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27 Cards in this Set
- Front
- Back
What are the two stages of digestion? |
Physical breakdown- teeth, stomach muscles
Chemical breakdown- enzymes |
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What is hydrolysis?
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Splitting up molecules by adding water to the chemical bonds that hold them together
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What enzymes break down carbohydrate, lipids, proteins?
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Carbohydrases
Lipases Proteases |
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What is a monosaccharide?
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The monomers (1 chain organic molecules) of carbohydrates
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Sucrose=
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Glucose + fructose
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Maltose=
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Glucose + glucose
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Lactose=
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Glucose and galactose
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What is a glycosidic bond?
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The bond that bonds two monomers together (eg. Glucose + glucose)
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What is a condensation reaction?
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Making bonds between two monosaccharides by removing H2O
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Give example of Carbohydrases and describe what they do and where the source is
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Salivary amalyse
Break down carbohydrates into sugars Salivary glands |
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Give example of Lipases, what they do and where the source is
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Pancreatic lipase
Break down fats into fatty acids and glycerol Pancreas |
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Give example of proteases, what they do and where is the source
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Pepsin
Break down proteins into amino acids Gastric band in stomach wall |
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Name of enzyme that breaks down lactose
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Lactase
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Describe and explain symptoms of lactose intolerance
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Diarrhoea is a symptom |
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Describe how starch is digested
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Teeth break it into smaller pieces to increase surface area.
Saliva contain salivary amylase, which start hydrolysing starch into maltose. In small intestine, pancreatic juices contains pancreatic amylase continue hydrolysis I starch to moltose because the preview enzymes where denatured in stomach. Finally, lining if small intestine produces maltase, which hydrolyses the maltase into glucose |
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How do enzymes speed up reactions?
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They lower activation energy needed for the reaction to take place
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Why are enzymes specific?
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Their shape of their active site is complementary to the specific substrate
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Describe lock and key model
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Enzymes are specific. The shape of the substrate (key) exactly fits the active site of the enzymes (lock)
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Name a limitation of lock and key model
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Locks are Considered rigid. Enzyme active stores are flexible
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Describe induced fit model
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Enzyme active site changes shape to fit precisely with substrate. The enzyme is flexible. As it changes shape the enzyme creates a particular bond and lowers the activation energy
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What 3 factors effect enzyme action?
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Temperature
PH Substrate concentration |
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What is the primary structure?
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Amino acids bonded by a condensation reaction. This forms a polypeptide chain
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What is the secondary structure?
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The polypeptide spontaneously folds into an alpha helix or a beta plated sheet. Different parts of the chain is held together by hydrogen bonds
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What is the tertiary structure?
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The polypeptide folds again to form a 3d structure.
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What is the quaternary structure?
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Two or more polypeptide chains linked together to form a single complex protein
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Describe and explain competitive inhibition
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The inhibitor is a similar shape to the subtrate. It competes with the substrate for the enzymes active site. This decreases probability that the enzyme will act on substrate, so rate of reaction decreases
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Describe and explain non competitive inhibitors
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Inhibitors attach to enzyme, making the active site shape change. Reaction rate decreases because some enzymes are unable to catalyse any subtrates
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