SC BIOL 541 - Competitive Inhibition (2 pages)

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Competitive Inhibition



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Competitive Inhibition

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Lecture number:
8
Pages:
2
Type:
Lecture Note
School:
University Of South Carolina-Columbia
Course:
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



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