Proteins

Protein Metabolism
Proteins make up the structural tissue for muscles and tendons, transport oxygen or hemoglobin, catalyze all biochemical reactions as enzymes, and regulate reactions as hormones. Our bodies must be able to synthesize the many proteins, amino acids, and other non-protein nitrogen containing compounds needed for growth, replacement, and repair. Proteins in excess are used to supply energy or build reserves of glucose, glycogen, or lipids.

Digestion of Proteins
Mouth-No digestion occurs Stomach-Protein digestion starts

Gastrin-stimulates parietal cells to secrete HCl: chief cells of the gastric glands to secrete pepsinogen. Hydrochcloric acid- denatures protein structure -activates pepsinogen (zymogen to pepsin) Pepsin (gastric protease)- hydrolyzes proteins to smaller polypeptides and some free amino acid Pepsin cuts protein into peptides in the stomach Small Intestine- peptidases enzyme Secretin- stimulates the pancreas to secrete bicarbonate into the small intestine to neutralize the gastric HCl

Cholecystokinin- stimulates secretion of several pacreatic enzyme with activity optima ph 7-8. Trypsin (pancreatic protease) and chymotrypsin cut proteins and larger peptides into smaller peptides in the small intestine Aminopeptidase and carboxypeptidases A and B degrade peptides into amino acids in the small intestine Proteins are break down into: Tripeptides Dipeptides Free amino acids

Absorption of Amino acid

Whole proteins are not absorbed. Too large to pass

through the cell membranes intact. Hydrolases(digestive enzymes)- break peptide bonds Free amino acid small intestine (villi) Liver blood circulation

Deamination of Proteins
-the bodily process in which amino groups are removed from excess proteins -allows the system to convert excess amino acids into usable resources such as hydrogen and carbon The process also plays a vital role in removing nitrogen waste from the body. Amino groups discarded as a result of the process are converted into ammonia, which is later expelled from the body through urination.

 Liver- chief cite of deamination in the human body.

- Hydrolytic enzymes found in the organ separate the NH2 amino groups from proteins. The process leaves behind a carbon skeleton composed primarily of hydrogen, carbon, and oxygen. This skeleton can later be converted into usable glucose and lipids, indirectly making deamination one of the body's energyproducing mechanisms.

The Process of deamination

Amino groups removed via deamination bond with a

hydrogen molecule to form ammonia. Ammonia, however, is toxic to the human body and must be discarded. A separate chemical process combines the resulting ammonia with carbon dioxide, converting it into either urea or uric acid. Both compounds are diffused into the blood and later filtered out through the kidneys. The urea and uric acid are then expelled from the body via urination.

The Process Of Deamination

The process was at first thought to be one of simple hydrolysis R-CHNH2-COOH + HOH = R-CHOH-COOH + NH3 -Otto Neubauer, who first showed that the process of deamination- might be one oxidation and not, hydrolysis. R-CHNH2- COOH + O = R-CO-COOH + NH3 - this method of oxidation is actually possible in the organism

 Deamination is also an oxidative reaction that occurs

under aerobic conditions in all tissues but especially the liver. During oxidative deamination, an amino acid is converted into the corresponding keto acid by the removal of the amine functional group as ammonia and the amine functional group is replaced by the ketone group. The ammonia eventually goes into the urea cycle.

Nitrogen or Amino Acid pool

mixture of amino acids available in the cell derived

from dietary sources or the degradation of protein. Since proteins and amino acids are not stored in the body, there is a constant turnover of protein. Some protein is constantly being synthesized while other protein is being degraded.

Synthesis of New Amino Acids

these reactions can also be used to synthesize amino acids needed or not present in the diet. An amino acid may be synthesized if there is an available "root" ketoacid with a synthetic connection to the final amino acid. Since an appropriate "root" keto acid does not exist for eight amino acids, (lys, leu, ile, met, thr, try, val, phe), they are essential and must be included in the diet because they cannot be synthesized

 if there are excess proteins in the diet those amino acids converted into pyruvic acid and acetyl CoA can be converted into lipids by the lipogenesis

process. If carbohydrates are lacking in the diet or if glucose cannot get into the cells (as in diabetes), then those amino acids converted into pyruvic acid and oxaloacetic acids can be converted into glucose or glycogen. The hormones cortisone and cortisol from the adrenal cortex stimulate the synthesis of glucose from amino acids in the liver and also function as antagonists to insulin.

Bodys requirements in amount of protein:

ADULT MEN :minimum 56 grams per day or 0.8 grams of

protein /kg of boy weight ,or double 1.6 grams /kg if athletically active and building muscle ADULT WOMEN: minimum 46 grams /day or 0.8 grams of protein /kg of body weight, or double to 1.6 grams/kg if athletically active and building muscle

Metabolic pathways
series of chemical reactions occurring within a cell.
A metabolic pathway involves the step-by-step

modification of an initial molecule to form another product. The resulting product can be used in one of three ways: To be used immediately, To initiate another metabolic pathway, called a flux generating step To be stored by the cell

 the products of one reaction are the substrates for subsequent reactions
Metabolic pathways are often considered to flow in

one direction Glycolysis- was the first metabolic pathway discovered. In times of excess protein energy sources, certain reactions in the glycolysis pathway may run in reverse in order to produce glucose 6-phosphate which is then used for storage as glycogen or starch.

