David L Nelson and Michael M Cox LEHNINGER
- Slides: 46
David L. Nelson and Michael M. Cox LEHNINGER PRINCIPLES OF BIOCHEMISTRY Sixth Edition CHAPTER 6 Enzymes © 2013 W. H. Freeman and Company
Name the reaction type and the coenzyme used
Binding of a substrate to an enzyme at the active site
There is an energy barrier between formation of product from substrate There is an activation energy formation of the transition state
Enzymes enhance reaction rates by lowering activation energies Enzymes do not affect equilibrium
How a catalyst circumvents unfavorable charge development during cleavage of an amide
Amino acids in general acid-base catalysis
Effect of substrate concentration on the initial velocity of an enzyme-catalyzed reaction Michaelis-Menten plot Double-reciprocal or Lineweaver-Burk plot
kcat = Vmax / [E]total kcat has units of reciprocal time
kcat / Km is a measure of catalytic efficiency
Many enzymes catalyze reactions with two or more substrates
Three types of reversible inhibition
Three types of reversible inhibition
Three types of reversible inhibition
Competitive inhibition Uncompetitive inhibition Mixed inhibition
Molecules that are transition state analogs are effective reversible competitive inhibitors
Irreversible enzyme inhibition
p. H – activity profiles for two enzymes
Structure of chymotrypsin, a serine protease
Mechanism of action of HIV protease
HIV protease inhibitors
The transpeptidase reaction
Mechanism of action of penicillin
Beta lactamase inactivates penicillin
Inactivation of beta lactamase by clavulanic acid
Subunit interactions in an allosteric enzyme, and interactions with inhibitors and activators
Aspartate transcarbamoylase, an allosteric enzyme
Regulation of enzyme activity by covalent modification
Regulation of enzyme activity by covalent modification
Regulation of enzyme activity by proteolytic cleavage Example: Activation of zymogens, inactive precursors of proteases
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