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15 Cards in this Set
- Front
- Back
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biochemical pathway |
chain of chemical reactions occurring in a cell |
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Why are enzymes important in body |
lower activation energy and catalyse reactions at a faster rate to sustain life |
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why is enzyme SO BIG compared to active site? |
to prevent free water molecules from watery media to bind to active site (protection) - as globular |
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active site |
specialised region formed by polypeptide chains into which the substrate fits |
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why can lipase split fats of various kinds into fattyacid and glycerol? (not specific) |
as all fats have SAME ESTER BOND |
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substrate binding amino acids |
R groups lining active site thats concerned in specific binding/orienting of substrate (other amino a. in active site = catalytic amino acid) |
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interactions that help substrate to bind |
- electrostatic interaction - hydrogen bonding - van der waals interaction - hydrophobic interaction |
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coenzyme |
non protein (vitamin), organic connects to apoenzyme (inactive) = holoenzyme |
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cofactor |
- ion - NOT organic - temporary |
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denaturation |
the change of tertiary structure that inhibits the enzymes ability to function |
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change in pH effect |
alter in state of ionisation of charged amino acids, so binding between active site and substrate no longer occur. |
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high substrate conc. effect |
= more collision btw molecules, thus more likely to encounter reactants (limited by enzyme) |
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reason for plateau in high substrate conc. |
system becomes saturated = all enzymes are working constantly |
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diff between reversible and irreversible inhibitors |
reversible: non-covalent interaction (H bond) irreversible: covalent |
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place where non-competitive inhibitor binds |
allosteric site |
