ENZYME KINETICS. Medical Biochemistry, Lecture 24. Lecture 24, Outline. Michaelis-Menten kinetics Interpretations and uses of the Michaelis-Menten equation Enzyme inhibitors: types and kinetics. Enzyme Kinetics Equation. Michaelis-Menten Equation. Initial Velocity (v o ) and [S].
Download Policy: Content on the Website is provided to you AS IS for your information and personal use and may not be sold / licensed / shared on other sites. SlideServe reserves the right to change this policy at anytime.While downloading, if for some reason you are not able to download a presentation, the publisher may have deleted the file from their server.
Medical Biochemistry, Lecture 24
A. Low [S] B. 50% [S] or Km C. High, saturating [S]
Vmax - No change
Km INCREASES - indicates a direct interaction
of the inhibitor in the active site
Vmax DECREASES - inhibitor affects rate of reaction
by binding to site other than substrate active-site
Km - No change