Metabolisme Protein

Susila sastri
Protein Utilization

3
 Metabolisme AA
• Transaminasi
• Deaminasi
• Siklus Urea
 Transamination

The body can transfer amino groups (NH2) from an amino acid to a
keto acid, forming a new nonessential amino acid and a new keto acid.
Transamination reactions require the vitamin B6 coenzyme.
 Transamination
(Reactions)

Amino Acid + Enzyme -Keto Acid + Enzyme–NH 2

Enzyme–NH 2 + -Ketoglutarate Enzyme + Glutamate

 Aminotransferases
(Transaminases)

Amino Acid + -Ketoglutarate -Keto Acid + Glutamate

Glutamate + Oxaloacetate -Ketoglutarate + Aspartate

 Transamination
(Enzyme Cofactor)

OH H O NH2
H2C C H2C
HO H2C OH PO H2C OH PO H2C OH

N CH 3 N CH 3 N CH 3
H H H

Pyridoxine Pyridoxal-5'-P Pyridoxamine-5'-P

(Vitamin B 6) (PLP) (PMP)
 Deamination

• The removal of the amino groups of all twenty amino

acids begins with the transfer of amino groups to just
one amino acid - glutamic acid (or glutamate ion).
This is catalyzed by transaminase enzymes which
transfer the amino group from amino acids to a
compound called alpha-ketoglutarate. The product is
an alpha-keto acid formed from the amino acid and
glutamate (formed from the addition of the amino
group to alpha-ketoglutarate.
 Amino Acid Deamination
(First Reaction in Amino Acid Breakdown)

O
R C COO–
Nitrogen-containing compounds
-keto acid
R
+
H 3N C COO– Glutamate
H Fumarate O
KG
OAA C
Aminotransferases Aspartate H2 N NH2
(Transaminases) aKG Urea
Cycle Urea
 Oxidative Deamination

Glutamate + NAD(P)+ + H2 O -Ketoglutarate + NH 4+ + NAD(P)H + H+

Glutamate
Dehydrogenase
 Glutamate Dehydrogenase
(Oxidative Deamination)

NAD(P) + NAD(P)H + H +
H2C COO –
H2C COO – H2O NH 4+
H2C COO –
CH 2 CH 2
CH 2
+ – –
H3N C COO H2N C COO
O C COO –
H

Glutamate -Iminoglutarate -Ketoglutarate

 Amino Acid Oxidase

Amino Acid + FAD + H2 O -Keto Acid + NH 3 + FADH2

FADH2 + O2 FAD + H2 O2
Amino acids are stripped of their carbon
 Protein and Amino Acid Catabolism
1. Protein  amino acids
2. Amino group (-NH2) is removed from amino acid in
process called deamination
– Requires vitamin B6
3. Amino group is removed with conjunction with a
hydrogen creating ammonia (NH3)
– Toxic
4. Liver converts the NH3  urea
– Harmless and excreted by the kidney
5. Remaining amino acid carbon chains are used at
various stages in the Citric Acid Cycle to generate ATP
– Amount of ATP produced varies
Figure 24.16 Transamination, oxidative deamination, and keto acid
Transamination 1 During
Amino acid + Keto acid Keto acid + Amino acid transamination
(-keto- (glutamic acid) an amine group
glutaric acid)
Liver Oxidative is switched from
deamination an amino acid to
NH3 (ammonia) a keto acid.
Keto acid
modification 2 In oxidative
3 During keto deamination, the
acid modification Urea amine group of
the keto acids CO2 glutamic acid is
formed during Modified removed as
transamination are keto acid ammonia and
altered so they can combined with CO2
easily enter the to form urea.
Krebs cycle
pathways. Blood

Enter Krebs
cycle in body cells Urea

Krebs
cycle
Kidney

Excreted in urine
 Urea Cycle
(Introduction)

Proteins
Fats
Carbohy drates
(Nutrients)

ADP

ATP
Catabolism Anabolism
NADP+
(Oxidation) (Biosy nthesis)
NADPH

Intermediates

Waste
(CO2/Urea/etc.)
 The Urea Cycle

Glutamate and glutamine function as the primary nitrogen carriers in most

organisms. In mammals, this nitrogen ends up in the liver where it is
converted to urea.

The two nitrogens in urea are derived from the NH4+ released when glutamate
or glutamine are deaminated, and from aspartate which is formed when
oxaloacetate is transaminated by aspartate aminotransferase.

The carbon atom in urea comes from CO2 (HCO3-) that is produced in the
mitochondrial matrix by the citrate cycle (the oxygen atom is derived from H2O
in the final reaction of the cycle).
The Urea Cycle
Urea Cycle
Urea Excretion: Amino Acids
Diagnostic Serum Enzymes