MCAT

Catalysts reduce activation energy and do not change a reactions thermodynamics

The allosteric site is where enzymes are able to be turned on or off

The active site is where the enzyme and the substrate bind

A cofactor is inorganic

A coenzyme is organic

Ligase is an enzyme that join substances together using ATP

Isomerase is an enzyme that causes structural rearrangements in a compound

Lyase is an enzyme that breaks compounds without water

Hydrolase is an enzyme that breaks apart compounds using water

Oxidoreductase is an enzyme that transfers electrons between compounds

Transferase is an enzyme that transfers functional groups from one compound to another

Synthetase is a ligase

Peptidase, nuclease, and lipase are hydrolases

Dehydrogenase, reductase, and oxidase are oxidoreductases

Kinase is a transferase

High Km=Low enzyme-substrate affinity

Competitive inhibitors compete for active site and only increasing substrate can overcome it

Noncompetitive inhibitors bind to the allosteric site so that the substrate cannot bind, there is an equal affinity for solo enzyme and enzyme-substrate complex

Uncompetitive inhibitors bind to the allosteric site and does not allow for the substrate to release

Mixed inhibitors decrease Vmax, when they prefer enzyme+substrate it lowers km, when they prefer solo enzyme it increases km

Increased turnover is associated with a higher Vmax

Apoenzyme is an enzyme without a cofactor

Holoenzyme is an enzyme with a cofactor

Competitive inhibitors have increased Km and unchanged Vmax

Noncompetitive inhibitors have unchanged Km and reduced Vmax

Uncompetitive inhibitors have reduced Km and reduced Vmax

In a lineweaver plot, The closer the y-intercept is to zero is the higher the Vmax