enzymes Flashcards
oxidoreductases
REDOX rxns that involve the transfer of electrons
transferases move a
function group from one molecule to another
hydrolases catalyze
cleavage w/ the addition of water
lyases catalyze cleavage without
the addition of water and transfer of electrons
isomerases catalyze the interconversion of
isomers
including constitutional isomers + stereoisomers
ligases join two large
biomolecules often of the same type
lipases catalyze the
hydrolysis of fats
dietary fats are broken down into
fatty acids and glycerol/other alcohols
kinases add a
phosphate group
type of transferase
phosphatases remove a
phosphate group
type of transferase
phosphorylases introduce a
phosphate group into an organic molecule (notably glucose)
exergonic rxn
RELEASE energy
gibbs free E = negative
endergonic rxns
require energy
gibbs free E = positive
enzymes do not alter the
gibbs free E or enthalpy or the final equilibrium position
enzymes only alter the
changing the rate of the reaction
as substrate increases, so does the
rxn rate until a max value is reached
K is the [S] at which an enzyme…
runs at half its Vmax
Vmax is the max rate at which an enzymes can….
catalyze a rxn
all enzyme active sites are saturated w/ substrate
cooperative enzymes display what kind of curve
sigmoidal curve b/c of activity change with substrate binding
enzymes stabilize the
transition state
enzymes provide a favorable microenvironment and/or…
bonding w/ the substrate molecules
site of catalysis is called
the active site
lock and key theory
enzyme and substrate are complementary and fit together like a key into a lock
induced fit theory is where the enzyme and substrate…
undergo conformational changes to interact fully
metal cation that is required by some enzymes
cofactor
what molecule is required by some enzymes
organic molecules
how does temp and pH affect enzymes
denaturation and loss of activity due to loss of 2/3/4 structure of proteins
salinity can impact the actions of
enzymes
feedback inhibition is when an enzyme is inhibited by
high levels of a product from later in the same pathway
reversible inhibition is the ability to replace the inhibitor with a….
compound of greater affinity or to remove i.t. using mild lab treatment
competitve inhibition
when inhibitior is similar to the substrate
binds at the active site
blocks substrate from binding
competitive inhibition can be overcome by
adding more substrate
vmax and km in competitive inhibtion
vmax unchanged
km increases
uncompetitive inhibition is when the inhibitors binds…
only w/ the ES complex
vmax and km in uncompetitive inhibtion
vmax and km decrease
noncompetitive inhibition is when the inhibitors binds with…
equal affinity to the enzyme and ES complex
vmax and km for noncompetitive inhibition
vmax decreases and km unchanged
mixed inhibition is when the inhibitor binds with unequal…
affinity to the enzyme and ES complex
vmax and km in mixed inhibition
vmax decreases
km increases/decreases depending on if the inhibitor has a higher affinity for the enzyme or ES complex
irreversible inhibition alters the enzyme in such a way that the
active site is unavailable for a prolonged duration / permanently
suicide inhibitor is a substrate analogue that binds…
IRREVERSIBLY to the active site via a covalent bond
allosteric effector binds at the allosteric site and induces a…
change in the conformation of the enzyme
the substrate can no longer bind to the active site
allosteric effector displays
cooperativity
does not obey MM-kinetics
positive allosteric effectors exert a
positive effect
increase activity
negative allosteric effector exert a
negative effect
decrease activity
homotropic effector is an allosteric regulator that is also the…
substrate
e.g. O2 is a homotropic allosteric regulator of hemoglobin
heterotropic effector is an allosteric regulator molecule that is
different from the substrate
what is phosphorylation
covalent modification with phosphate
catabolism
phosphorylated = active