ENZYMES
- Created by: AbbyRucker
- Created on: 15-03-22 12:29
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- ENZYMES
- models
- induced fit model
- newer model, more realistic and used today
- states that substrate interacts with bonds in tertiary structure of enzyme to make active site perfectly complimentary to substrate shape
- lock and key model
- old model, unrealistic and no longer used to explain ESC
- states that the substrate has to have exact complementary shape to active site, this is fixed
- induced fit model
- role of enzymes
- enzymes are biological catalysts and work by reducing the activation energy
- activation energy is the energy needed to complete a reaction
- anabolic - making up reaction
- breaking down reaction
- Vmax - maximum rate of reaction when the enzyme is fully saturated
- extracellular enzymes which worl outside the cell... protease
- intracellular enzymes which work inside the cell... catalyse/helicase
- enzymes are biological catalysts and work by reducing the activation energy
- activation
- co-factors, these are generally inorganic and temporarily
- co-enzymes
- type of cofactor that is organic (temporarily bound)
- prosthetic groups
- type of cofactor that is permanently bound (inorganic)
- co-enzymes
- Organic - contain a carbon molecule
- inorganic - doesn't contain carbon
- co-factors, these are generally inorganic and temporarily
- factors affecting activity
- temperature
- increases kinetic energy which increases amount of successful collisions
- when temperature increases past optimal level, hydrogen bonds break in tertiary structure permanently changing shape and preventing ESC forming
- PH
- hydrogen protons which determine PH interact with bonds holding together tertiary structure
- when the PH is not optimal, being either too low or high, complimentary tertiary strutcure not correct
- low PH (alkaline) - increase in protons
- temperature
- enzyme inhibition
- competitive inhibition
- involves inhibitor binding to active site of enzyme blocking complimentary substrate from forming the enzyme/subsrate complex
- these are temporary - if enzyme concentration or substrate concentration is increased Vmax can still be reached, it will just take longer
- non-competitve inhibitio
- inhibitor binds to allosteric site changing the tertiary structure of enzyme and therefore shape of active site so ESP cannot form
- Permanent change in structure, therefore Vmax may not be achievable
- competitive inhibition
- models
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