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Protein Metabolism

04/18/15

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Lab. Biokimia Nutrisi

Protein DIGESTION & ABSORPTION

Proteolysis (lysis of proteins) catalyzed by


proteases
Proteases cleave peptide bonds to
release free amino acids or smaller
peptide fragments
Endopeptidases cleave internal peptide
bonds
Exopeptidases cleave terminal peptide
bonds
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Protein DIGESTION & ABSORPTION

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Activation of protein digestion enzymes


Pepsinogen

Pepsin
HCl

Gastric Juice

Trypsinogen

enterokinase/
tripsin

Chymotrypsinogen

Trypsin

Trypsis

Procarboxypeptidase A & B
carboxypeptidase A & B

Chymotrypsin
Trypsis

Pancreatic Juice
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Specificity of protein digestion enzyme


Enzyme

Type

Pepsin

endopeptidase Aromatic or leucine

Trypsine

Endopeptidase Lysine or arginine

Chymotripsin

Endopeptidase aromatic

Carboxypeptidase A

exopeptidase

C-teriminal aromatic or neutral

Carboxypeptidase B

exopeptidase

C-terminal arginin or lysine

Leucine
aminopeptidase

exopeptidase

N-terminal leucine or neutral

04/18/15

Specificity

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Protein Digestion & Absorption

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DYNAMIC EQUILIBRIUM THEORY


OF BODY PROTEINS
Tissue protein are constantly being broken
down and resynthesized.
The "nitrogen or amino acid pool" is a grand
mixture of amino acids available in the cell
derived from dietary sources or the
degradation of protein.
Since proteins and amino acids are not
stored in the body, there is a constant
turnover of protein.
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Some protein is constantly being


synthesized while other protein is
being degraded.
Each day, some of the amino acids are
catabolized producing energy and
ammonia. The ammonia is converted to
urea and excreted from the body and
represents a drain on the nitrogen pool.

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DYNAMIC EQUILIBRIUM THEORY


OF BODY PROTEINS

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AMINO ACID METABOLISM

Purposes of amino acid degradation


supply energy
supply intermediates for synthesis of other
compounds
remove harmful excess of certain amino
acids

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Most amino acids are first stripped of their


amino group by two steps
1. transamination via Glu transaminase
transfers amino group to alphaketoglutarate (from TCA cycle) and forms
Glu
2. oxidative deamination via Glu
dehydrogenase; requires NAD+ co-factor
to oxidize the a carbon of the amino acid to
reform a-ketoglutarate; also releases
ammonium ion (NH4+); alpha-ketoglutarate
returns to the TCA cycle
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Transamination

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Glutamate
Dehyrogenase

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Deamination

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Other amino acid metabolism


3. Serine dehydratase
Non oxidative deamination of L-serine

4. Decarboxylations
Particularly decarboxylation of d-amino acid to
remove potential toxic of d-amino acid

5. Glutaminase and asparaginase


Much glutamic acid and aspartic acid in tissues
is found not as the free acid but in corespond
amide (asparagine and glutamine)
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Serine Dehydratase

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Decarboxylation
of Glutamic acid

-AMINO BUTYRIC ACID

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Amino Acid Oxidases

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The glutaminase reaction proceeds essentially irreversibly in the


direction of glutamate and NH4+ formation.
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Nitrogen Excretion
The body removes nitrogen waste in a
variety of forms.
NH4+ must be converted to other products
for excretion
Ammonia (NH3) in microorganisms, simple
aquatic and marine animals, fish
Uric acid in birds and land reptiles, in
primates comes from purine catabolism,
though
Urea via urea cycle
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UREA CYCLE

Argininosuccinase

Arginase
(key enzyme)

Argininosuccinate
synthetase
Ornithine
transcarbamylase

Carbamyl phosphate
synthetase

+ 2 ATP
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The relationship of urea cycle to TCA

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The relationship of urea cycle to TCA

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ENERGY UTILIZATION FROM AMINO ACIDS

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Abnormalities of Amino Acid Metabolism

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PURINE CATABOLISM

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PYRIMIDINE CATABOLISM

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See You
..

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