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

24
two main mechanisms involved in the degradation of amino acids:
transamination and oxidative deamination
25
A reversible process
transamination
25
Aminotransferase used as catalyst =, a-amino acids are converted to alpha Keto acid
Transamination (Glutamate can be produced through transamination, with a-ketoglutarate as amino group acceptor)
26
An alpha-amino acid is converted to an alpha-keto acid, releasing an amoonium ion
Oxidative Deamination
27
Occurs in the liver and kidney mitochondria
Oxidative Deamination
28
Summary of Oxidative Deamination and the Transport of Ammonia to the Liver
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
Cahill Cycle
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
__ ATP molecules are used to produce ONE urea molecule
4
31
Two molecules of ATP are used in the production of?
carbamoyl phosphate
32
The equivalent of 2 ATP molecules are consumed in the __ step to produce AMP
2nd
33
UREA CYLE First Step : Carbomoyl Group Transfer
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
UREA CYLE Second Step : Citrulline Aspartate Condensation
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
UREA CYLE Third Step : Argininosuccinate Cleavage
Argininosuccinate is cleaved to arginine and fumarate by the enzyme argininosuccinate lyase.
36
UREA CYLE Urea From Arginine Hydrolysis
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
PRODUCTS OF UREA CYCLE (8)
ORNITHINE CARBAMOYL P. CITRULLINE ASPARTATE ARGININOSUCCINATE FUMARATE ARGININE UREA
38
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