Tryptophan Metabolism : Biosynthesis And Catabolism

All of the essential amino acids must be present in the body at the same time for growth and tissue repair because.

Amino Acids are essential nutrients that are the primary building blocks of proteins found in meat, dairy products, and legumes. Proteins make up 20 percent of the human body, and the amino acids that make up these proteins play a critical

The right combinations of food help to guarantee that the food an individual consumes is complete in its nutritional content of proteins, such as combining vegetables and grains that separately have incomplete proteins but together provide complete proteins (Grosvenor & Smolin, 2012). Out of the 20 amino acids the human body needs, only 11 of those are produced in the liver. The remaining amino acids must come from protein sources. If the consumption of grain and vegetables continues to occur together complete protein will continue to be part of a healthy diet.

Proteins are a perfect example. The 3D structure and folding determine the use of the protein, such as the protein becoming an enzyme to fuel cellular respiration. However, before folding can occur, amino acids, which are the monomers of proteins, must be joined together through dehydration synthesis. In order for a protein to be used within an organism’s body, the polypeptide chain must first be built. Dehydration synthesis occurs by reacting the carboxyl group of one amino acid with an amine group in another amino acid. This can be pictured in Figure 1. The OH from the carboxyl group is removed, along with a Hydrogen from the amine functional group. This results in the byproduct of water, which is later used by the cell. The Carbon in the carboxyl group forms a bond with the Nitrogen in the amino group, which is called a peptide bond. The final product of this reaction is an H2O molecule, and the start of a polypeptide chain. The protein that was made through dehydration synthesis can now be used throughout the body for a variety of different processes. The protein made can be used for tissue and cell repair. A large portion of organs and bones are comprised of protein. Other ways that the protein are used is to be made into enzymes that control reactions in the body such as cellular respiration. The creation of a protein strand via dehydration synthesis is not exclusive to

Beta-alanine occurs as a natural beta amino acid, with the amino group represented by the B-position which is from the carboxylate group. Beta-alanine is also called 3-aminopropanoic acid. Since it is naturally found in the body, the amino acid is non-essential, though are found in other diets through carnosine and somehow in balenine and anserine. The foods include meat, fish and poultry. But it beta-alanine is ingested by supplementation.

Treatment can prevent mental disabilities and other health problems for an individual with phenylketonuria, but there is no cure for phenylketonuria. Phenylalanine is an essential amino acid that occurs as a constituent of many proteins and is normally converted to tyrosine in the body. Individuals who they have phenylketonuria must follow a diet that has low levels of phenylalanine in them. This diet should be started from birth. This diet should also be strictly followed. This diet will be watched by a registered dietitian or doctor. Any products containing aspartame should be avoided. TPKU infants have many different special formulas that should be taken. Older children and adults use a different formula that provides protein in the amounts

This article explores the correlation between purine catabolism in relation to the degree of psychiatric manifestations early in the Schizophrenic disease process. The final product of purine catabolism is uric acid. Purine catabolism is a homeostatic response of mitochondria to oxidative stress which may offer protection against progressive mitochondria dysfunction in Schizophrenics.

Trifunctional protein (TFP) deficiency is a fatty acid oxidation disorder in which the body has difficulty breaking down fat into energy for the body to utilize. Although the body prefers metabolizing glucose as its main source of energy, there are limited amounts available. When the body has depleted these glycogen stores, the body turns to breaking down fats as an alternative source of energy especially during long periods without food such as sleeping or fasting (“Mitochondrial”).

Trypsin is classified as a serine protease which is found in the human digestive system, where it hydrolyses proteins. Trypsin is produced in the small intestine when its proenzyme form called trypsinogen is activated.

Tryptophan is an amino acid used for the synthesis of proteins. An example of a bacterium that takes up the tryptophan and uses it to build proteins is Escherichia coli. This bacterium can synthesize tryptophan using enzymes that are responsible for producing five genes that are located next to each other in a tryptophan (trp) operon. An operon consists of operator, promoter and the five genes it controls. The trp operon from E.coli is normally is “on” and the genes for tryptophan synthesis are transcribed. The E.coli only uses enzymes to synthesize tryptophan when there is none in the medium but if it is present, then the enzymes are no longer needed and the operon is turned off by a protein repressor. The protein repressor does this by

Serine is a non-essential amino acid (Carpenter 1994, p.133). De Koning et al. (2003) claims it was originally discovered in silk, the material spiders use to spin their webs. Within the human body, among other organisms, serine holds several roles regarding cell production. Such as, phospholipid synthesis (De Koning et al., 2003) Phospholipids are responsible for making up the phospholipid bilayer of the cell membrane. Additionally,

Special dietary requirements are formulated to control and minimize the effects of the enzyme deficiency however, that lifestyle is hard to maintain and many patients often chose a synthetic enzyme to overcome the disease such as Sapropterin Hydrochloride. (Phenylketonuria (PKU), 2015) Suboptimal outcomes in cognitive and executive functioning have been reported in patients who adhere poorly to dietary therapy. (NCIB, 2015) Oral administration of Sapropterin Hydrochloride, recently approved for use by the US Food and Drug Administration and the European Commission, is a novel approach for the treatment of phenylketonuria (PKU), one of the most common inborn errors of metabolism. PKU is caused by an inherited deficiency of the enzyme phenylalanine hydroxylase (PAH), and the pathophysiology of the disorder is related to chronic accumulation of the free amino acid phenylalanine in tissues. (New era in treatment for phenylketonuria: Pharmacologic therapy with sapropterin dihydrochloride, 2010) . Sapropterin dihydrochloride is a synthetic version of tetrahydrobiopterin, the naturally occurring pterin (a heterocyclic compound composed of a pteridine ring system) cofactor that is required for PAH-mediated phenylalanine hydroxylation. (pterin,

Unnatural peptides define as the chemical process to peptides consisting of different unnatural amino acids.1,2 Unnatural peptides consist of two carbon atoms between the carboxylate group and the amino group comparing to natural peptides, which consist of one carbon atom between the carboxylate group and the amino group.1,3 There are many kinds of unnatural amino acids such as β-peptides (β3 and β2), Homo-amino acids, Proline and Pyruvic acid derivatives and N-methyl amino acids.1,4 The β-peptides are more popular than another kind.3 Because they are more stable. In addition, they show high selectivity.3,5 The β-peptides have at least five helices structures such as 12-helix, 14-helix, 12/10-helix, 10-helix and 8-helix.3 The 12-helix, 14-helix

Campbell and Farrell define proteins as polymers of amino acids that have been covalently joined through peptide bonds to form amino acid chains (61). A short amino acid chain comprising of thirty amino acids forms a peptide, and a longer chain of amino acids forms a polypeptide or a protein. Each of the amino acids making up a protein, has a fundamental design that comprises of a central carbon or alpha carbon that is bonded to a hydrogen element, an amino grouping, a carboxyl grouping, and a unique side chain or the R-group (Campbell and Farrell 61).

The titration curve of the unknown exhibited many characteristics, such as equivalence points, pKa of ionizable groups, isoelectric point, and buffer regions, that are particularly distinct to lysine. For unclear reasons, the pH during the titration did not reach the pH for pure 0.2 M NaOH nor 0.2 M HCl and normal equivalence points expected at two extreme ends of the titration curves for all amino acids were not observed. The titration of a phosphate buffer showed that the buffer capacity is directly proportional to the molarity of the buffer. However, our results showed that although the initial pH of the phosphate buffer was less than the pKa value, the measured buffer capacity was higher towards acid than base. The accuracy of the pH meter and calibration process was questioned under assumptions that the pH of the prepared phosphate buffer was actually above pKa.