Enzyme Regulation Flashcards

1
Q

The cell needs to be able to regulate:

A
  • when a reaction occurs

- how much product is produced from a reaction

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

Why does enzyme activity need to be regulated?

A

so that they function at the proper time and place

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

Name 5 ways enzyme activity is regulated

A
  1. controlling the amt of enzyme present
  2. allosteric regulation
  3. feedback regulation
  4. produce enzyme in an inactive form (zymogen or proenzyme)
  5. covalent modification
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What determines enzyme quantity?

A

rate of synthesis and breakdown of enzyme

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

The quantity of an enzyme may be :

A
  • increased by raising its rate of synthesis

- or decreased by lowering its rate of synthesis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

An allosteric enzymes has another

A

binding site

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Effector molecules change the activity of an

A

allosteric enzyme by binding to the other site

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

Some effectors

A
  • speed up enzyme action (positive effectors)

- slow down enzyme action (negative effectors)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Allosteric effectors can be

A

products, substrate, and so on

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

If too much product is created the enzyme may be shut off by an

A

intermediate becoming an allosteric inhibitor

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

Feedback inhibition is a

A

common form of enzyme regulation in which the product inhibits the enzyme

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

A zymogen is

A

an enzyme produced in an inactive form

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Zymogens (proenzymes) are converted to their active form when

A

needed by removing a part of the zymogen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Wha’ts an example of zymogens?

A

the digestive enzymes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Covalent modification

A

adding/removing groups-like phosphate groups

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Phosphate groups are located at the OH of

A

serine
threonine
tyrosine

17
Q

Isozymes

A

enzymes catalyzing the same biochemical reaction

18
Q

Isozymes have

A

different chemical composition and are found in different tisues
e.g. LDH lactate dehydrogense and CK creatine kinase

19
Q

2 different polypeptide chains (M and B) combine to give 3 isozymes:

A

CK-MM (muscle)
CK-MB (heart)
CK-BB (brain)

20
Q

Enzymes are released from

A

injured tissue into blood

21
Q

If CK-MB is found in the blood stream,

A

this suggest myocardial infarction

22
Q

Some isozymes in blood are indicative of

A

tissue damage, used for clinical diagnosis

23
Q

Increase in serum levels of H4 relative to H3M are

A

indicative of myocardial infarction (heart attack)