Lecture 7 - Enzyme Kinetics Flashcards
Substrates bound to enzymes by
Electrostatic bonds
H-bonds
Van der waals forces
hydrophobic interactions
Isomerase
catalyze intramolecular rearrangements of molecules
reverse reaction of lyase
synthase
Molecules that naturally regulate enzyme activity are
reversible noncompetitive inhibitors
enzyme is fully active when it has
sugar + ADP
Feedback Inhibition
Metabolic pathway turned off by its end product (inhibitor)
Kinase adds or removes PO4?
adds
transition state complex
increase reaction rates by decreasing the amount of energy required
Factors that influence enzyme catalyzed reactions
temperature
pH
enzyme concentration
substrate concentration
Km
Substrate concentration at which the reaction rare = ½ maximal value
Vmax
Maximal rate of product formation when substrate concentration is high
Characterization of Protein
-molecular masss
-isoelectric point
-chromatography
Kcat
Measure of catalytic activity