Nitrogen Flashcards

Does not cover inherited metabollic diseases

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1
Q

What is the process in which nitrogen is converted to Ammonium?

A

Fixation

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2
Q

What is nitrification?

A

NH4+ to nitrite and nitrate

We can get our Nitrogen from nitrate/nitrate

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3
Q

What amino acid is central to nitrogen entering our body?

A

Glutamate

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4
Q

What process is central to us conserving the nitrogen in our bodies?

A

Transamination

  • transferring amino acids between molecules
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5
Q

Give a general equation for transamination.

A

Amino acid 1 + keto acid 2 —-> Keto acid 1 + amino acid 2

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6
Q

What is formed when glutamate undergoes transamination with a keto acid?

A

Alpha-Ketoglutarate

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7
Q

Transamination reactions are readily reversible.

Why is this useful, in terms of how our body processes amino acids.

A

Can take part in both synthesis and degradation of amino acids

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8
Q

Pyridoxal phosphate cofactor is needed by what type of enzyme?

A

Aminotransferases

transamination enzyme

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9
Q

Pyridoxal phosphate cofactor (PLP) is derived from what essential vitamin?

A

B6

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10
Q

Amino acids undergo oxidative catabolism under 3 conditions.

What are they?

A

Leftover amino acids from normal protein turnover

Excess from diet

Stored proteins are broken down when carbohydrates are in short supply

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11
Q

What is pepsin and where does it function?

A

Enzyme - hydrolyses protein chains

Stomach

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12
Q

Trypsin and chymotrypsin cut proteins and larger peptides into smaller peptides, but where do they do this?

A

Small intestine

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13
Q

What enzymes hydrolyse peptides into amino acids, and where do they do this?

A

Aminopeptidase
Carboxypeptidases A & B

Small intestine

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14
Q

True or false

Peptides/proteins must be degraded to amino acids before they can cross through the epithelial cells and into the blood.

A

False

Amino acids, dipeptides and tripeptides can cross into the epithelial cells

But only single amino acids can go into the blood

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15
Q

What is ubiquitin used for?

A

Marks proteins that need to be degraded

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16
Q

Why are excess proteins/amino acids degraded and not stored like fats/sugars?

A

No storage for excess protein

17
Q

How do humans excrete nitrogen?

A

Urea + uric acid

18
Q

Ammonia is kinda toxic n stuff

How is it safely transported in the blood?

A

As glutamine or alanine

19
Q

Where is excess glutamine processed?

3

A

Intestines
Kidneys
Liver

20
Q

Ammonia + pyruvate = ?

A

Alanine

21
Q

Muscles exercising vigorously work anaerobically.

This would cause a problem in the muscles if it was not for glutamate. What is the problem, and how does glutamate solve it?

A

Anaerobic ∴ glycolysis

∴ pyruvate produced which cannot be broken down anaerobically

∴ lactate would build up

glutamate can donate ammonia, to make alanine from the pyruvate

alanine transported to liver ∴ no lactate build up

22
Q

Proteins can be broken down in exercising muscles if needed.

What cycle is central to protein break down?

A

Glucose - alanine cycle

23
Q

In the glucose - alanine cycle, why is glutamate converted to glutamine/alanine, only to be converted back to glutamate later on?

A

Glutamate is negatively charged

∴ can’t be transported to the liver

24
Q

What happens to excess glutamate?

A

Metabolised in mitochondria of hepatocytes

25
Q

When excess glutamate is metabolised, what happens to ammonia/nitrogen?

A

Re-captured via synthesis of carbamoyl phosphate

Carbamoyl phosphate then goes into the urea cycle

26
Q

Through processes such as the glucose - alanine cycle, carbon skeletons are produced from amino acids.

How are these carbon skeletons used?

A

Converted to glucose

Oxidised in CAC

Converted to ketones/fats

27
Q

Why are amino acids useful in terms of the citric acid cycle?

A

Enter as intermediates

Carbon skeletons

28
Q

Describe what the terms glucogenic and ketogenic mean.

A

Some amino acids ‘feed’ into gluconeogenesis (glucogenic) and some ‘feed’ into the acetyl CoA (ketogenic)

Some amino acids are both glucogenic and ketogenic

29
Q

Describe the fates of ketogenic amino acids.

A

CAC

Ketone bodies

30
Q

What nitrogen containing molecule is used in the second nitrogen acquiring reaction of the urea cycle?

A

Aspartate

31
Q

What are the possible fates of carbon skeletons produced from amino acid degradation?

A

Citric acid cycle - catabolism

Gluconeogenesis

Ketogenesis

32
Q

What are the possible fates of ammonia produced by amino acid degradation?

A

Biosynthesis

Excretion via Urea cycle

33
Q

Why are molecules like glutamate and aspartate not suitable for tranpsort in the blood?

A

They are charged

Glutamine and alanine are uncharged so are much more suitable