TA Review 1 Flashcards
Exam 2
when enzymes stabilize the transition state, what do they do?
reduce activation energy
chymotrypsin pocket is
large and hydrophobic
Trypsin pocket is
contains aspartate (- charged)
Elastase pocket is
size constrained
binds to small aa like glycine, alanine, valine
Elastase
binds to positively charged aa residues like argenine and lysine
trypsin
binds more hydrophobic aa residues, such as tryptophan and phenylalaline
chymotrypsin
pancreatic enzymes are
serine proteases
catalytic machinery is composed of
catalytic triad and oxyanion hole
serine 195 acts as an
alkoxide
asp 102, ser 57 and ser 195 form a network of hydrogen bonds that forces ser 195 to be
very active
what does the oxyanion hole does?
stabilizes the transition state via hydrogen bonding
catalyze redox reactions
oxidoreductase
catalyze transfer of chemical group
transferase
catalyzes cleavage with water
hydrolases
catalyzes cleavage reaction without water
lyases
catalyzes change of molecular configuration
isomerases
catalyzes joining of two compounds
ligases
process of serine protease (3)
(1) attack by serine
(2) stabilization of transition state
(3) release of products
release of products in serine protease
attack by water causes release of products and regeneration of enzyme
delta G = -
spontaneous reaction
delta G= 0
reaction at equilibrium
delta G= +
non-spontaneous reaction
delta G is sensitive to concentration of
reactants, products, temperature, pH