1.7, 1.8, 1.9: Enzyme Action Flashcards

1
Q

Enzymes

A

Speed up chemical reactions by acting as biological catalysts

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2
Q

Intracellular

A

within cells

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3
Q

Extracellular

A

outside cells

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4
Q

What are enzymes made of

A

Proteins

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5
Q

Activation energy

A

A certain amount of energy is needed to be supplied to the chemicals before the reaction will start

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6
Q

Enzymes … the activation energy

A

lower

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7
Q

What does the active site bind to

what does it form

A

substrate

enzyme-substrate complex (ESC)

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8
Q

reasons why ESC lowers actiation energy

A

= substrate molecules attached to the enzyme stay closer together which reduces any repulsion so they can bond more easily
=fitting into the active site puts a strain on the bonds in the substrate so they break up more easily

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9
Q

Older enzyme model

A

Lock and key model

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10
Q

New evidence to alter view of lock and key model

A

ESC changes shape slightly to complete the fit = locks the substrate even more tightly into the enzyme

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11
Q

More recent enzyme model

A

Induced fit model

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12
Q

Induced fit model

A

Helps to explain why enzymes are so specific and only bond to one substrate.
The substrate makes the active site change shape

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13
Q

Tertiary structure of enzyme determines…

A

the shape of the active site

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14
Q

Different enzymes have

A

different tertiary structures = different shaped active sites

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15
Q

Alteration to tertiary structure of an enzyme means…

A

Shape o the active site changes
substrate won’t fit
no ESC
enzyme can’t carry out its function

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16
Q

What affects the tertiary structure of enzymes

A

pH or temp changes

17
Q

How does a gene mutation affect the tertiary structure of the enzyme produced?

A

Gene mutation = amino acids sequence changes = primary structure different = tertiary structure different

18
Q

Competitive inhibitors

shape

A

Have a similar shape to substrate molecules

19
Q

Competitive inhibitors

how do they work

A

Compete with substrate molecules to bind to the active site but no reaction occurs and the active site is blocked

20
Q

Competitive inhibitors

Amount of enzyme inhibited

A

depends on relative concentrations of inhibitors and substrates

21
Q

Non-competitive inhibitors

A

Non-competitive inhibitors molecules bind to the enzyme away from its active site

22
Q

Non-competitive inhibitors

how do they work

A

Causes active site to change shape so substrate molecules can’t bind to it

23
Q

Non-competitive inhibitors

Amount of enzyme inhibited

A

Increasing substrate conc. won’t affect the ROR. = enzyme activity will still be inhibited

24
Q

Measuring the rate of an enzyme controlled reaction

2 methods

A

Measure hoe fast the product is made

Measure how fast the substrate is broken down

25
Enzyme controlled reaction results show in
line graphs
26
Calculating the initial rate of reaction
Tangent