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How do enzyme properties relate to their tertiary structure
enzymes are highly specific due to their tertiary structure
The active sites shape is determined by the enzymes tertiary structure
The tertiary structure of an enzyme may be altered by changes in the pH or temperature
The primary structure of a protein is determined by a gene. If a mutation occurs in that gene it could change the tertiary structure of the enzyme produced
How do enzymes change activation energy
enzymes lower the amount of activation energy that needed, making reactions happen at a lower temperature which speeds up rate of reaction
The enzyme substrate complex lower the activation energy (an enzyme substrate complex is formed when a substrate fits into the enzymes active site)
Whats induced fit
the active site changes shape slightly to be complementary to the substrate
Induced fit model explains why enzymes are so specific
Factors affecting enzyme activity
Temperature - if too low theres not enough kinetic energy for successful collisions between enzyme and substrate and if too high enzymes denature, active site changes shape and enzyme - substrate complex cannot form
pH - too high or too low can interfere with the charges in the amino acids in the active site. This can break bonds holding tertiary structure and active site changes shape, therefore enzymes denature and fewer enzyme - substrate complexes form
Substrate and enzyme concentration - if theres insufficient substrate, reaction will be slower as theres fewer collisions between enzyme and substrate, if theres insufficient enzymes, enzyme active sites will become saturated with substrate and unable to work any faster
Enzyme inhibitors - (competitive) are the same shape as substrate and can bind to active site, this prevents substrate from binding and reaction occurring (non-competitive) bind to enzyme away from active site and this causes active site to change shape so substrate can no longer bind