Enzymes as Catalysts Flashcards
oxidosreductases
oxidation-reduction reaction enzymes
transferases
transfer of a chemical group enzymes
hydrolases
lysis by water enzymes
lyases
cleavage without the use of water enzymes
isomerases
change of molecular configuration enzymes
ligases
joining of two compounds enzymes
serine proteases
proteolytic enzymes including trypsin, chmotrypsin, and elastase, enzymes involved in blood coagulation
specificity pocket of an enzyme
positions the substrate in the correct orientation for catalysis
chymotrypsin (specificity pocket)
a hydrolase, recognizes bulky hydrophobic side chains of suitable peptides
trypsin (specificity pocket)
has a negatively charged group, binds to peptides that are positively charged
elastase (specificity pocket)
has a very narrow pocket, binds specifically to smaller amino acids
catalytic triad
side chain functional groups of aspartic acid, histidine, and serine - in a particular configuration at the enzyme’s active site
alkoxide ion
CH20- - very reactive, serine 195 behaves like it during catalysis
oxyanion hole
enzyme stabilizes oxyanion transition state in this location
Delta G
the free energy of a reaction, when negative a reaction will proceed spontaneously
standard free energy
the free energy with the components at a concentration of one mole/liter
Delta G is 0 at…
equilibrium
irreversible reactions
have large negative values for delta G
catabolism
food or fuel is degraded to smaller molecules with the release of energy
anabolism
reactions of processes that require the input of energy
Vmax
the maximum velocity of an enzyme at a given concentration
(High/low) substrate levels are suitable for assays of enzyme concentration
High - the velocity is the highest and directly proportional to the amount of enzyme
(High/low) substrate levels are best for assays of substrate concentration
Low - the initial enzyme velocity is directly proportional to the amount of substrate
Km
equal to the substrate concentration at 1/2Vmax