Clutch Prep is now a part of Pearson
Ch. 7 - Enzyme Inhibition and Regulation WorksheetSee all chapters

# Apparent Km and Vmax

See all sections
Sections
Enzyme Inhibition
Irreversible Inhibition
Reversible Inhibition
Inhibition Constant
Degree of Inhibition
Apparent Km and Vmax
Inhibition Effects on Reaction Rate
Competitive Inhibition
Uncompetitive Inhibition
Mixed Inhibition
Noncompetitive Inhibition
Recap of Reversible Inhibition
Allosteric Regulation
Allosteric Kinetics
Allosteric Enzyme Conformations
Allosteric Effectors
Concerted (MWC) Model
Sequential (KNF) Model
Negative Feedback
Positive Feedback
Post Translational Modification
Ubiquitination
Phosphorylation
Zymogens

Concept #1: Apparent Km and Vmax

###### Expert Q&A

Ask unlimited questions and get expert help right away.

Concept #2: Kmapp and Vmaxapp Are Affected by α And/Or α’

###### Expert Q&A

Ask unlimited questions and get expert help right away.

Example #1: The KI value for a certain competitive inhibitor is 2 µM.  When no inhibitor is present, the Km value is 10 µM.  Calculate the apparent Km when 4 µM inhibitor is present.

###### Expert Q&A

Ask unlimited questions and get expert help right away.

Practice: Competitive inhibitor A at a concentration of 2 μM doubles the apparent K m for an enzymatic reaction, whereas competitive inhibitor B at a concentration of 9 μM quadruples the apparent Km. What is the ratio of the K I for inhibitor B to the K I for inhibitor A?

Practice: The KI value for a certain competitive inhibitor is 10 mM. When no inhibitor is present, the Km value is 50 mM. Calculate the apparent Km when 40 mM inhibitor is present.

Practice: Uncompetitive inhibitor A at a concentration of 4 mM cuts the K mapp in half for an enzymatic reaction, whereas the Kmapp is one-fourth the Km in the presence of 18 mM uncompetitive inhibitor B. What is the ratio of the K’I for inhibitor A to the K’I for inhibitor B?

###### Expert Q&A

Ask unlimited questions and get expert help right away.