enzymes
- Created by: Amber Tyas
- Created on: 20-05-19 11:36
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- Activation energy
- Enzymes
- Anabolic reactions
- where substrates are joined= larger product
- 2 molecules joining are held close together by attaching to enzyme= reduces repulsion
- where substrates are joined= larger product
- Examples of enzymes
- ATP-ase
- Breakdown of ATP producing ADP + phosphate group
- Releases small amount of energy
- Breakdown of ATP producing ADP + phosphate group
- Carboxylase oxidase
- Catalyses the binding of CO2 to ribulose bisphosphate in plants
- Catalase
- The breakdown of hydrogen peroxide to water and oxygen gas
- Catalyst
- Chemical that speeds up ROR remains unchanged and reusable at the end of the reaction
- Catalyst features of enzymes
- Increases ROR, specific to a reaction, unchanged at the end of the reaction, lowers the activation energy.
- Catalyst features of enzymes
- Chemical that speeds up ROR remains unchanged and reusable at the end of the reaction
- Glycogen synthase
- the building up of glycogen by catalysing the joining together of glucose molecules
- GLycogen is the storage carbohydrate of animals
- the building up of glycogen by catalysing the joining together of glucose molecules
- Lactase
- The breakdown of lactose into glucose and galactose monomers
- ATP-ase
- A type of protein that speeds up a chemical reaction in a living thing.
- cofactors
- Some enzymes work only if there is another non protein substance bound to them. No of diff subs that help control reactions at appropriate rates
- Competitive inhibition
- Substances that resemble the normal substrate competes with substrate for active site
- Levels of inhibition depends on relative conc of inhibitor and substrate
- Substances that resemble the normal substrate competes with substrate for active site
- inhibition
- non competitive inhibitor
- Sub that reduces the activity of an enzyme by binding to the allosteric site, changin tertirary structure= change shape of active site= substrate cant bind to it.
- non competitive inhibitor
- inorganic cofactors
- ions not permanently bound to enzyme. They help enzyme and substrate bind+ inc ROR. don't participate in reaction= noy used up/changed. binding of ion= ESC form easier. ions either changes charge distribution or shape of ESC
- where enzymes work
- extracellular
- enzymes work outside the cell, catalysing hydrolysis reactions to break down macromolecules into small soluble molecules to be absorbed
- e.g digestion
- enzymes work outside the cell, catalysing hydrolysis reactions to break down macromolecules into small soluble molecules to be absorbed
- intracellular
- Enzymes that work inside cells, catalysing reactions that occur in series
- E.g photosynthesis and respiration
- Enzymes that work inside cells, catalysing reactions that occur in series
- extracellular
- Anabolic reactions
- Energy needed to start a reaction
- Enzymes reduce this by providing an active site for reactions to be easier.
- Active site
- Indented area on the enzyme thats complementary to the shape of the substrate
- Active site
- Enzymes reduce this by providing an active site for reactions to be easier.
- Enzymes
- Reactions
- Catabolic reactions
- When substrates are broken down
- Fitting into the active site put strain on bonds in the substrate= bond break easier
- When substrates are broken down
- Catabolic reactions
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