Lecture16

Lecture16 - Lecture 16 11/2/11 Background reading: Berg, et...

Info iconThis preview shows pages 1–4. Sign up to view the full content.

View Full Document Right Arrow Icon
Lecture 16 11/2/11 Assignment: Segel: Page 319: problems 2, 6, 7 Background reading: Berg, et al: Pages 238 – 240 Garrett and Grisham: Pages 417 – 419 and 421 - 423 Outline: V max and K M Lineweaver-Burk plot Enzyme inhibition Competitive inhibition
Background image of page 1

Info iconThis preview has intentionally blurred sections. Sign up to view the full version.

View Full DocumentRight Arrow Icon
In the last lecture we derived the Michaelis-Menten equation that describes the hyperbolic curve we get by plotting initial velocity (v o ) as a function of [S]: v = V max [S] K M + S Can use this equation to calculate points on the curve. V max and K M When the [S] >> K M (Greater than 100 x K M ): The K M is small and drops out and the equation becomes v = V max P O Get Zero order kinetics in which the rate of reaction is independent of [S]. When the [S] << K M (Less than .01 x K M ): v = V max [S] K M = k [S] Get First order kinetics in which the velocity is directly proportional to the [S] and the line is straight. If v = ½ the V max the K M = [S] Thus the K M is equal to the substrate concentration at which the reaction rate is half its maximal value.
Background image of page 2
All enzymes show saturation effect, but they vary with respect to the [S] required to produce saturation. The K
Background image of page 3

Info iconThis preview has intentionally blurred sections. Sign up to view the full version.

View Full DocumentRight Arrow Icon
Image of page 4
This is the end of the preview. Sign up to access the rest of the document.

Page1 / 11

Lecture16 - Lecture 16 11/2/11 Background reading: Berg, et...

This preview shows document pages 1 - 4. Sign up to view the full document.

View Full Document Right Arrow Icon
Ask a homework question - tutors are online