Karteikarten
4. Enzymes
Karten in diesem Stapel (10)
- 1What is metabolism, and it's different forms?Reactions of the body
Anabolic - building molecules up
Catabolic - breaking molecules down - 2Key characteristic of enymesGlobular proteins, biological catalysts - lower activation energy of a reaction (min energy required for molecule to react)
work Intracellularly or extracellularly - 3StructureLock and key mechanism - active site and substrate = enzyme-substrate complex
- 4What's induced fit?Active site changes shape to accommodate the substrate, bringing the reactive groups of enzyme and substrate closer together.
e.g. lysozyme and anti-bacterial enzyme. - 5Effecting factors1. Temp - higher = more KE = higher ror, too high - denatures, breaking bonds, changing shape. Too low = inactive
2. pH - highest ror is at optimum, small alterations = reversible, inactivation, extremes = denaturing (low pH, excess H+ neutralise -, high pH, excess OH-, neutralise +)
3. Substrate concentration - higher = ror, limiting factor, saturated, plateaus
4. Enzyme concentration - 6How do competitive inhibitors work?Structurally similar to substrate, associates with as
- 7How do non-competitive inhibitors work?Combines to allosteric site away from as, alters shape e.g. potassium cyanide
- 8How are enzymes immobilised?Fixed/ trapped to inert matrix, e.g. alginate beads/ gel membrane - provides stability so high temp and pH can be used without altering as shape.
- 9Advantages of IEProducts not contaminated
Easily recovered for reuse
Small no of enzymes can be used - 10Examples of IE in action1. Lactose-free milk, lactase in enzyme binds to lactose, hydrolysed into glucose and galactose
2. Biosensors - turn chemical signal into electrical signal and detect.
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- Beschreibung
- A level Biology AS Karteikarten am 4. Enzymes, erstellt von Becky Hemming am 30/05/2017.
- Erstellt von
- Becky Hemming
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