Enzyme Kinetics II 10/16/2008.

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Presentation transcript:

Enzyme Kinetics II 10/16/2008

Kinetic data cannot unambiguously establish a reaction mechanism. Although a phenomenological description can be obtained the nature of the reaction intermediates remain indeterminate and other independent measurements are needed.

Reaction Mechanisms A: Sequential Reactions All substrates must combine with enzyme before reaction can occur

Bisubstrate reactions Single displacement reactions

Random Bisubstrate Reactions

Ping-Pong Reactions Group transfer reactions One or more products released before all substrates added

Inhibition kinetics There are three types of inhibition kinetics competitive, mixed and uncompetitive. Competitive- Where the inhibitor competes with the substrate.

Competitive Inhibition

HIV protease inhibitors

Competitive Inhibition: Lineweaver-Burke Plot

Uncompetitive Inhibition

Uncompetitive Inhibition: Lineweaver-Burke Plot

Mixed inhibition

Mixed inhibition is when the inhibitor binds to the enzyme at a location distinct from the substrate binding site. The binding of the inhibitor will either alter the KM or Vmax or both.

The effect of pH on kinetic parameters

Lecture 17 Tuesday 10/21/08 Enzyme Kinetics / Exam II Minireview