enzymes Flashcards
what are enzymes
biological catalysts as they speed up rate of chemical reactions
what is the lock and key model
-active site of enzyme is perfectly complementary to substrate
-an enzyme substrate complex is formed
-products of reaction leave active site
what is the induced fit model
Enzyme active site is complementary to the substrate
When substrate binds a conformital chnage occurs in the tertiary structure of the enzymes active site
This stresses the h bonds in the substrate
Reducing the activation energy for the reactionas they require little energy to break
The reaction occurs quicker
how does temperature affect enzyme activity
-high temperature will increase ke and make enzyme molecules vibrate more if temp gets too high this vibration can break the h bonds holding together the enzymes tertiary shape so the active site will no longer be complementary to the substrate so enzyme is denatured
how does ph affect enzyme activity
the H+ and OH- found in acids and alkalis can mess up the ionic and hydrogen bonds that holds together the enzymes tertiary structure which can denature the enzyme
how does substrate concentration affect enzyme activity
more substrate molecules means a collison between a substrate and enzyme is more likely so more esc will form until saturation point where all active sites are full
what is a competitive inhibitor
-have a similar shape to substrate
-bind to the active site to block any substrate molecules out so no esc can form
-adding substrates can knock out the comp inhibitor from the active site
what is a non competitive inhibitor
-bind to the allosteric site of the enzyme
-this causes a change in shape of the active site so substrate molecules can no longer bind to it