5. Explain/define Km and Vmax. Then explain the differences between competitive and noncompetitive inhibitors of enzyme(s).
Added by Timothy P.
Close
Step 1
**Km** (Michaelis constant) is the substrate concentration at which the reaction rate is half of the maximum rate (Vmax). It is a measure of the affinity of the enzyme for its substrate. A lower Km value indicates a higher affinity between the enzyme and Show more…
Show all steps
Your feedback will help us improve your experience
Sri K and 55 other Biology educators are ready to help you.
Ask a new question
Labs
Want to see this concept in action?
Explore this concept interactively to see how it behaves as you change inputs.
Key Concepts
Recommended Videos
How would a competitive inhibitor change the Km and the Vmax for an enzyme? Explain why a competitive inhibitor would result in these changes.
Sri K.
Differentiate between competitive and non competitive inhibition of enzymes.
Madhur L.
Arrange the phrases as describing a competitive inhibitor, uncompetitive inhibitor, or a pure noncompetitive inhibitor. Note that Km refers to apparent Km. Competitive inhibitor Uncompetitive inhibitor Noncompetitive inhibitor structurally similar to substrate binds enzyme-substrate complex only when present, Vmax of enzyme is unaffected when present, Km of enzyme will decrease Km is unchanged in the presence of this type of inhibitor forms inactive EI or ESI complex prevents substrate from binding enzyme
Rita D.
Recommended Textbooks
Biology for AP Courses
Objective Biology for NEET
Introduction to General, Organic and Biochemistry
Transcript
Watch the video solution with this free unlock.
EMAIL
PASSWORD