8.1 Flashcards

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1
Q

What is a metabolic pathway

A

any chain or cycle of linked reactions catalyses by enzymes

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2
Q

What is an example of a metabolic pathway

A

glycolysis

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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

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4
Q

What is the link reaction

A

When pyruvate forms acetyl CoA

3 carbon atoms to 2 carbon atoms

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5
Q

What happens to pyruvate if oxygen is present

A

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

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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

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7
Q

what is removed in the link reaction

A

a carboxyl group and hydrogen atom is removed from the pyruvate

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8
Q

What is decarboxylation

A

when a carboxyl group si s removed from the process

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9
Q

What is dehydrogenation when hydrogen atoms are removed

A

when hydrogen atoms are removed

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10
Q

what enzyme catalyses decarboxylation and dehydrogenation

A

pyruvate dehydrogenase

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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

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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

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13
Q

What does the decarboxylation and dehydrogenation of pyruvate result in

A

the result of an acetyl group

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14
Q

What does an acetyl group

A

two carbons

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15
Q

What happens at the end of the link reaction

A

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

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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

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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
Q

What is an allosteric site

A

a binding site on the surface of an enzyme other than the active site.

26
Q

Where does the product of the last reaction of an enzyme bind to

A

the allosteric site

27
Q

What does the inhibitor do in non competitive inhibition

A

binds to the allosteric site and blocks the activity of the enzyme

28
Q

What is an example of end product inhibition

A

the synthesis of isoleucine from threonine

29
Q

What happens in allosteric inhibition

A

the binding of the regulatory molecule changes the conformation of the enzyme

30
Q

What is isoleucine

A

an essential amino acid that is consumed from food

31
Q

What happens in the end product inhibition by isoleucine

A

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
Q

What is normally the compound that inhibits the enzyme of the first reaction

A

the end product

33
Q

What is a branch of bioinformatics concerned with

A

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
Q

What is malaria

A

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
Q

how is malaria transmitted

A

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
Q

Which disease is caused by the parasite Plasmodium falciparum?

A

Malaria

37
Q

How do databases identify the potential for new antimalarial drugs

A

Databases with Plasmodium falciparum genome and protein sequence information were used to screen chemicals for possible interactions before starting lab research.

38
Q

How to calculate the rate of reaction

A

1/ time taken in seconds

39
Q

What is the role of isoleucine

A

it is a non-competitive inhibitor

40
Q

Is end product inhibition reversible

A

yes