Karteikarten
enzymes
Karten in diesem Stapel (15)
- 1anabolic reactionbuilding up molecule
e.g. protein synthesis - 2catabolic reactionbreaking down of molecule
e.g. digestion - 3make up of enzymesThere are tertiary globular proteins that work as a catalyst Each enzyme has its own sequence of amino acids and is held in shape by hydrogen, disulphide and ionic bonds
- 4enzymes propertiesto speed up reaction
are not used or changed
and a high turn over number
only speed up reaction it does not create them - 5active siteenzyme act on substrate forming a enzyme substrate complex when the reaction is complete the particle split and separate
- 6lock and key modelever enzyme have a different shape of active site which only work with certain reaction
- 7lysozyme and the induced fit modelthat enzyme shape alter slightly according to substrate
- 8activation energyenzyme like all catalyst lower the activation energy allowing the reaction to happen with less energy
- 9effects on temperatureon average the rate of reaction will increase with increase in temperature reaching its optimal but if it goes to high they denature and completely stop working (kinetic energy - move quicker and increase the chance of molecules colliding)
- 10effects of pHsome enzyme prefer different pHs and can denature if you go a small way outside the narrow optimum range that enzymes work within ie too acidic or too alkali
- 11competitive inhibitorThese are molecules that have a complementary shape to the active site and take the place of the substrate. They are affected by substrate concentration . e.g. SUCCINIC DEHYDROGENASE (KREBS CYCLE)
- 12substrate concentrationif the is no increase in enzyme but an increase in substrate the rate of reaction will increase because there is more chance in the substrate hitting the enzyme but eventually the rate must stop increasing because all the active sites are full
- 13enzyme concentrationincreasing the enzyme concentration will increase the rate of reaction because the is a higher chance of the enzyme colliding with the substrate
- 14non competitive inhibitionthe inhibitor attaches its self to a part of the enzyme away from the active site and changes the shape of the molecule also changing the active site so it no longer can bind with the substrate. Increase in concentration of SUBSTRATE does not effect rate of reaction eg.CYANIDE a respiratory inhibitor
- 15immobilised enzymesenzyme are fixed ,bound or trapped on a inert matrix then put in glass columns where the substrate is then flow though it and bind with the active site but the substrates do not get contaminated
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- Beschreibung
- Karteikarten am enzymes, erstellt von ffavill am 26/04/2016.
- Erstellt von
- ffavill
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