8.1 Flashcards

1
Q

What is a metabolic pathway

A

any chain or cycle of linked reactions catalyses by enzymes

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

What is an example of a metabolic pathway

A

glycolysis

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

What is a link reaction

A

when metabolic pathways are linked to other pathways such as how glycolysis is linked to the Krebs cycle

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

What is the link reaction

A

When pyruvate forms acetyl CoA

3 carbon atoms to 2 carbon atoms

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

What happens to pyruvate if oxygen is present

A

it is transported into the mitochondrial matrix for the next stages of respiration

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

What takes place in the link reaction

A

conversion of pyruvate of a two carbon acetyl and takes place in the mitochondrial matrix

3 carbon forms two carbon

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

what is removed in the link reaction

A

a carboxyl group and hydrogen atom is removed from the pyruvate

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

What is decarboxylation

A

when a carboxyl group si s removed from the process

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

What is dehydrogenation when hydrogen atoms are removed

A

when hydrogen atoms are removed

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

what enzyme catalyses decarboxylation and dehydrogenation

A

pyruvate dehydrogenase

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

What happens when the carboxyl groups is removed from the pyruvate

A

Two carbons are produced in the acetyl final product

carbon dioxide as a product

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

What happens when the hydrogen atoms are removed from the pyruvate

A

they are accepted by NAD

NAD is reduced into NADH +H

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

What does the decarboxylation and dehydrogenation of pyruvate result in

A

the result of an acetyl group

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

What does an acetyl group

A

two carbons

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

What happens at the end of the link reaction

A

the two carbon acrylic combines with Coenzyme A (CoA) forming Acetyl - CoA

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

What is the activation energy

A

the minimum energy that reacting particles need to possess in order for a reaction to take place

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

A metabolic pathway

A

begins with a particular substrate, terminates with an end product and has many steps in between

18
Q

What are two types of enzyme inhibitors

A

competitive and non-competitive

19
Q

What does a competitive inhibitor do

A

competes with the substrate for the same active site

20
Q

What does the non-competitive inhibitor do

A

buns at a site away from the active site - allosteric site - altering the shape of the enzyme

21
Q

How is the maximum rate of reaction different with each inhibitor

A

with competitive inhibition, the rates eventually the same, as the substrate concentration increases, the rate will increase because there is more available substrate than the inhibitor

in non competitive inhibition, the rate levels off and never reaches the same level because all the enzyme molecules are effectively blocked from reaction with the substrate due to modification of their active site.

22
Q

compare competitive and non-competitive inhibitors

A

chemically similar to the substrate - it has no similarity to the substrate

it binds to the active site of the enzyme - it binds to the enzyme at a site other than the active site

binding of the inhibitor does not modify the active site - binding of the inhibitor modifies the active site `

as the concentration of the substrate is increased, the effect of the inhibitor on the reaction is reduced - increasing the concentration of the substrate does not decrease the impact of the inhibitor, therefore the rate of reaction is lower than normal at all substrate concentrations

23
Q

What can reduce the effect of competitive inhibition of an enzyme?

A

increasing the substrate concentration

24
Q

What usually happens in end product inhibition

A

the enzyme that catalyses the first reaction o the pathway are allosterically inhibited by the end product of the pathway

25
What is an allosteric site
a binding site on the surface of an enzyme other than the active site.
26
Where does the product of the last reaction of an enzyme bind to
the allosteric site
27
What does the inhibitor do in non competitive inhibition
binds to the allosteric site and blocks the activity of the enzyme
28
What is an example of end product inhibition
the synthesis of isoleucine from threonine
29
What happens in allosteric inhibition
the binding of the regulatory molecule changes the conformation of the enzyme
30
What is isoleucine
an essential amino acid that is consumed from food
31
What happens in the end product inhibition by isoleucine
Normal pathway, threonine goes to its enzyme threonine deaminase and continues to each enzyme after that. Isoleucine can then bind to the enzyme that catalyses the first step of the pathway in a non-competitive way, binding allosterically to the enzyme and changing its conformation of the active site. As a result, the substrate can no longer bind to the enzyme
32
What is normally the compound that inhibits the enzyme of the first reaction
the end product
33
What is a branch of bioinformatics concerned with
the binding of certain compounds to target sites meaning, if a chemical binds to a receptor, or another part of the cell wall of a parasite, bacterium or the proteins coat of a virus may change the infectivity of the pathogen or a chemical and an enzyme of a metabolic pathway, or with an enzyme in the metabolism of nucleic acids
34
What is malaria
a disease caused by a parasite, a major health issue that causes the deaths of over 400 000 people every year, mostly children under five years of age in developing countries.
35
how is malaria transmitted
from an infected person to another by blood sucking mosquitos, the malarial parasites invades the red blood cells and feeds on the proteins of these cells
36
Which disease is caused by the parasite Plasmodium falciparum?
Malaria
37
How do databases identify the potential for new antimalarial drugs
Databases with Plasmodium falciparum genome and protein sequence information were used to screen chemicals for possible interactions before starting lab research.
38
How to calculate the rate of reaction
1/ time taken in seconds
39
What is the role of isoleucine
it is a non-competitive inhibitor
40
Is end product inhibition reversible
yes