1.4 Flashcards
non competative inhibitors
binds to the alosteric site
alters the shape of the active site so the substrate cannot bind
if you want a faster rate add more ezymes
induced fit model
active site is flexible
once the substrate enters the shape of the active site is modified to fit around it
once the substrate complex leaves the active site returns to normal
temperature
ph rate of reaction graph
same as temp
substrate concentration
competative inhibitors
similar shape to substrate
competes with the substrate to bind to active site so the substrate can no longer bind
decreasing rate of reaction
increases the rate by adding more complex
temperature affect on enzymes
temperature increases
rate of reaction increases as the particles have more kinetic energy
more likely successful collisions
when temperature goes over the optimum the enzymes denatures
tertiary structure changes
so shape of active site changes
so substrate no longer fit/complimentary
no substrate complexes can be formed
acid affect on enzymes
acid affects hydrogen bonds
active site structure changes
so substrate no longer fits
substrate complexes no longer formed
why is initial rate of reaction important
as soon as the reaction starts the substrate is broken down
so substrate concentration can no longer be controlled
which limits the rate of reaction
why can misfolded protein not be digested
enzymes have a specific active site to certain amino acids
change in the base sequence changes the tertiary structure
no longer complimentary
so peptide bonds can not be formed
substrate complexes cannot form
