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Enzymes

Unit 3&4 Biology

TermDefinition
denature permanent change in tertiary structure of enzyme which changes shape of the active site and prevents the enzyme from functioning
enzyme-substrate complex complex formed when enzyme is bound to its substrate
active site location on enzyme where substrate binds
activation energy amount of energy required for reaction to begin, is lowered by enzymes
irreversible inhibition inhibitor is permanently bound to enzyme so substrate can not bind to active site
non-competitive inhibition inhibitor binds to allosteric site and prevents the substrate from binding to the active site
rate of reaction how quickly products are produced
substrate reactant that binds to the active site of its specific enzyme
optimal conditions specific pH and temperature which allows enzyme to function at its fastest
lock and key model model: complementary bonding between enzyme and substrate where the substrate fits perfectly into the active site of the enzyme
coenzymes substance which must bind to an enzyme to help it to function (Eg: ADP/ATP; NAD/NADH; NADP/NADPH)
enzyme protein that catalyses a reaction by binding to a specific substrate
allosteric site location on enzyme where non-competitive inhibitor binds to change the shape of the active site
induced fit model model bonding between enzyme and substrate is imperfect, and active site changes shape slightly to better bind with its substrate
competitive inhibition inhibitor competes with substrate for active site, when it binds to active site it prevents substrate from binding
catalyse speeds up the rate of reaction by lowering the activation energy
reversible inhibition inhibitor is not permanently bound to enzyme and once it is removed, the substrate can again bind to active site
Created by: BiologyBright
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