 Metabolic pathways are often regulated by feedback inhibition

Some metabolic pathways flow in a 'cycle' wherein each

component of the cycle is a substrate for the subsequent reaction in the cycle. Anabolic and catabolic pathways in eukaryotes often occur independently of each other, separated either physically by compartmentalization within organelles or separated biochemically by the requirement of different enzymes and co-factors.

Structure

OXIDATION OF AMINO ACID

oxidation of free amino acids and amino acid

residues of proteins are derived from radiolysis studies. most common pathway for the oxidation of simple aliphatic amino acids involves the hydroxyl radicalmediated abstraction of a hydrogen atom to form a carbon-centered radical at the alpha-position of the amino acid or amino acid residue in the polypeptide chain.

 Addition of O2 to the carbon-centered radicals leads to formation of proxy radical derivatives,

upon decomposition lead to production of NH3

and alpha-ketoacidosis, or to production of NH3, CO2, and aldehydes or carboxylic acids containing one less carbon atom. As the number of carbon atoms in the amino acid is increased, hydrogen abstraction at other positions in the carbon chain becomes more important and leads either to the formation of hydroxyl derivatives

 All amino acid residues in proteins are

subject to attack by hydroxyl radicals generated by ionizing radiation; however, the aromatic amino acids and sulfurcontaining amino acids are most sensitive to oxidation

Amino acids undergo oxidative catabolism under three circumstances:

Protein amino-acid residues from normal turnover are

recycled to generate energy and molecular components Dietary amino acids that exceed bodys protein synthesis needs are degraded Proteins in the body are broken down to supply amino acids for catabolism when carbohydrates are in short supply (starvation, diabetes mellitus),

UREA CYCLE

Oxidative phosphorylation or OXPHOS

-is the metabolic pathway in which the mitochondria in cells use their structure, enzymes, and energy released by the oxidation of nutrients to reform ATP. -during oxidative phosphorylation, electrons are transferred from electron donors to electron acceptors such as oxygen, in redox reactions. -is a vital part of metabolism, it produces reactive oxygen species such as superoxide and hydrogen peroxide, which lead to propagation of free radicals, damaging cells and contributing to disease and, possibly, aging (senescence).

 oxidative phosphorylation is a vital part of

metabolism, it produces reactive oxygen species such as superoxide and hydrogen peroxide, which lead to propagation of free radicals, damaging cells and contributing to disease and, possibly, aging (senescence).

Protein metabolism disorder

in which there is a deviation or interruption in the processing of proteins in the body.
- condition

Examples of protein metabolism disorders include:

1. Phenylketonuria

--often referred to as PKU, is one of the most common protein metabolism disorders. -their bodies have excess amounts of phenylalanine and low tyrosine levels.

untreated PKU: Lethargy Light pigment Eczema Intellectual disability Seizures Hyperactivity

2. Tyrosinemia
- occurs when an enzyme, called fumarylacetoacetase (FAH), is either missing or not working properly. - When FAH is not working, it cannot break down tyrosine.
Can Cause:serious liver and kidney damage

weakness or pain vomiting and diarrhea

3.Homocystinoria
- is an inherited disorder in which the body is unable to process certain building blocks of proteins (amino acids) properly. characterized by: nearsightedness (myopia), dislocation of the lens at the front of the eye, an increased risk of abnormal blood clotting, and brittle bones that are prone to fracture (osteoporosis)

 Untreated Homocystinuria may cause

intellectual disability, failure to grow and gain weight at the expected rate, problems with movement, blood disorder called megaloblastic anemia. Megaloblastic anemia- occurs when a person has a low number of red blood cells (anemia), and the remaining red blood cells are larger than normal (megaloblastic).

4. Maple Syrup Urine Disease

-is an inherited disorder in which the body is unable to process certain protein building blocks (amino acids) properly. The condition gets its name from the distinctive sweet odor of affected infants' urine.
A baby has the disorder may appear normal at birth. But

within three to four days, the symptoms appear. These may include: loss of appetite, fussiness, and sweet-smelling urine. The elevated levels of amino acids in the urine generate the smell, which is reminiscent of maple syrup. This is how MSUD got its name.
If untreated, maple syrup urine disease can lead to seizures,

coma, and death.

Treatment: - involved dietary restriction of the amino acids leucine, isoleucine, and valine. This treatment must begin very early to prevent brain damage. Babies with the disease must eat a special formula that does not contain the amino acids leucine, isoleucine, and valine. As the person grows to adulthood, he or she must always watch their diet, avoiding high protein foods such as meat, eggs, and nuts. -If levels of the three amino acids still get too high, patients can be treated with an intravenous (given through a vein) solution that helps the body use up excess leucine, isoleucine, and valine for protein synthesis.

-Gene therapy is also a potential future treatment for patients with MSUD. This would involve replacing the mutated gene with a good copy, allowing the patient's cells to generate a functional BCKD protein complex and break down the excess amino acids.

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