enzymes. This involves the enzyme being chemically modified, often through the addition or removal of functional groups, which can alter its activity.
Examine allosteric inhibition. This occurs when a molecule binds to a site other than the active site (an allosteric site) on the enzyme, causing a conformational change that reduces enzyme activity.
Understand the Michaelis-Menten saturation curve. This curve describes the relationship between substrate concentration and reaction velocity, showing how enzymes become saturated with substrate at high concentrations.
Analyze the image provided in the problem. Determine which of the described concepts (induced fit model, covalent modification, allosteric inhibition, or Michaelis-Menten curve) is best represented by the image based on the visual cues and characteristics depicted.