M1.2.4+5 Flashcards
Enzymes
1
Q
Enzymes
A
- Made of proteins
- Catalyses chemical reactions in the body without being used up
- Substrate binds to active site (site with shape on enzyme)
2
Q
Coenzymes
A
- Organic substances that assist in catalysing (bind to acitve site)
- E.g. B12 vitamin
3
Q
Cofactors
A
- Inorganic substances that bind to enzymes, stabilising the enzyme or assisting in the reaction.
- E.g. Magnesium
4
Q
Catabolic reaction
A
- Substrate breaks into smaller molecules
5
Q
Anabolic reaction
A
- Smaller substrates combine into larger molecule
6
Q
Substrate
A
- Reactants
7
Q
Inhibitors
A
- Substances that bind to enzymes, changes the shape of active site
- Inhibits enzyme action
- Can cause diseases or regulate enzyme activity in a healthy way
8
Q
Competitive inhibtor
A
- Bind to active site of enzyme
- Stops substrate from binding to enzyme
9
Q
Non-competitive inhibitor
A
- Binds to enzyme, but not on active site
- Changes shape of active site, stopping substrate-enzyme complex from forming
10
Q
Saturation point
A
- If substrate concentration continues to increase when enzyme concentration stays the same, reaction rate will not increase because all enzymes are occupied
11
Q
Effect of temperature
A
- More temperature = more enzyme activity = higher reaction rate UP TO the optimum temperature
- After optimum temperature has been passed, heat can denature (deform active site) enzymes, so enzymes stop working
12
Q
Effect of pH
A
- Each enzyme has narrow band of pH levels in which it can function
- Ideally environment must stay within optimum pH levels
- Enzymes can only work in specific locations due to pH requirements
13
Q
Catalase optimum pH
A
7-11
14
Q
Trypsin optimum pH
A
7.8-8.7
15
Q
Pepsin optimum pH
A
2
