enzymes Flashcards
enzymes
most are proteins. all are catalysts. not used up in reactions. highly specific. accelerate reactions
what are the 6 enzyme classes?
oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases
oxidoreductases
oxidation-reduction reactions
transferases
group transfer reactions
hydrolases
hydrolysis reactions
lyases
addition or removal of groups to form double bonds
isomerases
isomerization ( intramolecular group transfer)
ligases
ligation of two substrates at the expense of ATP hydrolysis
holoenzyme
the active enzyme with its non-protein component
apoenzyme
the enzyme without its non-protein moiety and is inactive
cofactor
non-protein moiety that is a metal ion (minerals)
coenzyme
small organic molecules (vitamins)
what do enzymes alter?
reaction speed
lock and key model
enzyme’s tertiary structure consists of a unique pocket or site which is tailor made to fit only its substrate
induced fit model
as enzymes interact with substrates they change their conformation so that the enzyme is snug around the substrate
factors affecting reaction rates
temperature, pH, enzyme concentration, and substrate concentration
Vo
initial velocity of reaction
[S]
concentration of substrate
Vmax
the theoretical maximal rate of the reaction
Km
substrate at which the reaction velocity is equal to 1/2 Vmax
inhibitor
any substance that can diminish the velocity of an enzyme-catalyzed reaction
irreversible inhibitors
bind to enzymes through covalent bonds
reversible inhibitors
bind to enzymes through noncovalent bonds
competitive inhibition
inhibitor binds reversibly to the same site as substrate
noncompetitive inhibition
inhibitor binds to different sites than enzymes
allosteric enzymes
have multiple subunits. can either inhibit or increase enzyme activity
homotropic effectors
substrate serves as effector, enhancing other substrate-binding sites. binding to one site “helps” other sites
heterotropic effectors
effector different from substrate, effector may be the product, + feeds back to cause inhibition
homotropic positive
substrate that is the same as the initial chemical activates itself
heterotropic positive
substrate that is different from the initial molecule is activating the reaction
homotropic negative
substrate that is the same as initial molecule in reaction is inhibiting reaction mechanism
heterotropic negative
substrate that is different from initial reaction molecule inhibits the reaction
Michaelis-Menten non-competitive
covalent, irreversible. decreases Vmax
Michaelis-Menten competitive
non-covalent, reversible. increases substrate and Km