14. Post-Absorption Processing of Proteins Flashcards

1
Q

What biologically active compounds are amino acids precursors for?

A
Haem
Nucleic acids
Hormones
Neurotransmitters
Biologically-active peptides
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2
Q

What determines the half life of a protein?

A

N-terminal residue

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3
Q

Which amino-acid sequences are rapidly degraded?

A

Proline
Glutamic acid
Serine
Threonine

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4
Q

What two ways are proteins degraded?

A

Ubiquitin-proteasome system

Lysosomal enzymes

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5
Q

What does the concentration of amino acids in circulation between meals depend on?

A

Utilisation by tissues

Release following protein degradation

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6
Q

How is alanine used in hepatic gluconeogenesis?

A

Alanine is made in muscle by the transamination of pyruvate

Liver coverts the carbon skeleton of alanine to glucose

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7
Q

What does it mean for an amino acid to be glucogenic?

A

Its breakdown yields TCA cycle intermediates

Used to make glucose: gluconeogenesis

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8
Q

What does it mean for an amino acid to be ketogenic?

A

Breakdown yields acetoacetate or acetyl-CoA

Ketogenesis

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9
Q

Which amino acids are glucogenic?

A
Alanine
Arginine
Asparagine
Aspartate
Cysteine
Glutamate
Glutamine
Glycine
Proline
Serine
Histidine
Methionine
Threonine
Valine
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10
Q

Which amino acids are both glucogenic and ketogenic?

A

Tyrosine
Isoleucine
Phenylalanine
Tryptophan

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11
Q

Which amino acids are ketogenic?

A

Leucine

Lysine

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12
Q

Which amino acids are formed from essential amino acids?

A

Cysteine
Tyrosine
Hydroxylysine

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13
Q

Which enzymes play a role in forming amino acids from amphibolic intermediates?

A

Transaminases
Glutamine synthetase
Glutamate dehydrogenase

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14
Q

What reaction does phenylalanine undergo to make metabolic intermediates?

A

Enzyme: phenylalanine hydroxylase
Produces tyrosine
Tyrosine converted to fumarate or acetoacetate

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15
Q

Which disorder is caused by a deficiency of phenylalanine hydroxylase?

A

Phenylketonuria

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16
Q

How is glutamine synthesised?

A

Glutamate converted to glutamine by glutamine synthetase

Reaction is useful for storing free ammonia in a non-toxic form

17
Q

What coenzyme is used by transaminases?

A

Vitamin B6

18
Q

What is the mostly widely used ‘donor-acceptor’ transaminase couple?

A

Glutamate

a-ketoglutarate

19
Q

Which amino acids use the glutamate - a-keoglutarate pair as part of their degradation?

A
Aspartic acid
Asparagine
Arginine
Isoleucine
Leucine
Lysine
Tryptophan
Tyrosine
Valine
20
Q

Which enzyme converts alanine and a-ketoglutarate to pyruvate and glutamate?

21
Q

Which enzyme converts oxaloacetate and glutamate to aspartate and a-ketoglutarate?

22
Q

What reaction does ALT catalyse?

A

Alanine and a-ketoglutarate
to
Pyruvate and glutamate

23
Q

What reaction does AST catalyse?

A

Oxaloacetate and glutamate
to
Aspartate and a-ketoglutarate

24
Q

What are the two steps in disposal of amino acids?

A

Transamination

Oxidative deamination

25
What are the two steps in synthesis of amino acids?
Reductive amination | Transamination
26
Where does the urea cycle take place?
Liver
27
How is amino nitrogen transported in circulation?
Alanine (made from pyruvate in muscle) | Glutamine (made from glutamate in most tissues)
28
What is free ammonia produced in the body by?
Breakdown of purines and pyrimidines Breakdown of amines and monoamines Breakdown of glutamine Bacterial digestion of urea
29
Where do the two amino groups on urea come from?
Carbamoyl phosphate | Aspartate
30
How much energy is required to produce urea?
3 ATP molecules per molecule of urea
31
What are normal levels of free ammonia in blood serum?
5-50mmol/L
32
What is acquired hyperammonaemia caused by?
Liver disease or failure
33
What is hereditary hyperammonaemia caused by?
Inherited urea cycle defect
34
What are the effects of hyperammonaemia?
CNS toxicity Tremors, slurred speech, vomiting, cerebral oedema Coma, death
35
What is the most common urea cycle disorder in humans?
Ornithine transcarbamylase deficiency
36
What is the function of ornithine transcarbamylase?
Converts carbamoyl phosphate and ornithine into citrulline
37
What are the symptoms of an OTC deficiency?
``` Hyperammonaemia Vomiting Refusal to eat Progressive lethargy Coma ```