Enzymes Flashcards
Lock and Key model
Induced fit model
Factors affecting enzyme function
- pH, salinity, temperature, cofactor association
- Apoenzyme: enzyme without its cofactor
- Holoenzyme: enzyme with its cofactor
Enzyme Regulation
- covalent modification i.e. phosphorylation
- proteolytic cleavage (zymogens)
- Association with other proetins
- Allosteric regulation (feedback inhibition)
Proteolytic cleavage
i.e. zymogens
Saturation
All active sites are occupied by substrate, so increasing [s] will not increase the rate (Vmax)
Km (michaelis constant)
- Substrate concentration at 1/2 Vmax
- The smaller the Km, the greater affinity for the substrate
Michaelis-Menten equation
Lineweaver-Burk Plots
Competitive, uncompetitve, noncompetitive
inhibition
Oxidoreductases
catalyze redox reactions (electron transfer)
Transferases
catalyze transfer of functional groups
Hydrolases
catalyze cleavage of molecules driven by the addition of water
Lyases
catalyze addition of atoms or groups to a double bond
Isomerases
catalyze transfer of functional groups within a
molecule (creates different isomers of the same molecule)
i.e. mutase