Enzymes and Digestive System

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structure of amino acid
carbon atom; amino group; carboxyl group; hydrogen group; R grop
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formatiobn of peptide bonds
condensation reaction of amino acids; water is made by combining carboxyl and hydrogen group; linked by peptide bond of carbon and N
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primary structure
chain of amino acid
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secondary structure
amino group + charge; carboxyl group - charge; coiled; hydrogen bonds
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tertiary structure
alpha helix twisted using bonds
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hydrogen bonds
numerous but easily broken
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ionic bonds
formed between carboxyl and amino groups; easily broken through change in pH
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disulfide bonds
fairly strong so not easily broken
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quaternary structure
prosthetic group; made up of many tertiary structures
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test for protein
buiret test; detects peptide links
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colour turned if peptide bonds are present?
purple; if not blue
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starch digestion- step 1
food chewed into smaller pieces to give a large SA
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step 2
saliva enters mouth and is mixed in with food
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step 3
amylase is secreted in the mouth by the salivary glands, hydrolyses glycosidic bonds to produce disaccharide maltose. Amylase contains mineral salts that keep the pH neutral.
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step 4
food is swallowed; acidic conditions in stomach; acid denatures amylase to prevent hydrolysis of starch
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step 5
food passed into small intestine into staomch; pancreatic juice is created
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pancreatic juice
contains pancreatic amlyase
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step 6
starch is turned into maltose; pancreas is at a high pH
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step 7
muscles in intestine wall push food along small intestine
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step 8
epithelial lining produces maltase; this hydrolyses the maltpse into alpha-glucose
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sucrose
contained in cells; broken down in mouth by teeth
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epithelial lining
produces sucrase; hydrolyses single glycosidic bond to produce glucose anld fructose
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lactose
found in sugar of milk; epithelial lining produces lactase; hydrolyses glycosidic bond to produce glucose and galactase
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enzymes
act as catalysts to alter the rate of reaction without being used up
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equation
sucrose+water=glucose+fructose; hydrolysis; sucrase is enzyme
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colliding
substrate must collide with energy; alters arrangement of atoms; energy of products must be less than those of substrates
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activation energy
initial boost is needed to activate reaction
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lowering activation energy
enzymes lower the activation energy; allows reaction to take place at a lower temperature to normal
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metabolic processes
occur rapidly at body temperature
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enzyme structure
specific 3-D shape; sequence of maino acids; active site is the functioning part of shape; enzyme acts on substrate which fits in active site and is held in place by bonds; enzyme-substrate complex
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lock and key model
fits and operates single lock; substrate only fits one active site; enzymes are specific but does not change shape- does not allow for movement to bind or denature
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induced model fit
hand and glove; structure of enzyme is flexible so that it can mould itself to the substrate; enzyme puts strain on substrate; distorts bond and lowers activation energy
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induced model fit explains
how other molecules can affect enzyme activity; how the activation energy is lowered- colliding causes strain
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affecting factors
physical contact and substrate myst be complementary
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temperature
increases kinetic energy increases collisons
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pH
measure of hydrogen ion concentration; alters charges on amino acid; denatures
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substrate concentration
rate of reaction increases with higher concentrations as enough substrates to fill active sites; when all active sites are full, cannot increase rate anymore
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denature
bonds in enzyme begin to break; active site changes shape; substrate no longer fits active site; can be a permanent change
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how to measure enzyme-catalysed reactions
time course; volume of oxygen produced; reductio in concentration of starvh
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method of measuring enzyme-catalysed reactions
lots of substrate but no product; substrate molecules easily join; active sites fully filled; substrate broken down into its products; substrate decreases- increase product; difficult for substrate to make contact; rate of reaction is lowered
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inhibition
reduce activity by interfering with function
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competitive inhibition
occupies active site; high substrate, lowers effect of inhibitor; substrate can replace inhibitor once it has left
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non-competitive inhibitor
binds to enzyme; alters shape of active site; more likely to permanent; not affected by substrate concentration
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metabolic pathway
series of reaction; each catalysed by enzyme; highly structure; enzyme usually attaches to inner membrane in a precise sequence; use chemical as inhibitor to steady rate of reaction; increased product-increased inhibitors- decrease next reaction
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hydrolysis
+H20; mono to di; photosynthesis
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condensation
-H20; di to mono; respiration
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maltose
glucose+glucose; maltase; twins; glycosidic bonds
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sucrose
fructose+glucose; sucrase; isomer; found in fruits which are fruity
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lactose
galactose+glucose; lactase; not very soluble, role in production of glycolipids; lactose are from out of space
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starch
plants; maltose using amylase, glucose using maltase
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benedict's test
reducing sugar; orange to brown
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buffer
maintains pH of solution
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iodine test
yellow to blue; detect start
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Other cards in this set

Card 2

Front

condensation reaction of amino acids; water is made by combining carboxyl and hydrogen group; linked by peptide bond of carbon and N

Back

formatiobn of peptide bonds

Card 3

Front

chain of amino acid

Back

Preview of the back of card 3

Card 4

Front

amino group + charge; carboxyl group - charge; coiled; hydrogen bonds

Back

Preview of the back of card 4

Card 5

Front

alpha helix twisted using bonds

Back

Preview of the back of card 5
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