Protein Metabolism
Protein Degradation:
• Degradation of proteins proceeds at different
rates which vary , depending on the
physiological needs and roles of proteins.
• Protein degradation will result in amino acids
• The first step in catabolism of all amino acids
involves the removal of amino group.
Removal of amino group from amino acids
• The first step in the catabolism of all amino acids
involves the removal of the amino group through:
A. TRANSAMINATION
B. Deamination
C. Transdeamination
A. TRANSAMINATION:
It is the transfer of the amino group from an
α-amino acid to an α-keto acid with the
production of a new amino acid and new
keto acid.
Transamination reactions are carried out by
Transaminases (Aminotransferases)
TRANSAMINASES
H
- -
R1 C COO + R2 C COO
+
NH3 O
Transaminase
H
- -
R1 C COO + R2 C COO
+
O NH3
TRANSAMINASES
• Transaminases (aminotransferases) are present in
cytoplasm and mitochondria of all tissues especially
liver.
• Vitamin B6 (PLp) (pyridoxal phosphate) is essential
for transamination reaction.
• All amino acid can do transamination EXCEPT :
– Proline
– Hydroxyproline
– Threonine
– Lysine
TRANSAMINASES
• The commonest α-keto acid used is α-ketoglutaric
acid which can accept amino group from all amino
acids converting them to Glutamic acid
• This is important because Glutamic acid is the only
amino acid that undergoes oxidative deamination
at an appreciable amounts in liver by (L-glutamate
dehydrogenase).
COO COO
COO CH2 COO CH2
CH2 CH2 AST CH2 CH2
+ +
HC NH3 + C O C O + HC NH3
COO COO COO COO
aspartate -ketoglutarate oxaloacetate glutamate
Aminotransferase (Transaminase)
COO COO
CH2 CH2
ALT
CH3 CH2 CH3 CH2
+ +
HC NH3 + C O C O + HC NH3
COO COO COO COO
alanine -ketoglutarate pyruvate glutamate
Aminotransferase (Transaminase)
Clinical significance of serum
Transaminases
• These enzymes are abundant in liver and heart and are
released in case of cell injury.
a) AST (Aspartate Amino Transferase) : the blood level of
this enzymes increases in case of heart and liver damage ,
but it is more specific to the heart (myocardial infarction)
b) ALT (Alanine Amino Transferase): The blood level of this
enzyme increases in case of liver damage (liver cirrhosis
and hepatitis).
Removal of amino group from amino acids
B- Deamination:
1. Oxidative deamination: it results in release of
amino group in the form of free ammonia (NH3).
a) L Glutamic dehydrogenase:
– Site: mitochondria of liver, heart ,kidney and muscle
– It is Zn metalloenzyme
– It needs NAD as coenzymes
– It catalyzes the reversible oxidative deamination of
Glutamic acid into α-ketoglutaric acid
L-Glutamate Dehydrogenase
Removal of amino group from amino acids
b) L- amino acid oxidases:
• They are flavoprotein dependent enzymes
L amino acid oxidases
Removal of nitrogen from amino acids
2. Non Oxidative deamination (Hydrolytic
deamination):
a) Glutaminase
b) Asparginase
Removal of amino group
Transamination Deamination Transdeamination
Oxidative Nonoxidative
AST ALT Deamination deamination
L-glutamate Hydrolytic
L-D oxidases
dehydrogenase deamination
Nutritional Function of Protein
Proteins play a major role in ensuring your health well being.
There are innumerable functions of proteins in the body.
building and repairing of body tissues.
protein makes up nearly 17 percent of the total body weight. For example: muscle
contains about 1/3 protein, bone about 1/5 part and skin consists of 1/10 portion.
The rest part of proteins is in the other body tissues and fluids.
Take part in some kinds of important physiological
activities
regulation of body processes and formation of enzymes and hormones,
antibody.
Oxidation and supply energy
How to assess the condition of protein
metabolism?
1. Nitrogen balance
the balance between the amount of nitrogen
taken in (foods or the body) and the amount given
off (lost or excreted)
Significance:
Measuring the amount of intake and losses of total
nitrogen can help us to know the general situation of
protein metabolism.
nitrogen balance
★ positive: synthesis > degradation
(e.g., growth, body building)
★ negative: synthesis < degradation
(cancer)
★ Equilibrium: synthesis = degradation
(healthy adults eating a balanced diet)
2. Physical requirements of proteins
• Lowest requirement:
30~50g/day
• Recommend requirement:
80g/day (65kg man)
Some sources of dietary protein include:
Meat,
fish
Eggs,
3. Nutrition value of proteins
(1) Essential amino acids :
some Amino acids that cannot be synthesized
by the body and must be obtained from the diet.
(2) Non- essential amino acids
(4) nutrition value
A protein’s nutritional value is judged by how
many of the essential amino acids it provides and
in what quantity.
Different foods contain different numbers and
amounts of the essential amino acids.
lysine tryptophan
(5) Complementary effect of dietary proteins
Two or more plant proteins are consumed
together which complement each other in
essential amino acid content.
Digestion
2.1 Digestion
Amino
hydrolysis acids absorb
Dietary protein
Significance:
◆ Large small Help to absorb
◆ eliminate the species specificity and
antigenicity, avoid allergy , toxic reaction.
site:
stomach,
small intestine
Pepsin
Chymotrypsin, trypsin,
and exopeptidases
Proteolytic enzymes of
pancreatic juice
Amino acids
Initiated in stomach
enzymes: pepsin
HCl
Pepsinogen Pepsin
HCl from parietal cells
• Stomach pH 1.6 to 3.2
• Pepsinogen from chief cells
The substrate mainly are
phenylalanine,tyrosine,tryptophan
Aromatic amino acids
Products:
insoluble protein, soluble protein,
polypeptides and amino acids
Protein Digestion – Small Intestine
Activation of Pepsinogen
Pepsinogen Pepsin + peptide
Protein Digestion
• Pancreatic enzymes take over protein digestion by
hydrolyzing polypeptides into shorter oligopeptides
amino peptidase endopeptidase carboxy peptidase
O O O
H2N-CH-C-NH-CH--- NH-CH-C-NH-C--- NH-CH-C-NH-CH-COOH
R1 R2 R Rn-1 Rn
polypeptide
dipeptidase
O
amino acid + H2N-CH-C-NH-CH-COOH
R R dipeptide
amino acid
Protein Digestion
• Proteins are broken down to
– Tripeptides
– Dipeptides
– Free amino acids
2.2 absorption
Free Amino Acid Absorption
Lumen
(small intestine)
Carrier systems
Neutral AA
Basic AA
Acidic AA
Amino acids Amino Amino
Amino acids carrier acids
acids Na+ protein
Na+ pump Na+
Na+
ATP
Entrance of some AA is
via active transport
Requires energy Brush broad membrance
§ 3.1 Protein turnover
the balance between protein synthesis and protein
degradation .
In healthy adults, the total amount of protein in the
body remains constant, because the rate of protein
synthesis is just sufficient to replace the protein that is
degraded. this process is called protein turnover.
• Decarboxylation of amino acids
• Metabolism of one carbon unit
• Metabolism of sulfur-containing AAs
• Metabolism of aromatic AAs
• Metabolism of branched-chain AAs
§ 5.3 Metabolism of sulfur-
containing AAs
Methionine cysteine cystine
S CH3 CH2SH
CH2 S S CH2
CH2 CHNH2
CHNH2 CHNH2
CH2
COOH
COOH COOH
CHNH2
COOH
