1.7, 1.8, 1.9: Enzyme Action Flashcards

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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
Q

Enzyme controlled reaction results show in

A

line graphs

26
Q

Calculating the initial rate of reaction

A

Tangent