2.4 Enzymes Flashcards

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1
Q

What are the physical features of enzymes?

A
  • Globular proteins- Spherical with lots of alpha helix
  • Generally soluble in water due to R groups
  • Biological catalysts
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2
Q

What is the definition of activation energy?

A
  • Minimum amount of energy required for a reaction to take place
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3
Q

How do enzymes work?

A

Reduce activation energy through complimentary fit between enzyme and substrate.

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4
Q

What is the induced fit hypothesis?

A

That there is a change in shape of the enzyme in response to a substrate binding

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5
Q

What are the steps of the induced fit hypothesis?

A
  1. Substrate collides with active site
  2. Enzyme molecule;e changes shape slightly so active site fits more closely around substrate
  3. Enzyme substrate complex formed **
  4. Destabilises substrate producing product
  5. Enzyme product complex formed
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6
Q

What is meant by the term ‘anabolic reactions’?

A

Build up larger molecules e.g. protein synthesis

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7
Q

What are catabolic reactions?

A

Break down larger molecules

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8
Q

What are intracellular enzymes?

A

Act within cells e.g. synthesis of polymers

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9
Q

What are extracellular enzymes?

A

Make substrates outside of cells
Released from cells

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10
Q

What do extracellular enzymes allow for?

A

Use of polymers
Single cell use it to absorb glucose

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11
Q

How is starch digested?

A

Starch polymers are broken down into maltose by amylose in saliva
Maltose is broken down into glucose in small intestine

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12
Q

How are proteins digested?

A

Trypsin is a protease which catalyses digestion of proteins into smaller peptides
Broken down further into amino acids
Trypsin is produced in pancreas

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13
Q

What is the effect of temperature on enzymes?

A

Kinetic energy causes bonds to vibrate
More likely to collide successfully

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14
Q

What happens to enzymes if temperatures goes to high?

A

Bonds vibrate too much and break causing enzymes to lose 3D shape and denature

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15
Q

What does denature mean?

A

Enzyme has permanently changed shape

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16
Q

What are thermophiles?

A

Living organisms adapted to withstand hotter temperatures?
Enzymes are more stable and more resistant to change

17
Q

What are cryophiles?

A

Enzymes that function in very cold environments.
Enzymes have more flexible structures and are less stable

18
Q

What is the effect of pH on enzymes?

A

H + ions interact with polar groups and charged R groups where bonds break and substrate no longer fits active site

19
Q

What is renaturation?

A

Where if pH of solution returns to optimum enzymes will return to original shape

20
Q

What is V max?

A

Maximum rate of reaction
All active sites are occupied by substrate particles

21
Q

What is the effect of increasing substrate concentration?

A
  • Increases number of collisions between enzymes and substrate
  • Increases number of enzyme substrate complexes which in turn increases rate of reaction
22
Q

How can V max be increased?

A

Increasing the limiting reactant or temperature e

23
Q

What is the effect of increasing enzyme concentration?

A
  • Increases number of active sites available
  • Increases number of enzyme substrate complexes increasing rate of reaction
24
Q

What is an inhibitor?

A

Any substance/molecule that slows down the rate of an enzyme controlled reaction by affecting the enzyme molecule

25
Q

What are competitive inhibitors?

A
  • Similar shape to substrate
  • Occupy active site to form enzyme-inhibitor complexes
  • number of enzyme substrate complexes decreases causing rate to decrease
  • Most don’t bind permanently
26
Q

What are non competitive inhibitors?

A
  • Bind elsewhere on the enzyme at the allosteric site
  • Affects tertiary structure
  • Level of inhibition depends on concentration of inhibitor
  • Many bind permanently
  • Used in insecticides
27
Q

What is an allosteric site?

A

Another binding point on an enzyme

28
Q

What is end product inhibition?

A

Product of one reaction is an inhibitor to the enzyme that produced it

29
Q

What are co-factors?

A

Non protein components
Bind temporarily at allosteric site
Obtained from diet e.g. Fe +

30
Q

What are co-enzymes?

A
  • Organic co-factor
  • Many derived from vitamins e.g. NAD
  • Carry chemicals between enzymes.
31
Q

What are prosthetic groups?

A
  • Also a cofactor
  • Bind permanently
32
Q

How are enzymes activated?

A
  • Need a change in tertiary structure
  • Can be activated either by co factors or a change in pH