Nitrogen - w5 Flashcards

1
Q

How do amino acids get absorbed from the lumen of the intestines into the bloodstream?

A

Na+-dependent transporters (secondary active transporters)

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2
Q

How do amino acids get transported out of the cell?

A

facilitated diffusion

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3
Q

How do amino acids get transported from the blood into the cells?

A

Na+ dependent (secondary active)

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4
Q

Which enzymes on the brush border break down oligopeptides?

A

pancreatic enzymes

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5
Q

What tells us how long a protein can function in the body?

A

the half life

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6
Q

From where can we generate our intracellular amino acid pool?

A

dietary protein and protein degradation

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7
Q

What are the proteases in lysosomes that are activated at low pH?

A

cathepsins

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8
Q

What are the two steps in the ubiquitin-proteasome pathway?

A

ubiquitin tags proteins for degradation, proteasome complex degrade the proteins

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9
Q

Proteins with regions rich in what are more likely to be degraded?

A

PEST (proline, glutamate, serine, threonine)

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10
Q

Other than proteins, what else can amino acids be converted into?

A

carbohydrate (glycogen) or fat (triacylglycerols) ; as storage

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11
Q

What process are amino acids important in formation?

A

gluconeogenesis

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12
Q

What do you call the removal of an a-amino group?

A

transamination

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13
Q

Transamination transfers the amino group from the og amino acid to a-ketoglutarate forming what?

A

glutamate

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14
Q

What is the co-factor that helps to catalyze almost every amino acid reaction?

A

pyridoxal phosphate (PLP)

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15
Q

In what vitamin can we get PLP?

A

Vitamin B6

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16
Q

Where does oxidative deamination occur (liberation of ammonia)?

A

liver and kidneys

17
Q

What catalyzes the oxidative deamination of glutamate?

A

glutamate dehydrogenase

18
Q

What is the allosteric regulator of glutamate dehydrogenase?

19
Q

What is the most abundant AA in blood and is essential for ammonia transport?

20
Q

What is the molecular structure of ammonia?

21
Q

What makes up glutamine with the help of ATP?

A

glutamate + NH3

22
Q

In the liver, how does glutamine get broken back down to glutamate and NH3?

A

with the help of water (hydrolase)

23
Q

What enzyme takes NH3 from glutamine and changes pyruvate to alanine?

A

alanine aminotransferase

24
Q

Where is urea produced?

A

the liver (first two reactions in the mitochondria, rest in cytoplasm)

25
What two molecules make up urea/
NH3 + CO2
26
Where does 10% of urea end up?
in the intestine, cleaved by bacterial urease (splitting the CO2), NH3 is excreted in stool
27
What is the disease of an accumulation of urea in the kidneys?
uremia
28
What can hyperammonemia cause?
neurotoxicity, brain swelling, coma
29
A genetic deficiency of what enzyme most commonly causes hyperammonemia?
ornithine transcarbamylase (OTC)
30
What are some treatment for hyperammonemia?
antibiotics, low protein diet, arginine therapy, gene therapy