Proteins

Proteins and Amino Acids
Unlike fats and carbohydrates, amino acids are not stored by the body. That is, no protein exists
whose sole function is to maintain a supply of amino acids for future use. Therefore, amino acids
must be obtained from the diet, synthesized de novo , or produced from normal protein
degradation.
Nitrogen enters the body in a variety of compounds present in food, the most important being
amino acids contained in dietary protein. Nitrogen leaves the body as urea, ammonia, and other
products derived from amino acid metabolism. The role of body proteins in these transformations
involves two important concepts: the amino acid pool and protein turnover.
1. Amino acid pool: Free amino acids are present throughout the body, such as in cells,
blood, and the extracellular fluids. Envision all of these amino acids as if they belonged
to a single entity, called the amino acid pool. This pool is supplied by three sources
● Amino acids provided by the degradation of endogenous (body) proteins, most of
which are reutilized
● Amino acids derived from exogenous (dietary) protein
● Nonessential amino acids synthesized from simple intermediates of metabolism
Conversely, the amino pool is depleted by three routes
● Synthesis of body protein
● Consumption of amino acids as precursors of essential nitrogen-containing small
molecules
● Conversion of amino acids to glucose, glycogen, fatty acids, and ketone bodies, or
oxidation to CO2 + H2O.
In healthy, well-fed individuals, the input to the amino acid pool is balanced by the output. That
is, the amount of amino acids contained in the pool is constant. The amino acid pool is said to be
in a steady state, and the individual is said to be in nitrogen balance.
2. Most proteins in the body are constantly being synthesized and then degraded, permitting
the removal of abnormal or unneeded proteins. 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, called protein turnover, leads to the
hydrolysis and resynthesis of 300–400 g of body protein each day. The rate of protein
turnover varies widely for individual proteins.
Metabolism of Proteins and amino acids
Digestion and absorption of proteins as well as amino acids
Proteins are the most important group of endogenous macromolecules. A person weighing 70 kg
contains about 10 kg proteins, with most of it located in muscle. Protein molecules undergo
metabolism according to the requirements of the body. The nitrogen balance of an organism is
primarily determined by protein metabolism. This is the proportion of nitrogen made by nitrogen
containing compounds like proteins. The molecules other than proteins are minor.
Digestion in Stomach
The digestion of protein begins in the stomach. Where, HCl uncoils (denatures) each protein
strand so that digestive enzymes can attack the peptide bonds. The HCl also converts the inactive
pepsinogen to active pepsin. Pepsin cleaves proteins as well as large polypeptides molecules into
smaller polypeptides and amino acids molecules.
Digestion in Small Intestine

Protein degradation continues in the lumen of the intestine due to the activity of proteolytic
enzymes secreted by pancreas. These enzymes are secreted as inactive zymogens and converted
into active enzymes. Many enzymes secreted in the small intestine are:
1. Enteropeptidase indirectly activates a number of pancreatic enzymes.
a. It converts pancreatic trypsinogen into trypsin.
b. Trypsin converts pancreatic chymotrypsinogen into chymotrypsin.
c. Trypsin converts pancreatic procarboxypeptidase into carboxypeptidases.
d. Trypsin inhibits trypsinogen synthesis.
2. Elastase and collaganase cleaves polypeptides into smaller polypeptides and tripeptides.
3. Carboxypeptidases cleave amino acids from the acidic (carboxyl) ends of polypeptides.
4. Aminopeptidases cleave amino acids from the amino ends of small polypeptides
(oligopeptides).
5. Tripeptidases cleave tripeptides to dipeptides and amino acids.
Absorption
The cells of the small intestine have peptidases on their surface that split most of the dipeptides
and tripeptides into single amino acids and then these amino acids absorb from intestine walls. A
few dipeptides, tripeptides, and even larger molecules sometimes escape from digestion and
cross the intestinal wall.
Protein Metabolism
Proteins are constantly being made and broken down within each cell. During breakdown of
proteins, free amino acids are released and enter the general circulation. Some of these amino
acids may be promptly recycled into other proteins while others may be utilized for energy.
Constant synthesis and degradation of body proteins together is called protein turnover. The
protein that participates in this flux is called endogenous protein. Protein turnover is the balance
between protein synthesis and protein degradation. More synthesis than breakdown indicates an
anabolic state that builds lean tissues, more breakdown than synthesis indicates a catabolic state
that burns lean tissues. Protein turnover is believed to decrease with age in humans
Nitrogen Balance
1. If the body maintains the same amount of protein in its tissues from day to day then the
body is said to be in nitrogen balance. If the body adds protein, it is in positive nitrogen
balance. If the body loses protein, it is in negative nitrogen balance.
2. Normally, healthy adults receive enough protein to meet their needs, and they dispose of
any excess. Their nitrogen intake equals their nitrogen output and they are said to be in
zero nitrogen balance, or nitrogen equilibrium.
3. Growing infants, children, pregnant women and people recovering from protein
deficiency or illness are in positive nitrogen balance. Their nitrogen intake exceeds their
nitrogen output. They are building protein, tissues, adding new blood, bone, skin, and
muscle cells to their bodies.
4. In contrast, people who are starving or suffering other severe stresses such as burns,
injuries, infections, and fever are in negative nitrogen balance. Here, nitrogen output
exceeds nitrogen intake. During these times, the body loses protein as it breaks down
proteins for energy.
Amino Acid Metabolism

