2.4: Enzymes (new) Flashcards
What is an enzyme?
Biological catalysts that speed up the rate of chemical reaction by decreasing activation energy
Substrate binds to active site to form an enzyme substrate complex
Made up of globular proteins
What are the two enzyme mechanisms?
- Lock and key - enzyme and substrate bind perfectly
- Induced fit - active site slightly changes shape it fit substrate
What is an apoenzyme?
An inactive form of the enzyme
When they experience activation they turn into a holoenzyme
What are features of cofactors?
- Inorganic (minerals)
- Temporarily bound to the enzyme - when they bind they will activate it
e.g Chlorine ions bind to amylase
What are featuress of coenzymes?
- Organic (vitamins)
- Temporarily bound
e.g NADP
What are features of prosthetic groups?
- Permenantly bound by covalent bonds
e.g Iron in haem group or zinc in carbonic anhydrase
What does the enzyme carbonic anhydrase do?
It contains a zinc ion permemantly bound, as a prosthetic group, to it’s active site
- Found in erythrocytes (rbc)
- catalyses the interconversion of CO2 and H2O to carbonic acid
- this then breaks down into protons and hydrogencarbonate ions
What does temperature do to enzymes?
- When temperature increases the molecules gain more kinetic energy and start to move quicker
- There is a higher chance for the enzyme and substrate to collide with each other (more successful collisions)
- This increases the rate of reaction
- After it reaches it optimum temperature the enzymes denature and the rate of reaction slows down
What happens when substrate concentration increases?
- There will be more substrate to form enzymes substrate complexes
- The rate of reaction will increase only to a certain extent
- It is a limiting factor because all the enzymes are occupied
- Max ESC is formed
What happens when enzyme concentration increases?
- There will be more enzymes to form enzymes substrate complexes
- The rate of reaction will increase only to a certain extent
- It is a limiting factor because therer would be no substrate left
- Max ESC is formed
What is an inhibitor?
A chemical that could bind to the enzyme in a certain way to reduce the rate of chemical reaction
What is a competitive inhibitor?
An inhibitor that has a similar shape to the substrate molecule that is complementary to the active site. Therefore it competes with the substrate for the active site
What is a non - competitive inhibitor?
It binds to the allosteric site . The binding causes a conformational change (structural change) to the active site of the enzyme. This means it is no longer complementary to the substrate
What does the competitive inhibitor do?
- Similar structure to substrate
- Competes with the substrate for the same active site
- Less active sites are avaliable
- Less ESC formed and the rate of reaction decreases
- When there is a higher concentration of substrate molecules it can outcompete and restore the Vmax
What does the non-competitive inhibitor do?
- Binds to the allosteric site
- Changes the 3D structure of the active site
- Active site no longer complementary to substrate
- Less ESC formed so the rate of reaction decreases
- HIgher substrate concentration cannot restore Vmax