Nitrogen Flashcards

Does not cover inherited metabollic diseases (33 cards)

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 = ?

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
When excess glutamate is metabolised, what happens to ammonia/nitrogen?
Re-captured via synthesis of carbamoyl phosphate Carbamoyl phosphate then goes into the urea cycle
26
Through processes such as the glucose - alanine cycle, carbon skeletons are produced from amino acids. How are these carbon skeletons used?
Converted to glucose Oxidised in CAC Converted to ketones/fats
27
Why are amino acids useful in terms of the citric acid cycle?
Enter as intermediates Carbon skeletons
28
Describe what the terms glucogenic and ketogenic mean.
Some amino acids 'feed' into gluconeogenesis (glucogenic) and some 'feed' into the acetyl CoA (ketogenic) Some amino acids are both glucogenic and ketogenic
29
Describe the fates of ketogenic amino acids.
CAC Ketone bodies
30
What nitrogen containing molecule is used in the second nitrogen acquiring reaction of the urea cycle?
Aspartate
31
What are the possible fates of carbon skeletons produced from amino acid degradation?
Citric acid cycle - catabolism Gluconeogenesis Ketogenesis
32
What are the possible fates of ammonia produced by amino acid degradation?
Biosynthesis Excretion via Urea cycle
33
Why are molecules like glutamate and aspartate not suitable for tranpsort in the blood?
They are charged Glutamine and alanine are uncharged so are much more suitable