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Zymogen
Cosubstrate
Enzymes
Free energy of activation ΔG‡ of a one step reactions
Enzymes
Free energy of activation ΔG‡ of a two step reactions
Enzymes
Catalyst affect ΔG‡ of a reaction
Enzymes
Catalytic Mechanisms
Acid-base catalysis
Covalent catalysis
Nucleophile
Carbonic anhydrase
Enzymes
Proximity and Orientation
Glu35 acts
as an acid
catalyst
Asp52 acts as
a covalent
catalyst
Serine Proteases
Active site residues identification by chemical labeling
Serine Proteases
Chymotrypsin
Serine Proteases
Serine Proteases
Serine Proteases
Serine Proteases
Stabilization of the transition state
Tetrahedral intermediate
Oxyanion
H-bond
Strong H-bond with
shorter bond lengths
Low barrier H-bonds (LBHB)
y = mx + b
Half-time /
Half-life
Enzyme kinetics
For a second order reaction
β-fructofuranosidase
At very high concentration of Sucrose the reaction
rate is zeroth order with respect to sucrose
Difficult to integrate
Enzyme kinetics
Michaelis-Menten equation assumes that [ES] maintains a steady state
Assumption of equilibrium
Michaelis constant
Enzyme kinetics
Initial velocity of the reaction Vo
Michaelis-Menten equation
At KM = [S], Vo = Vmax/2
Lineweaver-Burk Plot
Double-Reciprocal Plot
Enzyme Inhibition
Competitive inhibitor binds to the active site of the enzyme
A noncompetitive / mixed inhibitor binds both the enzyme and the enzyme-
substrate complex, alters both catalytic activity and substrate binding
Enzyme Inhibition
Competitive inhibition
Enzyme Inhibition
Competitive inhibition
Alcohol dehydrogenase
(liver)