Cofactors and coenzymes Flashcards

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1
Q

What is a cofactor?

A

A non-protein which, alongside a protein, enzymes consist of

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2
Q

How do cofactors bind?

A

Loosely to the enzyme or form part of the active site to activate them

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3
Q

What do cofactors do?

A

They help the enzyme to carry out it is function by transferring atoms or groups from one reaction to another in a metabolic pathway

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4
Q

What are the two types of cofactors?

A

Organic or inorganic

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5
Q

How are inorganic cofactors taken in?

A

Through the diet as mineral ions

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6
Q

What are examples of inorganic cofactors?

A

Zinc, iron, calcium and chloride ions

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7
Q

What is an example of how inorganic cofactors are used?

A

Amylase, which breaks down starch to maltose, needs the chloride ion to help form the correct shape of the active site

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8
Q

What is another name for organic cofactors?

A

Coenzymes

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9
Q

Where are coenzymes derived from?

A

From vitamins such as Vitamin B3 which is used to synthesis the coenzyme NAD (nicotinamide adenine dinucleotide)

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10
Q

What does NAD do?

A

It transfers hydrogen atoms between molecules in the reactions in respiration

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11
Q

How is NAD needed?

A

The enzyme alcohol dehydrogenase needs NAD to transfer hydrogen in the conversion of ethanal to ethanol in anaerobic respiration

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12
Q

What is an example of a vitamin used to make a co-enzyme?

A

Vitamin B5 is used to make co-enzyme A which is essential in the breakdown of fatty acids and carbohydrates in respiration

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13
Q

What are prosthetic groups needed for?

A

They are required by enzymes to carry out their function so are a type of cofactor

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14
Q

How do prosthetic groups bind?

A

They are permanently and tightly bound to the enzyme

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15
Q

What is an example of a prosthetic group?

A

Carbonic anhydrase is involved in the metabolism of carbon dioxide and it has a zinc ion, forming an important part of its structure

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16
Q

What is an apoenzyme?

A

An enzyme in its inactive form how thy are often made

17
Q

What is a holoenzyme?

A

An activated enzyme

18
Q

What is an example of enzyme activation?

A

A protease enzyme is used to activate the inactive form of another enzyme by chopping through bonds in the protein

19
Q

What is the inactive precursor of an enzyme called?

A

A zymogen or proenzyme

20
Q

How are enzymes activated by temperature or pH?

A

The surrounding temperature or pH may have to change to activate an an enzyme which changes the tertiary structure

21
Q

What is an example of pH activation?

A

Pepsinogen is released into the stomach to digest protein in its inactive form and the acid in the stomach activates the proenzyme turning it into pepsin (the active form)

22
Q

What is thrombin?

A

An enzyme which catalyses the conversion of fibrinogen (factor I), a soluble plasma protein, into a long, sticky thread of insoluble fibrin

23
Q

What do fibrin threads form?

A

A mesh that traps platelets, blood cells and plasma

24
Q

How do you calculate rate using end point?

A

You divide the time to get the rate

25
Q

What are the units of rate?

A

s⁻¹