Enzymes 1 Flashcards
how do enzymes act as catalysts
lower activation energy by providing alternative transition state
5 key features
- Globular proteins
- Show specificity
- Catalysts
- Sensitive to changes in physical and chemical environment
- Their activity can be controlled
Lysozome
2 points
- enzyme in tears and secretions on exposed surfaces of body
- attacks bacterial cell walls killing the bacteria (natural antibiotic)
Lysozome
shape
includes a cleft into which part of the bacterial cell wall (made of peptidoglycan) can fit
Lysozome
which bond does it break
bond between sugars 4 and 5 of a hexamer
2 parts of AS
Substrate Binding Site
Catalytic Site
lock and key
binding site has complementary shape to substrate(s)]
induced fit
contact between part of the binding site and the substrate induces a change in shape of the active site to bind to the substrate
4 levels of enzyme specificity
absolute
bond
group
stereo
catalysts lower
activation energy
catalysis
proximity
substrate molecules close together
catalysis
orientation
substrates have correct relative orientation
catalysis
Strain/distortion
binding puts strain on bond making it easier for reaction to occur
acid-base catalysis
protons (H+) donated/accepted
Covalent catalysis
temporary covalent bond between enzyme and substrate
effect of time
start of reaction
very quick
Maximum ratio of S/E so greatest chance of collision
effect of time
middle of reaction
amount of S decreases (it is converted to P) less chance of S colliding with E so rate of reaction decreases
effect of time
end of reaction
Rate decreases until reaction reaches equilibrium (no net change in amount of S or P) when graph reaches plateau. Rate = 0
dont understantd inital reaction velocity on graph
?
IRV
Initial Reaction Velocity (t=0) =
x/y
used to compare enzyme activities
Katal
1 Katal of enzyme activity produces 1 mole of product per second
or utilises one mole of substrate per second
(1 Katal = 1 mole/sec)
Unit
1 Unit of enzyme activity produces 1 umole of product per minute
or utilises 1 umole of substrate per min
(1 Unit = 1 mmole/min)
Turnover number (kcat)
the number of substrate molecules that can be converted to product by 1 enzyme molecule in 1 second
Changes in pH affect
electrostatic bonds