Midterms_Enzymes Flashcards
Explains the specificity of enzyme, enzyme is pictured as conformationally rigid.
Emil Fischer’s Lock and Key Model (1984)
For catalytic isomerizations.
Isomerases
Occurs when an inhibitor binds with an enzyme but does not dissociate from it under reaction conditions or within time-frame.
irreversible inhibition
Aka absolute specificity
Substrate Specificity
Oxidizes or reduce substrate by transferring hydrogen or electrons
Oxido-Reductates
Cause condensation of two molecules by splitting a phosphate bond
Ligases or synthetases
characterized by the maintenance of enzyme activity even at high inhibitor concentrations
partial inhibition
Structure is maintained by weak IMF
Koshland’s Induced Fit Hypothesis (1958)
Hanes-Woolf Plot
S/v = (1/vmax)S + Km/Vmax
Inhibitor binds to the enzyme at non active sites and reduces affinity of enzyme to substrate.
Noncompetitive inhibitors
Approach of the substrate in induced fit is viewed as
perturbation
Studies enzyme-catalyzed reaction rates and how changes in experimental conditions affect the reaction rates.
Enzyme kinetics
Inhibitor may dissociates more easily from the enzyme after binding
Reversible inhibitors
enzymes for hydrolytic reactions
hydrolases
Lineweaver-Burk equation
1/v = km/vmax (1/s) + 1/Vmax
Michaelis Menten Kinetics do not apply to irreversible inhibition (True or False)
True
compounds bind to enzyme and reduce their activity
enzyme inhibitors
removes groups and transfer them to acceptor molecules
Transferases
Selectivity of the enzyme to their substrate, molecular recognition mechanism
Specificity
proteins produced by living cells and acts as biological catalysts
Enzyme
Essential feature of enzyme-catalyzed reactions is
saturation
In the absence of _______, the enzyme will be inactive even if there are plenty of substrates.
Specific co-factor
inhibitor forms a stable complex with the enzyme
Irreversible inhibitors
Factors affecting enzyme activity
Temperature, pH, enzyme concentration and substrate concentration