Amino Acid Metabolism Flashcards

1
Q

Proteases in lysosomes are called

A

cathepsins

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2
Q

Which proteins do lysosomes degrade during starvation?

A

During starvation, lysosomes selectively degrade proteins in tissues that atrophy in response to fasting (kidney, liver). Not in brain.

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3
Q

What is the first step in amino acid catabolism?

A

removal of an amino group

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4
Q

Problem with removing NH3 from amino acids?

A

NH3 is toxic.

Cannot be permitted to accumulate.

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5
Q

In mammals, what does the liver convert amino groups into?

A

Urea (non toxic)

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6
Q

What do reptiles and birds make instead of urea?

A

uric acid

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7
Q

How do fish deal with ammonia?

A

fish continuously dump ammonia

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8
Q

Where do the nitrogens from amino acids burned in the muscle go?

A

N’s added to pyruvate to make alanine, which is sent to the liver.
This is how it can be transported to the liver through the blood without making toxic ammonia

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9
Q

Where do the nitrogens from amino acids burned in non-muscle tissues go?

A

sent to the liver as gln

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10
Q

What happens to the amino groups in amino acids in the liver?

A

the amino groups from amino acids in the liver are transferred to a-kg, yielding glutamate and the a-keto acid of that particular amino acid

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11
Q

Where does the deamination of glu occur?

A

in the liver ONLY

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12
Q

What does the liver do with the alanine sent by the muscle?

A
  • remove the amino group yielding pyr
  • run gluconeogenesis
  • ship glucose back to muscle

GLUCOSE-ALANINE CYCLE

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13
Q

What does the liver do with the glutamine sent by non-muscle tissue?

A

-remove the amide
-make urea
DEAMIDATION RXN (not eamination, not transamination)

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14
Q

Where in the cell does the Urea Cycle take place?

A

Some reactions in the mito and some in the cyto

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15
Q

Carbamoyl phosphate synthase has a high affinity for _____.

A

Carbamoyl phosphate synthase has a high affinity for AMMONIA.
Will consume ammonia if the concentration gets too high.

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16
Q

How many ATP’s can a mammalian liver cell make from the complete catabolism of alanine?

A

ANSWER: +16 ATP/ala

2 ala –> 2 pyr
2 pyr–> AcetylCoa = +2 NADH (+6ATP)
Kreb’s x 2 = +6NADH (+18 ATP)
+2 FADH2 (+4 ATP)
+2 GTP (+2 ATP)
Making Urea:
deamination of glu =+1 NAD(P)H (+3ATP)
make carbamoyl-P = -2 ATP (-2 ATP)
make argininosuccinate = -AMP (-2 ATP)
fum–>oxa = +1 NADH (+3 ATP)

Net: +32 ATP/2 ala = +16ATP/ala

17
Q

What happens to the a-keto acids of the degraded amino acids?

A
  • Some become Acetyl-Coa or acetoacetate (ketogenic)

- Some are converted to pyr or Kreb’s intermediates. Can be used for gluconeogenesis (glucogenic).

18
Q

T/F some amino acids have both glucogenic and ketogenic parts

A

Truuuuuuuuuuuuuuuuu

ex. tryptophan

19
Q

essential amino acids are…

A

amino acids which cannot be made in mammals

20
Q

Is serine keto or glucogenic?

A

glucogenic

21
Q

Is lysine keto or glucogenic?

A

ketogenic