Lab 3 : Enzymes II Flashcards
Enzyme kinetics
Study of the rate of enzyme-catalyzed reactions
Vmax
Maximum rate of reaction for a given enzyme and substrate
Km
Substrate concentration at which the reaction rate is half of its maximum value
reaction is at its most effcient
Michaelis-Menten plot
Graph showing the relationship between reaction rate and substrate concentration in enzyme kinetics
Asymptote
A line that a curve approaches but never reaches
Reciprocal graphing
Graphing the reciprocal of variables to obtain a straight line
Lineweaver-Burk plot
Graphical representation of enzyme kinetics using reciprocal graphing
Competitive inhibitors
Inhibitors that compete with the substrate for binding to the active site of an enzyme
Non-competitive inhibitors
Inhibitors that bind to other sites on the enzyme and change its shape, reducing catalytic activity
Denatured
Loss of catalytic activity due to disruption of the enzyme’s shape
Active site
Region of an enzyme where substrates bind and are converted into products
Substrate
Molecule that binds to the active site of an enzyme and undergoes a reaction
Product
Molecule formed as a result of an enzyme-catalyzed reaction
Competitive inhibition
Inhibition where a competitive inhibitor increases Km but does not affect Vmax
Non-competitive inhibition
Inhibition where a non-competitive inhibitor reduces Vmax but does not affect Km
