product information
CAS number: 54-12-6
Groups: All Chemicals
IUPAC Name: 2-Amino-3-(1H-indol-3-yl)propanoic acid

CAS Number: 73-22-3

Chemical Formula: C11H12N2O2

Synonyms: 153-94-6, 162698_ALDRICH, 1H-Indole-3-alanine, 27813-82-7, 2-amino-3-(1H-indol-3-yl)propanoic acid, 2-amino-3-(1H-indol-3-yl)propionic acid, ()-2-Amino-3-(3-indolyl)propionic acid, 2-amino-3-indolylpropanic acid, 2-azanyl-3-(1H-indol-3-yl)propanoic acid, 54-12-6, 6912-86-3, 73-22-3, ACon1_001815, AI3-24395, ()-alpha-Amino-3-indolepropionic acid, alpha-amino-beta-3-indolepropionic acid, alpha-Amino-beta-(3-indolyl)-propionic acid, ARONIS003561, beta-3-indolylalanine, BSPBio_002938, C00806, C11H12N2O2, CCRIS 719, CHEBI:27897, CID1148, DL-3beta-Indolylalanine, DL-.alpha.-Amino-3-indolepropionic acid, DL-alpha-Amino-3-indolepropionic acid, DL-Tryptophan, DL-Trytophan, DL-Trytophane, D-Trypophan, D-Tryptophan, D-Trytophane, EH 121, EINECS 200-194-9, Htrp, IN1423, ITR, KBio2_000507, KBio2_003075, KBio2_005643, KBio3_002158, KBioGR_001018, KBioSS_000507, LS-7746, L-Trp, L-tryptophan, NCGC00094805-01, NCGC00094805-02, NCGC00094805-03, NCGC00094805-04, NCI60_000685, NCI-C01729, NCIOpen2_006535, NSC122286, NSC13118, NSC 13118, NSC13119, NSC97942, Pacitron, Propionic acid, 2-amino-3-indol-3-yl, Racemic Tryptophan, SDCCGMLS-0066645.P001, SPBio_001204, Spectrum_000087, SPECTRUM1500600, Spectrum2_001102, Spectrum3_001379, Spectrum4_000579, Spectrum5_001310, STK029637, T3300_SIGMA, T-8310, T-8320, triptofano, trofan, trp, tryptacin, tryptophan, (+-)-Tryptophan, Tryptophan, D-, TRYPTOPHAN, DL-, Tryptophane, Tryptophan, L-, WLN: T56 BMJ D1YZVQ -L

Product Info: Amino Acid is any of the organic compounds in which one (or more ) amino group (-NH2) and one (or more ) carboxylic acid group (-COOH) are both present with general formula R-CH(NH2)COOH containing carbon, hydrogen, oxygen, nitrogen, and in certain cases sulfur atoms. Two groups attached to the same carbon (called the alpha-carbon atom at the end of the compound) are polymerized to form peptides and proteins. The amine group is protonated to form -NH3+ at low pH. The carboxylic acid group is deprotonated to form -CO2- at high pH. The carbon atom in the carboxyl group of one amino acid binds covalently to the nitrogen atom in the amino group of another amino acid to form a peptide bond with the release of a water molecule. Proteins are synthesized through the covalent chemical polypeptide bonds. The sequence of these amino acids in the protein polypeptides determines the shape, properties, and hence biological role of the protein that function as chemical messengers and as intermediates in metabolism. Proteins are composed of various proportions of about 20 commonly occurring amino acids. Plants or other biological systems can synthesize amino acids from simple inorganic compounds, but animals rely on adequate supplies in their diet. More than 100 common amino acids occur in plants or in other microorganic systems. The 20 amino acids commonly found in animals are Alanine, Arginine, Asparagine, Aspartic Acid, Cysteine, Glutamic Acid, Glutamine, Glycine, Histidine, Isoleucine, Leucine, Lysine, Methionine, Phenylalanine, Proline, Serine, Threonine, Tryptophan, Tyrosine, and Valine. Many of the amino acids can be synthesized in the human or animal body from other cellular metabolites when needed (called Non-essential Amino Acids). Animals are not able to synthesize some amino acids necessary in metabolism in sufficient quantities. It must therefore be present in the diet (called Essential Amino Acids). In man, these essential amino acids are Arginine, Histidine, Isoleucine, Leucine, Lysine, Methionine, Phenylalanine, Threonine, Tryptophan and Valine. Tryptophan is formed from proteins during digestion by the action of proteolytic enzymes and is necessary for normal growth and development. Branched amino-acids (Valine, Isoleucine and Leucine ) with tryptophan and phenylalanine (aromatic side chain amino acids) contribute to the structure of protein by the tendency of its side chain composed only of carbon and hydrogen to participate in hydrophobic interactions which determines the tertiary structure of the peptide chain. Infants require greater amounts of tryptophan than adults. Only the l-stereoisomer is biologically active form in mammalian protein. Tryptophan is also a precursor for serotonin (a neurotransmitter), melatonin (a neurohormone) and niacin (a vitamin of the B complex).
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