Ch 2: Enzymes Flashcards
Oxidoreductases
catalyze oxidation-reduction reactions that involve the transfer of electrons
Transferases
move a functional group from one molecule to another molecule
Hydrolases
catalyze cleavage with the addition of water
Lyases
catalyze cleavage without the addition of water and without the transfer of electrons
Isomerases
catalyze the interconversion of isomers, including both constitutional isomers and stereoisomers
Ligases
responsible for joining two large biomolecules, often of the same type
Enzymes do NOT alter
free energy (G), enthalpy (H), or final equilibrium position change that accompanies the reaction
Enzymes DO alter
rate (kinetics) at which reaction is reached
Enzymes bind to the
active site
Affect an enzyme’s activity in vitro
temperature, pH, and salinity
Reversible inhibition
ability to replace inhibitor with a compound of greater affinity or to remove it using mild laboratory treatment; competitive, noncompetitive, mixed, uncompetitive
Competitive inhibition
inhibitor is similar to substrate and binds at the active site and can be overcome by adding more substrate; vmax unchanged, Km increases
Noncompetitive inhibition
inhibitor binds with equal affinity to the enzyme and enzyme-substrate complex; vmax decreased Km unchanged
Mixed inhibition
inhibitor binds with unequal affinity to the enzyme and the enzyme-substrate complex. vmax decreased, Km unchanged
Uncompetitive inhibition
inhibitor binds only with enzyme-substrate complex; Km and vmax both decrease