PROTEIN (METABOLISM)

Mica Corporal
Danica Juanillo
Meika Kurahashi
Angelene Rojo
Jacqueline Solivio
Japheth Vijar
Eduardo Jose V. Villanueva
What is Protein Metabolism?

Protein metabolism denotes the various biochemical

processes responsible for the synthesis of proteins and
amino acids, and the breakdown of proteins and other
large molecules by catabolism.
Why are proteins important?

Proteins are responsible for most of the structure and

function in our body tissues.

The body employs several regulatory mechanisms to

spare body proteins from metabolism.
● Proteins contain carbon, hydrogen, oxygen, nitrogen , and
sometimes other atoms. They form the cellular structural
elements, are biochemical catalysts, and are important
regulators of gene expression .
Protein Metabolism

When proteins undergo catabolism, they are broken down to

individual amino acids (proteolysis).

Amino acids differ with respect to the "R group, which will
determine where in the metabolic cycles that the amino acid
products will enter.
Protein Digestion
Whole proteins are too large to be absorbed into the bloodstream,
so during digestion they’re metabolized -- or broken down -- into
single amino acids and small pieces with only a few amino acids.
This part of protein metabolism depends on stomach acid to flatten
out the protein, plus several enzymes that split protein into amino
acids.
Enzymes involved in protein metabolism
Enterokinase, an enzyme located in the wall of the small intestine, activates
trypsin, which in turn activates chymotrypsin. These enzymes liberate the
individual amino acids that are then transported via sodium-amino acid
transporters across the intestinal wall into the cell.

The amino acids are then transported into the bloodstream for dispersal to
the liver and cells throughout the body to be used to create new proteins.
When in excess, the amino acids are processed and stored as glucose or
ketones.
These amino acids are absorbed by the blood stream and transported to different
tissues of the body where they are either used in replacing the damaged tissues
or in the synthesis of proteins.

Some amino acids are oxidised in the body to form CO2 and H2O, and others may
be deaminised in the kidney or liver. The amino acid metabolism involves a
number of enzymes, and amino acids may undergo the following metabolic fates:
1. Oxidation, transamination, deamination and decarboxylation
reactions.

2. Conversion to other nitrogen containing compounds such as

certain vitamins.
3. Protein biosynthesis.
 Transamination

This process involves the reversible transfer of an amino group to an or­ganic

acid, called keto acid. Thus, there is an interconversion of an amino acid to the
corresponding keto acid and vice versa. These changes are catalyzed by
transaminases. An important example of transamination is the conversion of
glutamic acid in the presence of pyruvic acid to α-ketoglutaric acid and alanine
as shown below.
With a few exceptions nearly all amino acids take part in transami­nation.
These are of great importance as connecting links between carbohydrate and
amino acid metabolism. Thus, carbohydrates may enter amino acid
metabolism and vice versa.
Transamination
 Deamination

● This process involves the removal of amino group by oxidation of a particular

amino acid to produce the corresponding keto or hydroxy acid and free
ammonia.
● The reaction is catalyzed by an oxidase, an enzyme specific for the deamination
of a particular type of amino acid.
 Thus, alanine is converted into pyruvic acid, glutamic acid into
a-ketoglutaric acid and so on. The deamination of glutamic
acid is catalyzed by the enzyme glutamic dehydrogenase and
the coen-zyme NAD or NADP.

● The action of glutamic dehydrogenase is also an important link

between carbohydrate and protein metabolism, since it
converts α-ketoglutaric acid (an intermediate of Kreb’s cycle) to
an impor­tant amino acid, namely glutamic acid. The latter is
used not only as amino acid component of many proteins but
also takes part in the formation of other amino acids.
Decarboxylation
In this enzymatic reaction of amino adds, amino acid decarboxylases require
pyridoxal phosphate as cofactor. Some of the amines formed as a result of
decarboxylation have important physiological effects. Thus, histidine
decarboxylase, found in animal tissues produce histamine, a substance
which, among other effects, stimulates gastric secretion.
Formation of Urea:
It is also an important aspect of the protein metabolism. The urea is formed
in the liver (to some extent in the kidney also) from ammonia, amino groups,
and CO2 in the presence of ATP and some enzymes. The amino groups
separated in the deamination process unite with CO2 to form urea.
● The nitrogen waste that is liberated in this process is converted
to urea in the urea acid cycle and eliminated in the urine. In
times of starvation, amino acids can be used as an energy source
and processed through the Krebs cycle.
Energy Yield of Protein Respiration:

● The ATP yield of protein and amino acid respiration vary considerably,
depending on whether the respiratory pathways follows the ketogenic
or glucogenic routes. The efficiency of protein respira­tion is roughly
equivalent to that of fats or carbohydrates, that is, about 40%.
● The net usefulness of protein as energy source is only about 70% of its
potential value as protein respiration is accompanied by many other
energy requiring and, therefore heat producing reaction.
AMINO ACID SYNTHESIS

● Amino acid synthesis is the set of biochemical processes ( metabolic

pathways) by which the various amino acids are produced from other
compounds.
● Amino acids are critical to life, and have a variety of roles in
metabolism. The substrates for these processes are various compounds
in the organism's diet or growth media. Not all organisms are able to
synthesise all amino acids, for example humans are only able to
synthesise 10 of the 20 standard amino acids.
Gluconeogenesis

● In order to make glucose from scratch (Gluconeogenesis), our cells have

to use a substrate that is not acetyl CoA and will not go through CO2
expelling steps.
● Some amino acids can enter the metabolic pathways in places that meet
these requirements and therefore are the best choice for raw material to
make glucose.
● Gluconeogenesis is the metabolic process by which organisms produce
sugars (namely glucose) for catabolic reactions from non-carbohydrate
precursors, converting pyruvate to glucose.
 Gluconeogenesis
● When amino acids enter the metabolic pathways for the purpose of
making glucose, the reactions of glycolysis run in reverse to synthesize a
new glucose molecule, which the liver is good at doing.
● Gluconeogenesis is stimulated by hormones in the body that are released
when blood sugars become low.
 Absorption into the blood

● Water-soluble food molecule, e.g. monosaccharide, amino acids, minerals

and water soluble vitamins can be absorbed into the capillaries by diffusion
and active transport.
● As the absorption of digested food into the blood increases the water
potential of the content in the small intestine, water is drawn into the blood
by osmosis. In other words, absorption of digested food in the small
intestine is accompanied by absorption of water at the same time. Over 90%
of the water in food is absorbed in the small intestine.
Sources
https://www.livestrong.com/article/532626-how-much-protein-can-be-digested-per-hour/

https://content.byui.edu/file/a236934c-3c60-4fe9-90aa-d343b3e3a640/1/module8/readings/protein_
meta.html

https://chem.libretexts.org/Textbook_Maps/Biological_Chemistry/Metabolism/Anabolism/Gluconeogen
esis

http://www.yourarticlelibrary.com/proteins/protein-metabolism-the-process-of-protein-metabolism-oc
curred-in-an-organism/22746