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?

A

ATP

19
Q

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

A

glutamine

20
Q

What is the molecular structure of ammonia?

A

NH3+

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
Q

What two molecules make up urea/

A

NH3 + CO2

26
Q

Where does 10% of urea end up?

A

in the intestine, cleaved by bacterial urease (splitting the CO2), NH3 is excreted in stool

27
Q

What is the disease of an accumulation of urea in the kidneys?

A

uremia

28
Q

What can hyperammonemia cause?

A

neurotoxicity, brain swelling, coma

29
Q

A genetic deficiency of what enzyme most commonly causes hyperammonemia?

A

ornithine transcarbamylase (OTC)

30
Q

What are some treatment for hyperammonemia?

A

antibiotics, low protein diet, arginine therapy, gene therapy