Enzymology Flashcards

1
Q

What is catabolism?

A

Large molecules broken down in smaller ones
releasing energy

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2
Q

What is Anabolism?

A

Small molecules being assembled into larger ones
Using energy

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3
Q

What do cells need to carry out metabolic reactions?

A

supply of oxygen and nutrients

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4
Q

Where is oxygen absorbed into?

A

Lungs

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5
Q

Where are nutrients and other materials obtained?

A

Digestive tract

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6
Q

what does primary structure consist of?

A

Amino acids and peptide bond

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7
Q

Why does secondary structure fold?

A

Hydrogen bonds

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8
Q

Why does a tertiary structure have secondary folding?

A

Interaction within the polypeptide and it’s immediate environment

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9
Q

What is a quaternary structure

A

Relationships between individual subunits

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10
Q

In enzyme- catalysed biochemical reactions, what molecule is being acted upon?

A

substrate

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11
Q

In enzyme- catalysed biochemical reactions, what molecule is formed

A

product

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12
Q

What molecule supports enzymes when they are unable to act of their own?

A

Co-factors

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13
Q

What does a cell have many thousands of?

A

enzymes

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14
Q

What can enzymes do?

A

Be manufactured by it’s cell when required
Be regulated- switched on and off
Speed up reactions

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15
Q

What does activation energy do?

A

Makes conditions favourable for the reaction to occur

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16
Q

Are enzymes able to lower their activation energy?

A

yes, if conditions are favourable

17
Q

What are the two types of enzyme substrate complex?

A

Lock and key model
Induced fit model

18
Q

What factors affect enzyme activity?

A

Substrate concentration
temperature
pH
Enzyme molecule concentration

19
Q

What is the effect of a low substate concentration

A

Collisions are infrequent and products made slowely

20
Q

What is the effect of a medium substrate concentration?

A

Increase collisions
reaction rate will increase proportionately

21
Q

What is the effect high substrate concentration

A

enzymes working at maximum capacity
further increases will have no effect
enzyme is saturated

22
Q

What happens to enzymes when the temperature increases too much?

A

enzyme will denature

23
Q

What effect does altering pH have?

A

Affect charges of amino acids
affects critical 3D structure
affects activity of molecules within the active site

24
Q

What is a non-competitive inhibitor?

A

an inhibitor that targets the enzyme at other points, rather than the active site

25
Q

What occurs briefly when an enzyme binds with their substrate?

A

become susceptible to inhibition

26
Q

Why do inhibitors bind reversibly to the active site?

A

to reduce access of the substrate to the enzyme

27
Q

What is one type of inhibitor?

A

Cyanide

28
Q

What are the symptoms of cyanide poisoning?

A

Stomach cramps
Headache
nausea and vomiting
Cardiac arrest
Respiratory failure
Coma
death

29
Q

What are the different types of enzymes?

A

Lactase
Sucrase
Maltase
Glucoamylase
Protease
Lipase
Cellulase

30
Q

What does the enzyme lactase do?

A

Break down lactose (milk sugars)

31
Q

What does the enzyme sucrase do?

A

digest complex sugars and starches

32
Q

what does the enzyme maltase do?

A

Digest disaccharides to monosaccharides (malt sugars)

33
Q

What does the enzyme glucoamylase do?

A

Break down starch to glucose

34
Q

What does the enzyme protease do?

A

Break down proteins found in meats, nuts, eggs and cheese

35
Q

What does the enzyme lipase do?

A

Breaks down fats found in most dairy products, nuts oils and meat

36
Q

What does the enzyme cellulase do?

A

Breaks down cellulose, plant fibre (not found in humans)