Enzymes/enzyme action Flashcards

1
Q

what are enzymes?

A

biological catalysts that speed up the reaction by lowering the activation energy of a reaction without being used up

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2
Q

why are enzyme shighly specific?

A

because of their tertiary structure

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3
Q

what does the locke and key model state?

A

the substrate fits into the enzyme like a key and a lock - the active site is an exact fit

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4
Q

why does the induced fit model go against the landk model?

A

it states that enzymes arent an exact fit - the active site changes shape as the substrate binds to fit = forming es complexes

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5
Q

what are the three factors that affect enzyme activity?

A
  1. Temperature 2.Ph 3. Enzyme conc 4. Sub conc
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6
Q

Temp. increase in temp

A

increase in temp = increases the rate of reaction - more kinetic energy/more molecules have the activation energy = more successful collisions between the AS and Substrate = ES complexes

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7
Q

Temp above opt temp

A

vibrations break the hydrogen bonds - alters the tertiary structure, so it changes the shape of the active site = the enzyme is denatured

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8
Q

How does Ph affect enzyme activity

A

opt ph - the h+ and OH-ions interact with the ionic and hydrogen bonds/affecting the tertiary structure
= enzyme becomes denature

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9
Q

how does enzyme conc/sub conc

A

increase in enzyme conc increase the rate reaction, successful collisions with substrate molecules (vice versa), forming more es complexes
- reaches the saturation point - when all the substrate molecules are used up, so further increase has no effect.

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10
Q

what are the two types of inhibitors?

A
  1. competitive

2. non competitive

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11
Q

What are competitive inhibitors? 2 points

A
  • similar shape to the substrate molecules

- compete with the sub to bind to the AS, block the sub molecule and prevent the normal reaction from taking place

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12
Q

what are non competitive inhibitors?2 pointd

A
  • different shape to sub molecule

- bind to the enzyme away from the AS, changing the shape of the AS, the sub can’t bind to the AS

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