What is Phenylalanine and what does that do to us?
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They call it PKU because saying "phenylketonuria" over and over again is a mouthfull.  The "uria" ending at the end signifies that phenylketones appear in the urine.  People with PKU also usually have phenylketonemia (with the "emia" ending meaning that phenylketones appear in the blood).
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Tryptophan is an amino acid (part of a protein).  It is the stuff in turkey that makes you sleepy.
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If it's what I'm thinking of it's a drug to increase your metabolism used in weight loss. Usually any drug labeled with EP or EPH stands for ephedrinee which is actually illegal in the US but companies can get away with it if the ephedrin is still in the herbal form and not actually excreted!
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A single nucleotide change in a DNA sequence can result in a change in the codon that could then lead to a change in the amino acid that is made in the protein.  When proteins have a mutation in their amino acid sequence due to the change in DNA sequence, you can get a protein that no longer functions.  This often leads to a disease, and that is a profound effect on a phenotype.  If a DNA change occurs in the promoter of a gene, it's possible that gene which is normally transcribed won't be any more because the transcription factor does not bind recognize the new sequence.  You can also get frame shifts, which would result in a nonsense amino acid sequence.
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an essential amino acid, (C8H6N)CH2CH(NH2)COOH, colorless, crystalline, and aromatic, released from proteins by tryptic digestion and a precursor of serotonin\n\n\namytriptilyne\na white crystalline powder, C20H23N, used to treat depression and enuresis.
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Proteins, amino acids.
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It affects us at the DNA level by increasing the level of mutations.  These mutations can cause abnormal growths, cancerous cells, & other unpleasant things.\n\nHowever it is possible that some of these mutations could be benificial.
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thanks to God there r more urea than amino acids in our urines.otherwise we will face kidney failure very soon.amino acids are deaminated(removal of the amino group) to release ammonia.the ammonia is coverted to urea through the ornithine cycle while the keto acids(amino acids that have their amino group removed) can be metabolised.urea is excreted out of our body through kidneys via active secreation into the distal convoluted tubule.
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everyone is wrong, trust me, its glutamate, the ones you hear a lot about, serotonin, norepinephrine, epinephrine, are really rather scarce, acetylcholine is probably third or fourth behind gaba and probably glycine
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Protiens are denatured when body temperatures are raised. Protien shape is what gives them their function. The shape of protiens are changed, because the heat breaks the bonds which unravels the polypeptide chains, and ultimately their shape. When shape changes, they lose their function.
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peptide: Any of various natural or synthetic compounds containing two or more amino acids linked by the carboxyl group of one amino acid to the amino group of another.
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tryptophan a kind of amino acid
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Acceptor and a donor of ammonia, a compound toxic to the body.\n\nglutamic acid (gltăm´ĭk) is organic compound, one of the 20 amino acids commonly found in animal proteins. Only the L-stereoisomer occurs in mammalian proteins. Like aspartic acid, glutamic acid has an acidic carboxyl group on its side chain which can serve as both an acceptor and a donor of ammonia, a compound toxic to the body. Once glutamic acid has coupled with ammonia, it is called glutamine and can as such safely transport ammonia to the liver, where the ammonia is eventually converted to urea for excretion by the kidneys. Free glutamic acid (that not incorporated into proteins) can also be converted reversibly to α-ketoglutaric acid, an intermediate in the Krebs cycle, and as such can be degraded to carbon dioxide and water, or transformed into sugars. The acidic side chain of glutamic acid confers one negative charge under most conditions to proteins in which this amino acid is found, thus increasing the water solubility of the protein. Monosodium glutamate (MSG), the monosodium salt of L-glutamic acid, is widely used as a condiment. The amino acid was isolated from wheat gluten in 1866 and chemically synthesized in 1890. It is not essential to the human diet, since it can be synthesized in the body from the common intermediate α-ketoglutaric acid.
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It's the least reactive. It's non-polar. It's pKa is simply the average of the N and C terminus. It's also Ambivalent, meaning it can be inside and outside a protein. Because of these properties, if it was replaced with a polar AA, it would change the protein property, and in 99% of time, change in AA is deleterious.
