1.5 Enzymes Flashcards
name three properties of enzymes
biological catalysts
specific shape
lower activation energy
proteins with a tertiary/globular structure
describe an anabolic reaction
catalysed by anabolic enzymes
involves making bonds
includes building up larger molecules
e.g. protein synthes
describe a catabolic reaction
catalysed by catabolic enzymes
involves breaking bonds
produces smaller molecules
e.g. digestion
describe the lock + key hypothesis of enzyme action
- the enzyme’s active site and the substrate have complementary shapes
- the substrate binds onto the active site of the enzyme
- an enzyme-substrate complex forms
- the enzyme reduces the activation energy required to break bonds in the substrate
- products move away from the active site + enzyme is reusable
described the induced fit theory of enzyme action
- suggests that enzymes induce their active site to have a complementary shape with the substrate
- when products are formed, the enzyme returns to its original shape
factors affecting enzyme action
enzyme concentration substrate concentration temperature pH co-factors inhibitors
describe how a competitive inhibitor works
- the substrate and competitive inhibitor have a similar shape
- competitive inhibitor fits into the active site, blocking the substrate
- rate of reaction is reduced
- reversible
describe how a non-competitive inhibitor works
non-competitive inhibitors bind somewhere other than the active site
- causes a permanent change to the shape of the active site
- irreversible
describe the effect of temperature on enzymes
- as the temperature increases, kinetic energy of the molecules increases
this means the enzyme and substrate are more likely to collide and form enzyme-substrate complexes so rate of reaction INCREASES - after the optimum temp is reached, kinetic energy causes intramolecular vibration that breaks bonds within the enzyme so the active site changes
this means enzyme-substrate complexes cannot form
rate of reaction DECREASES
describe the effect of pH on enzymes
in highly acidic or alkaline environments, H+ or OH- ions interact with amino acids in the enzyme, breaking bonds and altering the shape of the active site, causing the enzyme to denature