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METABOLISM OF

PROTEINS
Prepared By: Maricris R. Ranara
DYNAMIC STATE OF TISSUE PROTEIN
All the proteins in the body are constantly breaking down to their
constituent amino acids and being resynthesized. The rate of turn
over varies from different proteins in different tissues. Turn over rate
of a compound is the percentage of the amount present which is
metabolized per unit time or it may be expressed in terms of mass
compound transformed per unit weight of tissue or animal.

Nitrogen – the element which characterizes protein; hence protein


metabolism is measured in terms of nitrogen.

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Folin conceived of two independent fates of ingested
proteins:

1. Endogenous metabolism which utilizes the amino acids of


ingested protein for the repair and rebuilding of degraded tissue.
The excretion of creatinine, derived from muscle breakdown is its
index.
2. Exogenous metabolism which involves an oxidative degradation
of dietary amino acids not needed for tissue protein synthesis.
The amount of urea excreted is its measure.

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Nitrogen Balance – is the quantitative difference between the
nitrogen intake and nitrogen output, both expressed in the same
units (such as grams N per day).

Intake – the nitrogen, in the form of protein of food.

Output - such routes or excretion as urine and feces.

When normal adults excrete an amount of nitrogen equal to their


intake, they are said to be in nitrogen equilibrium.

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Positive Nitrogen Balance – exists when intake exceeds output. This
condition occurs whenever new tissue is being synthesized, such as
during growth in the young and in pregnancy.

Negative Nitrogen Balance – the output exceeds the intake. This


condition occurs on inadequate intake of protein (starvation), and in
states of accelerated catabolism of tissue protein (fever, infection,
wasting disease).

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Role of Protein in the diet
 Nutritional Requirement

Dietary proteins provide amino acids required for optional growth of


the young and maintenance of nitrogen equilibrium in the adult.

From the standpoint of amino acid requirement, the amino acids are
classified into two groups:

1. Essential or indispensable amino acids – those which cannot be


synthesized from the components of the diet at a rate adequate
for maximal growth and must be supplied in the diet.
• arginine, histidine, isoleucine, leucine, methionine, phenylalanine,
threonine, tryptophan and valine
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2. Non-essential or dispensable amino acids – are synthesized by
animal under specific experimental conditions at a rate sufficient to
meet the requirements for normal growth.
• glycine, alanine, serine, aspartic acid, glutamic acid, proline,
hydroxyproline, citrulline, cystine, and tyrosine

 Biological Value of Proteins


- the percentage of absorbed protein in a food that is utilized by the
body for the building and maintenance of body tissues.

Factors influencing the biological value of proteins:

1. The amounts and relative proportions of their constituent amino


acids.
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2. The nutritional availability (rates of liberation and absorption) of
their constituent amino acids under condition of digestion in the
gastrointestinal tract.

3. The various methods of processing and preparation of foodstuff.

The most important single factor that influences the nutritional


quality of a protein is its amino acid composition. A “complete” food
protein must contain all the essential amino acids. In general, animal
proteins are nutritionally superior to plant proteins.

The digestibility of various proteins and the rates of release of amino


acids may be affected by the manner of preparation of foods.

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 Supplementary Value of Proteins

The value of proteins for supplying essential amino acids which are
lacking in other proteins is called supplementary value. If a protein
has the proper assortment of amino acids for tissue building, it is said
to have a very high biological value, but it is of little value in
supplementing a protein of a very poor biological value.

 Protein – Sparing Effect

The dietary requirement for protein is influenced by the level in the


diet of fat and carbohydrate, these latter foodstuff appearing to have
a “protein sparing effect”.

Fat – functions primarily as a fuel.


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Carbohydrates – also serve as a fuel, but in addition are required for
the synthesis of certain catalytic compounds of metabolic cycles and
provide the carbon skeletons for the synthesis of non-essential
amino acids.

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General Metabolic Reactions of Amino Acids
 Oxidative Deamination

the deamination of amino acids to the corresponding L-keto acids is


catalyzed by an enzyme called amino acid oxidase. It is shown to
contain FAD as coenzyme. The enzyme is present in the liver and in
the kidney.

R-CH-COOH + (O) ----- R-CO-COOH + NH3


l
NH2

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 Decarboxylation

A number of animal tissues contain amino acid decarboxylase which


convert the amino acid to its corresponding amines. Several of the
decarboxylases require pyridoxal phosphate as coenzyme.

-CO2
R-CH(NH2)-COOH ------R-CH2-NH2 + CO2
Primary amine

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 Transmination

The transfer of an amino group from an amino acid to an L-keto acid


forming a new amino acid and keto acid, without the appearance of
ammonia in free state. Pyridoxal phosphate is the coenzyme of the
transaminase.

R-CH(NH2)-COOH + R’ –CO-COOH---R-CO-COOH+R”-CH(NH2)-COOH

Glutamic acid + Oxaloacetic acid -- a-ketoglutaric acid + aspartic acid

Aspartic acid + Pyruvic acid -- Oxaloacetic acid + Alanine

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The importance of transamination:

1. It provides a mechanism for the interconversion of amino acids via keto


acids.
2. It provides a mechanism for the oxidation of many amino acids.
3. It is a reaction by which amino acids are formed from other organic
materials.

Formation of Urea:

The formation of urea from ammonia is represented by the overall equation:

2NH3 + CO2 ----- NH2-CO-NH2 + H2O

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Energy is required for the formation of urea from ammonia and carbon
dioxide. Krebs made the important discovery that urea formation proceeds
only in the presence of ornithine.

3 steps in the formation of Urea

1. Ornithine combines with NH3 and CO2 to form citruilline.


2. Citruilline is converted to arginine by the addition of ammonia.
3. Arginine is hydrolyzed into urea and ornithine in the presence of
arginase.

Ornithine is regenerated, thus a cycle results. This is known as the ornitinine


cycle for urea formation.

The amount of urea formed is a measure of the oxidative degradation of


proteins. 16