Lecture 6 - Nitrogen Metabolism Part 2 Flashcards

1
Q

when does amino acid catabolism occur

A

Excess protein is consumed (high protein diet)

Insufficient dietary protein (Kwashiorkor)

Insufficient dietary energy (starvation)

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2
Q

what happens to carbon backbones and amino groups in amino acid catabolism

A

carbon skeletons enter the main energy pathways and amino groups are processed to urea in the liver for excretion

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3
Q

what is another word for aminotransferase

A

Transaminase

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4
Q

what is the co factor that is very important for the function of transaminase enzyme

A

pyridoxal phosphate

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5
Q

what vitamin is pyridoxal phosphate derived from

A

vitamin B6

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6
Q

where is pyridoxal phosphate found in the transaminase enzyme

A

Pyridoxal phosphate is found in the active centre of the transaminase enzyme

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7
Q

what is pyridoxamine phosphate

A

when the amino group from the amino acid has been transferred to the pyridoxal phosphate

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8
Q

once the amino group has been transferred and pyridoxamine phosphate has been formed, what will then occur

A

that amino acid will be transferred to another keto acid and will form new a-amino acid based off what the keto acid was

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9
Q

what part of the body has the highest concentrations of aminotransferases

A

the liver

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10
Q

what is the corresponding keto acid to aspartate

A

oxaloacetate

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11
Q

what is the corresponding keto acid to alanine

A

pyruvate

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12
Q

what is the corresponding keto acid to glutamate

A

a-ketoglutarate

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13
Q

what is a characteristic of aminotransferase reactions and what do they depend on

A

Reactions are reversible and dependent on concentration of substrates

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14
Q

aminotransferases are specific for what and what does that mean (use alanine as an example)

A

aminotransferases are specific for the donor amino acid,

example: alanine aminotransferase (ALT) primarily catalyzes the transfer of an amino group from alanine to a keto acid

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15
Q

what do most aminotransferases only accept as their donor keto acid

A

αketoglutarate or oxaloacetate

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16
Q

what catalyses the reaction of glutamate to glutamine

A

glutamine synthase

17
Q

why is glutamine a very efficient molecule in terms of transferring nitrogen

A

it can carry two amine groups

18
Q

how many steps are required in the process of deamination of glutamine

A

two step process

19
Q

what is the opposite reaction to glutamate > glutamine, and where is it important

A

glutamine > glutamate

important in the liver

19
Q

what enzyme hydrolyses glutamine back to glutamate

A

Glutaminase enzyme

20
Q

how is glutamate deaminated and what by

A

oxidatively deaminated by glutamate dehydrogenase

21
Q

oxidatively deaminated by glutamate dehydrogenase

A

NAD and NADP

22
Q

why is the deamination of glutamate in the liver very important

A

for releasing ammonia in the liver, so that it can be used to make urea

23
Q

what are the three ways that amino groups can be removed

A

1- transamination
2- oxidative deamination
3- hydrolysis

24
Q

what is an example of oxidative deamination to remove amino group

A

glutamate dehydrogenase

25
Q

what is an example of hydrolysis to remove an amino group

A

glutaminase

26
Q

what will the glutamine synthetase catalysed reaction produce

A

glutamine

27
Q

in the process of removing nitrogen from the body what will happen to the glutamine that is produced in the glutamine synthetase catalysed reaction

A

Glutamine will be secreted from the tissue and then found in the blood stream and by amino acid transporters it will be taken up the liver

28
Q

what reaction will the glutamine undergo in the liver to produce glutamate and release what

A

Glutamine will then undergo the glutaminase reaction in the liver, releasing an ammonia group and forming glutamate

29
Q

what reaction can glutamate undergo to release its remaining amino group in the liver

A

Glutamate can also undergo the glutamate-dehydrogenase reaction to release its remaining ammonia group

30
Q

what amino acid is prominently formed in muscle and why

A

alanine due to higher levels of pyruvate

31
Q

what will alanine get converted back to in the liver and what will happen to its nitrogen group

A

alanine will get converted back to pyruvate

its nitrogen group will be transferred to a-ketoglutarate which will form glutamate

32
Q

What would be the likely product from the activity of glutamine synthetase under conditions of high ammonium ions (NH4 +)

A

glutamine

33
Q

What would be the likely product from the activity of glutamate dehydrogenase under conditions of high ammonium ions

A

glutamate