What role do cofactors play in enzyme catalysed chemical reactions? Flashcards

1
Q

Why are cofactors important

A
  • Some enzymes can only function with a cofactor present.
    *
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What is a cofactor

A
  • A non protein molecule!
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What do co factors do

A
  • The modify the the structure of the enzyme is some way so the enzyme can function more effectively
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What is an example of the way a co factor works

A
  • Amylase catalyses the break down of starch to maltose
  • This reaction can only occur if the co factor Chloride ions (CL-) ions are present
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

What are the 3 types of co factors

A
  • Prosthetic groups
  • Coenzymes
  • Activators
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What are prosthetic groups

A
  • Prosthetic groups are molecules that form permanent attachments to an enzyme
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

What is an example of a prosthetic group

A
  • Haemoglobin
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

What is haemoglobin

A

Haemoglobin has

  • 4 polypeptide chains
  • which are joined together by Disulfide bonds
  • At the centre of each polypeptide chain is an iron containing group called haem (A prosthetic group)
  • Each of these Haem prosthetic groups has an iron ion Fe2+
  • As each Iron ion can bind with one molecule of oxygen (O2), there are 4 molecules of oxygen
  • This protein combines with the prosthetic group forming a cojugated protein.
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

What is the metabolic role of haemoglobin

A
  • Haemoglobin picks up O2 in the lungs forming oxyhaemoglobin
  • Oxyhaemoglobin is broken down (dissacociates) in the tissues giving up its oxygen, and then reverts back to haemoglobin.
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What cofactor does carbonic acid collaborate with

A

Carbonic anhydase collaborates with a zinc based co factor (ZN2+)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

What role does carbonic anhydrase play in the blood?

Car bon ic

An hy drase

A
  • Carbonic anhydrase plays a critical function in the blood…
  • Carbonic anhydrase catlyses the combination of water and dioxide
  • Forming carbonic acid
  • Which enables carbon dioxide to be transported in the blood
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

What are co enzymes

A
  • Co enzymes are smal nonprotein organic molecules are not permanently attached to the enzyme (Unlike prosthetic co factors)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

What do co enzymes do?

A
  • Co enzymes help certain enzymes and substrates to bond with each other
  • NB: Where a co enzyme is needed to catlyse a reaction, the enzyme can only function when it is present.
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

What are many enzymes derived from

A
  • Vitamins
    • e.g. The coenzyme NAD is derived from the vitamin nicotinic acid
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q
A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

What is NAD the coenzyme for

A
  • It is the coenzyme for a number of dehydrogenase enzymes
  • It acts as a hydrogen receptor
17
Q

What are activators

A
  • Activators are inogranic metal ions
    • e.g. Magnesium Mg2+, Iron Fe2+, Calcium Ca2+
18
Q

What is the function of activators

A
  • Activators form a temporary attachment to the enzyme…and change the active site….to increase the probability that a reaction will occur
19
Q

What are examples of activators

A
  • Protein synthesis cannot occur without magnesium present as a co factor
  • Muscle contraction and nerve impulses cannot happen without calcium present as a co factor
20
Q

Where do most metal activators come frome

A
  • Diet