Chapter 4- Enzymes Flashcards

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1
Q

What is an enzyme?

A

An enzyme is a biological catalyst (re-usable) that speeds up metabolic reactions in living organisms without changing the end product.

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2
Q

Define Anabolic and Catabolic:

A
  • Anabolic: involved in synthesis (make muscles, ligaments, cell structures, they build by joining AAs and carbo. together)
  • Catabolic: hydrolysis types of reactions (digestion, breaks down e.g. lysosomes contain powerful hydrolytic enzymes)
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3
Q

Draw the graph for Enzyme Action, and explain why reactant energy begins at a figure above 0.

A
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4
Q

How is activation energy lowered by a catalyst?

A
  • If 2 substrate molecules need joining?
  • enzyme holds them together so they can bond easily = synthasase
  • If enzyme is catalysing breakdown?
  • Fitting into Active Site puts strain on bonds of substrate so they can be broken down easily = hydrolytic.
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5
Q

What is an intracellular enzyme?

A

Made + retained inside the cell.

E.g. Catalase - breaks down hydrogen peroxide into water + oxygen. (catalase is 1 of the fastest enzymes in body, has ‘high turnover number’, no.molecules catalysed per min = 5.6 million!!!

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6
Q

What is an extracellular enzyme?

A

E.g. Amylase - works outside of cells.

Amylase- works in saliva to catalyse hydrolysis of starch into maltose.

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7
Q

What is the structure of enzymes?

A
  • Globular Proteins
  • 3D shape, almost spherical
  • Soluble in water due to position of hydrophobic / hydrophilic R groups
  • Contain an ACTIVE SITE
  • specific shape (complementary to substrate)
    • Where substrate binds to
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8
Q

Describe the lock and key hypothesis of enzymes:

A
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9
Q

Describe the induced fit theory on enzymes:

A
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10
Q

According to the Induced Fit Theory, how does the active site change its shape slightly to fit the substrate?

A

Align the changed ‘R’ groups (H bonds form between delta+ and delta-)

so the attractions temporarily form H bonds and ionic bonds

Causes AS to change shape so not based on shape alone.

Although shape of Active Site should be mostly complementary to substrate.

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11
Q

How does temperature affect enzymes. Draw a graph and explain:

A
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12
Q

What is the temperature Q10 coefficient?

A
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13
Q

How does pH affect enzymes?

A
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14
Q

What are inorganic cofactors?

A
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15
Q

What are organic cofactors?

A
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16
Q

What are the two types of inhibition?

A
17
Q

what are prosthetic groups?

A
18
Q

Draw the inhibitors graph:

A
19
Q

What is the abbreviation for Enzyme-Inhibitor Complex:

A

EHC

20
Q

Describe Reversible and Irreversible inhibition and how they are different.

A

Reversible: Weaker H-bonds or weak ionic bonds. The inhibitor can be removed.

Irreversible: Strong Covalent Bonds, the inhibitors cannot be easily removed.

21
Q

What is Cytochrome C?

A

A group of enzymes that work together- found in respiration + photosynthesis.

22
Q

Describe how Snake Venom acts as an inhibitor:

A
23
Q

Describe how Cyanide Poisoning act as an inhibitor response:

A
24
Q

Describe how Medicinal Inhibitors such as antifreeze work as an inhibitor?

A
25
Q

Just look at this card on end-point inhibition.

A
26
Q

Define ‘denaturing’:

A

Denature- change in tertiary structure of protein/enzyme resulting in loss of normal function.

27
Q

What is Vmax?

A

Vmax = maximum initial velocity / rate of enzyme-catalysed reaction.

28
Q

What is co enzyme A?

A

A co enzyme with important roles in oxidation of pyruvate in Krebs - Cycle + synthesis + oxidation of fatty acids.