Amino Acid Metabolism (Lec) Flashcards

1
Q

repetitive process in which proteins are degraded and resynthesized

A

protein turnover

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2
Q

T/F - The rate of protein synthesis is just sufficient to replace the protein being degraded

A

T (Leads to hydrolysis and resynthesis of 300-400 g of body protein eaach day

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3
Q

state that results when the amount of nitrogen taken into the human body as protein equals the amount of nitrogen excreted from the body in waste materials

A

nitrogen balance

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4
Q

amount of nitrogen in urine exceeds consumed amount, also results in tissue wasting

A

negative nitrogen imbalance

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5
Q

rate of protein synthesis (anabolism) is more than protein degradation (catabolism)

A

positive nitrogen imbalance

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5
Q

indicated by the synthesis of large amounts of tissue

A

positive nitrogen imbalance

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6
Q

T/F - Amino acids are not stored by the body, unlike fats and
carbohydrates.

A

T (must either be obtained from the diet,
synthesized de novo, or produced from normal protein
degradation)

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7
Q

T/F - Proteins can be used as an energy source, but is rarely
used as such.

A

T

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8
Q

directed towards conserving tissues to the
greatest extent possible

A

Metabolism

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9
Q

Digestion of protein compromises?

A

muscle

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10
Q

where the mechanical breakdown of the proteins begins

A

teeth

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11
Q

Protein digestion starts in the?

A

stomach

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12
Q

Dietary protein stimulates the release of?

A

gastrin (a hormone that stimulates the stomach to
release gastric acid (hydrochloric acid) and pepsinogen
(Recall: zymogens))

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13
Q

Functions of HCl:

A

Antiseptic - kill most bacteria
low pH will denature proteins
Acidic environment activates pepsinogen

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14
Q

Pepsin affects the hydrolysis of __ of peptide bonds

A

10%

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15
Q

stimulated by the passage of small
amounts of acidic content into the small intestine.

A

Secretin production
(promotes the secretion of pancreatic digestive
enzymes : trypsin, chymotrypsin, and carboxypeptidase in
their inactive forms)

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16
Q

secreted by enterocytes - cells in the intestinal lining - and
further breakdown the remaining polypeptides into amino
acids.

A

Dipeptidase, tripeptidase, and aminopeptidase

17
Q

The pool of amino acids are then used to:

A
  • synthesize proteins
  • synthesize nitrogen-containing compounds (purines,
    pyrimidines)
  • turned into glucose, glycogen, fatty acids, ketone bodies,
    water, or carbon dioxide (energy source)
18
Q

the state of which amino acids are especially catabolized
to yield the carbon skeleton and to form intermediates for
carbohydrate and lipid biosynthesis, which are then used as
an energy source.

A

In the starved state

19
Q

degraded to form ketone bodies ,
which degrade to acetyl-CoA or acetoacetyl-CoA

A

Ketogenic amino acids

20
Q

degraded to TCA intermediates,
which can then be used for glucose synthesis
(gluconeogenesis)

A

Gluocgenic amino acids

21
Q

Body protein is catabolized primarily in?

A

muscle and liver

22
Q

Amino acids released from proteins usually lose their amino
group through?

A

transamination or oxidative deamination

23
Q

T/F - Each amino acid has a unique degradation pathway

A

T

24
Q

two main mechanisms involved in the degradation
of amino acids:

A

transamination and oxidative deamination

25
Q

A reversible process

A

transamination

25
Q

Aminotransferase used as catalyst =, a-amino acids are converted to alpha Keto acid

A

Transamination

(Glutamate can be produced through
transamination, with a-ketoglutarate
as amino group acceptor)

26
Q

An alpha-amino acid is converted to
an alpha-keto acid, releasing an
amoonium ion

A

Oxidative Deamination

27
Q

Occurs in the liver and kidney
mitochondria

A

Oxidative Deamination

28
Q

Summary of Oxidative Deamination and the Transport of Ammonia to the Liver

A

the amino acids are broken down, while passing along the amino group with the help of enzymes until it can finally be sent to the urea cycle.

Tissues use glutamine synthase to combine ammonia with glutamate to form glutamine.

Glutamine is then transported in the blood to the liver.

Cleavage is then done by glutaminase to produce glutamate and free ammonia.

29
Q

Cahill Cycle

A

Alanine is transported by the blood to the liver
where it is converted to pyruvate
Connects with the Cori Cycle. Alanine serves as carrier of ammonia and of the carbons of pyruvate from skeletal muscle to liver (Cori)

30
Q

__ ATP molecules are used to produce ONE urea molecule

A

4

31
Q

Two molecules of ATP are used in the production of?

A

carbamoyl phosphate

32
Q

The equivalent of 2 ATP molecules are consumed in the __ step to produce AMP

A

2nd

33
Q

UREA CYLE

First Step : Carbomoyl
Group Transfer

A

Carbon dioxide and ammonia are
combined to form carbamoyl phosphate
with the help of carbamoyl phosphate
synthetase (formed in the
mitochondrial matrix)

The carbamoyl group of carbamoyl
phosphate is transferred to ornithine to
form citrulline

34
Q

UREA CYLE

Second Step : Citrulline Aspartate Condensation

A

Citrulline is then transported into the
cytosol, reacting with aspartate to form
argininosuccinate synthetase, utilizing
ATP.

This step makes use of the enzyme
argininosuccinate synthetase, utilizing
ATP.

35
Q

UREA CYLE

Third Step : Argininosuccinate
Cleavage

A

Argininosuccinate is cleaved to
arginine and fumarate by the enzyme
argininosuccinate lyase.

36
Q

UREA CYLE

Urea From
Arginine Hydrolysis

A

Hydrolysis of arginine produces urea
and regenerates ornithine under the
influence of the enzyme arginase.
The oxygen atom present in urea
comes from water. Ornithine is transported back to the
mitochondria, to be reused in the urea
cycle.

37
Q

PRODUCTS OF UREA CYCLE (8)

A

ORNITHINE
CARBAMOYL P.
CITRULLINE
ASPARTATE
ARGININOSUCCINATE
FUMARATE
ARGININE
UREA

38
Q

The fumarate produced is ultimately
converted to aspartate.

Aspartate reenters the urea cycle at Step 2
Both the urea cycle and the Krebs cycle
were discovered by Hans Adolf Krebs

A