UNIT 1 (topic 4) proteins and enzymes Flashcards
what is a enzyme
- a biological catalyst that lowers the activation energy of a reaction to speed up reactions
- they are proteins, globular shaped
define the active site
specific 3D shape because of the tertiary structure that binds to the substrate
define the substrate
the reactants that are complementary to an enzyme
what is the lock and key theory
- substrate and active site are complementary
- when they bind, E-S complex is formed
- reaction occurs and products are released from the active site
- active site is free to bind to other complementary substrate
what is the induced fit theory
- the binding of substrate causes the active site to change shape
- active site becomes complementary forming E-S complexes
- places stress on the bonds within the substrate - lowering the active site
- forces a reaction to take place
what are the factors effecting enzymes
- temperature
- pH
- concentration of enzymes
- concentration of substrate
why does temperature increase enzyme rate
- increases kinetic energy of enzymes and substrate
- more collisions between substrate and active site
- more E-S complexes formed
why does temperature decrease enzyme rate
- high temperature causes the H-bonds in the tertiary structure to break
- change shape of the active site meaning substrate no longer complementary
- E-S complexes no longer form
how is rate affected at the optimum pH
more E-S complexes formed, increased rate
what is the rate above and below the optimum pH
- changing pH affects concentration of H+ / OH-
- Disrupts H-bonds and ionic bonds in the tertiary structure
- changes shape of the active site
- no longer complementary so E-S complexes can’t be formed
why does the rate increase as the concentration of enzyme/ substrate increases
- more substrate/ active sites so higher chance of collisions
- more E-S complexes formed
why does the rate plateaus as the concentration increases
- enzyme/ substrate becomes the limiting factor
- all is occupied so rate cannot increase further
define an enzyme inhibitor
substances that prevent the active site from binding to the substrate to prevent E-S complexes
how does competitive inhibitors prevent E-S complexes
- inhibitor has similar shape to the substrate and bind to active site
- physically prevents the binding of substrate and active site
how does the non- competitive inhibitors prevent E-S complexes
- the inhibitor binds to an allosteric site in the enzyme
- this alters the tertiary structure
- changes shape of the active site