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An enzyme is a protein that catalyzes, or speeds up, a chemical reaction. The word comes from the Greek ένζυμο, énsymo, which comes from én ("at" or "in") and simo ("leaven" or "yeast"). Certain RNAs also have catalytic activity, but to differentiate them from protein enzymes, they are referred to as RNA enzymes or ribozymes.\n\nEnzymes are essential to sustain life because most chemical reactions in biological cells would occur too slowly, or would lead to different products without enzymes. A malfunction (mutation, overproduction, underproduction or deletion) of a single critical enzyme can lead to a severe disease. For example, the most common type of phenylketonuria is caused by a single amino acid mutation in the enzyme phenylalanine hydroxylase, which catalyzes the first step in the degradation of phenylalanine. The resulting build-up of phenylalanine and related products can lead to mental retardation if the disease is untreated.\n\nLike all catalysts, enzymes work by providing an alternate pathway of lower activation energy of a reaction, thus allowing the reaction to proceed much faster. Enzymes may speed up reactions by a factor of many millions. An enzyme, like any catalyst, remains unaltered by the completed reaction and can therefore continue to function. Because enzymes do not affect the relative energy between the products and reagents, they do not affect equilibrium of a reaction. However, the advantage of enzymes compared to most other catalysts is their sterio-, regio- and chemoselectivity and specificity.\n\nEnzyme activity can be affected by other molecules. Inhibitors are naturally occurring or synthetic molecules that decrease or abolish enzyme activity; activators are molecules that increase activity. Some irreversible inhibitors bind enzymes very tightly, effectively inactivating them. Many drugs and poisons act by inhibiting enzymes. Aspirin inhibits the COX-1 and COX-2 enzymes that produce the inflammation messenger prostaglandin, thus suppressing pain and inflammation. The poison cyanide inhibits cytochrome c oxidase, which effectively blocks cellular respiration.\nEnzymes are usually specific as to the reactions they catalyze and the substrates that are involved in these reactions. Shape, charge complementarity, and hydrophillic/hydrophobic character of enzyme and substrate are responsible for this specificity
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Phenylketonuria (PKU) diet\n\nA low-protein diet is the main treatment for phenylketonuria (PKU). This is because people with PKU lack an enzyme to properly process the amino acid phenylalanine, a component of protein. PKU diets generally do not contain high-protein foods such meat, eggs, and nuts, or bread and wheat products.\n\nThe PKU diet may result in certain nutritional deficiencies. It is important that everyone with PKU see a specialist for nutritional counseling. This is especially important for those considering pregnancy.\n\nRead food labels carefully. Phenylalanine is present in all protein foods and in some nonprotein foods, such as soda pop and artificial sweeteners (for example, aspartame [such as Nutrasweet]). All foods that contain phenylalanine should have "contains phenylalanine" on the label. http://health.yahoo.com/ency/healthwise/ug1465\n\n What is Included in a Low Phenylalanine Food Pattern?\nThe diet for PKU consists of a phenylalanine-free medical formula and carefully measured amounts of fruits, vegetables, bread, pasta, and cereals. Many people who follow a low phenylalanine (phe) food pattern eat special low protein breads and pastas. They are nearly free of phe, allow greater freedom in food choices, and provide energy and variety in the food pattern. \n\nWhat is Not Included in a Low Phenylalanine Food Pattern?\nFoods that contain large amounts of phe must be eliminated from a low phe diet. These foods are high protein foods, such as milk, dairy products, meat, fish, chicken, eggs, beans, and nuts. These foods cause high blood phe levels for people with PKU.  \n \nA low phe diet helps most young adults with PKU to feel better and improves attention span, concentration, and memory. In general, young adults who have made these changes report that they think and feel better. The effort that it takes to bring down blood phe levels is well worth it for everyone, no matter how long they have been "off diet." \nhttp://depts.washington.edu/pku/diet.html