| Enzymes functions | -SPECIFIC TERTIARY STRUCTURE
-SPECIFIC ACTIVE SHAPE
-ONLY COMPLEMENTARY TO THE ACTIVE SITE
-LOWER ACTIVATION ENERGY |
| Lock and Key theory | active site is complimentary |
| Induced fit theory | The acitve site is not complimentary so it changes the active site |
| endings of enymes and their meaning | ase- carbohydrate - glycosidic bond
ease-protein- peptide |
| Factors affecting rate of reaction | -enzyme concentration
(run out substrates for es complexes)
-substrate concentration increases so more es complexes then substrate conc is no longer the limiting factor ( max es complexes not enough enzymes)
-temperature
(kinetic energy increases so more collisions creating es complexes quicker until it reaches optimum temp and the max everything until it suceeds this then causes hydrogen/ionic bonds in enzyme to break
Causes enzyme’s ts to change,so active s changes no longer compimentary)
PH
(ph changes cause hydrogen bonds to break in the specific tertiarty structure) |
| What is a competitive inhibitor ? | inhhibitor competes with the substrate for the active site and binds preventing the substrate and active site binding so the rate of r is slower |
| Keywords for when an enzyme denatures. | Bonds break
Tertiary structure
Active site shape
Not complementary
No ES complexes |
| Enzyme denatures | Bonds break -hydrogen and ionic bonds in the enzyme break
Tertiary structure - changes
Active site shape -this causes the active site shape to change
Not complementary -not complementary to active site
So no ES complexes form |
