SC BIOL 541 - Competitive Inhibition (2 pages)

Previewing page 1 of 2 page document View the full content.
View Full Document

Competitive Inhibition

Previewing page 1 of actual document.

View the full content.
View Full Document
View Full Document

Competitive Inhibition


Lecture number:
Lecture Note
University Of South Carolina-Columbia
Biol 541 - Biochemistry

Unformatted text preview:

BIOL 541 1st Edition Lecture 8 Outline of Last Lecture I Molecular basis for properties Outline of Current Lecture II Competitive Inhibition III Non competitive Inhibition IV Catalysis Current Lecture Biochem Lecture 8 Competitive Inhibition Lineweaver and Burk Double reciprocal plot gives straight line graph to determine the parameters of kinetics Competitive Inhibition When inhibitor binds to the same binding catalytic site that the substrate binds but since it is not substrate there is no reaction In other words it occupies the same place as the substrate and competes with the substrate for the active site Non Competitive Inhibition When the inhibitor binds on the site of the enzyme separate from the catalytic site so the substrate enzyme and inhibitor bind together with no competition Catalysis These notes represent a detailed interpretation of the professor s lecture GradeBuddy is best used as a supplement to your own notes not as a substitute Enzymes need thermodynamic reactions Spontaneous reactions enzymes need free energy to be reduced In other words the increase in the reactants free energy causes a decrease in the free energy of the product A high energy state called the transition state is the hurdle whereby small hurdle can be overcome and spontaneous reaction can go ahead Free energy reactions can bounce this Reactions that have high energy of activation have a difficult and slow reaction Pyranose 6 member ring has 3 conformations Boat half chair and chair less energy than boat Half chair conformation has more energy than other forms In other words half chair can overcome hurdle Enzymes can lower energy of activation by 1 Reactants in solution can form products The enzyme thus has an active site for both substrate A and B and brings them together or APPROXIMATES reactants and causes randomness and enthropy It brings proper joining of A and B to a molecule site oriented next to each other 2 Therefore ORIENTATION mechanism affects free energy but not

View Full Document

Access the best Study Guides, Lecture Notes and Practice Exams

Loading Unlocking...

Join to view Competitive Inhibition and access 3M+ class-specific study document.

We will never post anything without your permission.
Don't have an account?
Sign Up

Join to view Competitive Inhibition and access 3M+ class-specific study document.


By creating an account you agree to our Privacy Policy and Terms Of Use

Already a member?