There are 20 amino acids present in protein and each amino acid has a unique structure. Thus
their metabolic pathways are different. However, there are some common points in the
biosynthesis and degradation of all amino acids.
Biosynthesis of amino acids

1. About half of twenty amino acids can be synthesized in the body and they are called
“nonessential amino acids”. The other amino acids which cannot be synthesized in the
body are considered as “essential amino acids”. Essential amino acids must be obtained
from the diet.
2. Almost all of the nonessential amino acids are used for the synthesis of other nitrogen
containing compounds e.g. glycine is used for synthesis of porphyrin and purine.
Glutamate is required for synthesis of neurotransmitters and purine. Aspartate is required
for synthesis of both purine and pyrimidine.
3. Nonessential amino acids are produced from glucose, ammonia and some other amino
acids. The carbon skeletons of the nonessential amino acids derived from glucose as they
produced from intermediates of glycolysis and TCA cycle. Where, 4 amino acids
(alanine, glycine, cysteine and serine,) are produced from glycolytic pathway while 6
amino acids (glutamate, glutamine, proline, arginine, aspartate and asparagine) are
produced by intermediates of TCA cycle. Here, α-Ketoglutarate is the precursor for the
synthesis of glutamate, glutamine, proline, and arginine while Oxaloacetate provides
carbon for the synthesis of aspartate and asparagine. Regulation of biosynthesis of
individual amino acids is complex but these are regulated by feedback i.e. as the
concentration of free amino acid increases, a key biosynthetic enzyme is inhibited.
Degradation of amino acids

In animals, amino acids undergo oxidative degradation in three different metabolic
circumstances.
1. During the normal synthesis and degradation of cellular proteins, some free amino acids
are released. When these amino acids are not needed for new protein synthesis, they
undergo oxidative degradation.
2. When a diet is rich in protein and ingested amino acids exceed the body's need for protein
synthesis, the surplus amino acids are catabolized. Amino acids cannot be stored in the
body.
3. During starvation and in uncontrolled diabetes mellitus, when carbohydrates are either
unavailable or not properly utilized, cellular proteins are used as fuel.
Under all these metabolic conditions, amino acids lose their amino groups to form keto acids.
The keto acids degrade into CO2 and H2O. These keto acids can provide 3 or 4 carbon units that
can be converted to glucose via gluconeogenesis. The pathways of amino acid catabolism are
quite similar in most organisms. As occur in carbohydrate and fatty acid catabolism, the
processes of amino acid degradation converge into central catabolic pathways of TCA cycle. One
important feature distinguishes amino acid degradation from other catabolic processes is that
every amino acid contains an amino group, and the pathways for amino acid degradation
therefore include a key step in which the amino group is separated from the carbon skeleton and
shunted into the pathways of amino group metabolism.

Proteins

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Proteins

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Proteins and Amino Acids

Digestion and absorption of proteins as well as amino acids

Digestion in Small Intestine

Amino Acid Metabolism

Biosynthesis of amino acids

Degradation of amino acids

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