Block 1 Flashcards
(426 cards)
what do enzymes increase
speed of reaction
what type of molecule are most enzymes
proteins
what is an apoenzyme
enzyme without its co-factor
non functional
a cofactor that is tightly bound to the enzyme is called what
prosthetic group
cofactors that are complex organic molecules are called what
coenzymes
what are isoenzymes
same enzyme, different structure
what is a zymogen
an inactive enzyme that must be cleaved to become active
what are 2 examples of zymogens
trypsin and chymotrypsin
what are the 4 basic steps of enzyme catalyzed reactions
- binding of substrate
- formation of enzyme substrate complex
- conversion of substrate to product
- release of product from active site
the active site of an enzyme is composed of the __ site and the __ site
catalytic and substrate binding
what does the induced fit model tell
interaction of substrate with enzyme induces conformational changes so the binding is a better fit
what do enzymes reduce
activation energy
what is the transition state for enzymes
peak of energy curve where reactants convert to products
what is involved in catalysis by bond strain
rearrangement when enzyme is bound to substrate induces strain
what is involved in covalent catalysis
formation of a covalent intermediate
what is an example of a covalent intermediate in covalent catalysis
serine proteases
what amino acids make up the serine protease triad
histidine
serine
glutamate (or aspartate)
co-enzymes are often what
water soluble vitamins
increased transcription of a gene or decreased proteolysis of enzyme protein increases or decreases enzyme activity
increases
effect of temperature on enzyme activity
too high= denature
too low= slow down
pH effect on enzyme activity
too high or low= denature
what is Km
the substrate concentration at 1/2Vmax
small Km means high or low enzyme affinity for substrate
high
high enzyme affinity means high or low substrate concentration
low