MCAT

Catalysts

Reduce activation energy without altering thermodynamics of a reaction

Allosteric site

Location on enzymes for activation or deactivation

Active site

Region where enzyme and substrate bind

Cofactor

Inorganic molecule assisting enzyme function

Coenzyme

Organic molecule aiding enzyme activity

Ligase

Enzyme joining molecules with ATP

Isomerase

Enzyme causing structural changes in compounds

Lyase

Enzyme breaking compounds without water

Hydrolase

Enzyme breaking compounds with water

Oxidoreductase

Enzyme transferring electrons between compounds

Transferase

Enzyme moving functional groups between compounds

Synthetase

Type of ligase enzyme

Km

Measure of enzyme-substrate affinity

Competitive inhibitors

Compete for active site, overcome by increasing substrate

Noncompetitive inhibitors

Bind to allosteric site, affecting substrate binding

Uncompetitive inhibitors

Bind to allosteric site, prevent substrate release

Mixed inhibitors

Decrease Vmax, affect Km based on preference

Turnover

Associated with higher Vmax

Apoenzyme

Enzyme lacking a cofactor

Holoenzyme

Enzyme with a cofactor

Lineweaver plot

Y-intercept proximity to zero indicates higher Vmax