Many Proteins Are Enzymes Flashcards

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1
Q

How do enzymes speed up a reaction

A

Provide an alternate pathway with a lower activation energy

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2
Q

What type of catalyst are enzymes

A

Biological

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3
Q

Are enzymes proteins

A

Yes

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4
Q

What is the lock and key model

A

Shape of the active site doesn’t change when substrate binds

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5
Q

What is the induced fit model

A

Tertiary structure of the enzyme changes as substrate approaches so active site fits around substrates

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6
Q

What structure proteins are enzymes

A

Tertiary

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7
Q

What is the key word to always through in for a mark when talking about enzymes

A

Enzyme substrate complex

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8
Q

Explain in words
Temperature - rate of reaction increasing

A

Increasing kinetic energy of substrate and enzyme
Increases chance substrate collide with active site
Increase frequency = increase rate of reaction

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9
Q

Explain in words
Temperature - optimum temperature

A

Maximum number of collisions between active site and enzyme

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10
Q

Explain in words
Temperature - rate of reaction decreases
Enzymes

A

Higher temperature enzymes vibrating more rapidly
Causes bonds E.g. hydrogen bonds to break
Tertiary structure changes
Substrate no longer fits active site
Denatured

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11
Q

Can a denatured enzyme return to original shape

A

No
Denaturing is permanent because tertiary structure changed

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12
Q

What does the PH depend on

A

Concentration of H+ ions

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13
Q

High PH has a …. Concentration of H+
Low PH has a …. Concentration of H+

A

Low
High

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14
Q

What happens if PH is do low or high on enzyme detailed x3

A

Interfere with the charges in amino acid
This breaks bonds changing tertiary shape of enzyme
Change active site

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15
Q

What does a competitive inhibitor do

A

Similar shape to substrate
Bonds to active site and occupies it
Prevents substrate from binding

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16
Q

How to reduce effect of competitive inhibitor

A

Increase substrate

17
Q

Does a reaction happen with a competitive inhibitor

A

No
It’s not the substrate

18
Q

How do non-competitive inhibitors work

A

Bind to allosteric site
Tertiary structure of enzyme changes - active site changes no longer complementary to substrate
Less enzyme-substrate complex’s formed

19
Q

How to limit effect of non-competitive inhibitor

A

Increasing substrate has NO effect
Can’t do anything

20
Q

Why is an answer given to a whole number when using a ruler to measure

A

Reduces uncertainty

21
Q

Describe how an enzyme can be phosphorylated

A

Attachment of a phosphate
Released from hydrolysis of ATP

22
Q

Explain how the active site of an enzyme causes a high rate of reaction.

A

Lowers activation energy
Induced fit causes active site of enzyme to change
So enzyme-substrate complex causes bonds to break

23
Q

Formation of enzyme-substrate complex increases rate of reaction
Explain how x2

A

Lowers activation energy
Due to bending bonds
( because of induced fit model the bonds have to bend to fit around substrate)

24
Q

Explain how chemical X binding to an enzyme could increase the rate of reaction

A

( if it is increasing rate of reaction it is NOT an inhibitor)
Binding alters tertiary structure of enzyme
This cause active site to change shape
More Enzyme-substrate complexes formed