product information
(+)-Aspartic acid
CAS number: 56-84-8
Groups: Pharmaceutical, Fine & Specialty Chemicals, Food Additives, All Chemicals, Animal Feed, Cosmetics
IUPAC Name: (2S)-2-aminobutanedioic acid

CAS Number: 56-84-8

Chemical Formula: C4H7NO4

Synonyms: (+)-Aspartic acid, (2S)-2-aminobutanedioic acid, (2S)-Aspartic acid, (L)-ASPARTIC ACID, (S)-(+)-Aminosuccinic acid, (S)-(+)-Aspartic acid, (S)-2-aminobutanedioic acid, (S)-2-Aminosuccinic acid, (S)-Aminobutanedioic acid, (S)-Aspartic acid, 1-amino-1,2-carboxyethane, 1115-63-5, 14007-45-5, 17090-93-6, 181119-33-5, 181119-34-6, 2-Aminosuccinic acid, 2001-89-0, 2068-80-6, 21059-46-1, 221628-95-1, 25608-40-6, 26834-87-7, 27881-03-4, 3792-50-5, 39162-75-9, 4-04-00-02998 (Beilstein Handbook Reference), 5598-53-8, 56-84-8, 6899-03-2, Acide aspartique [INN-French], Acido aspartico [INN-Spanish], Acidum asparticum, Acidum asparticum [INN-Latin], AI3-04461, AIDS-071820, AIDS071820, Aminosuccinic acid, ASP, ASP NH3+ COOH, Asparagic acid, Asparagic acid (VAN), Asparaginic acid, Asparaginic acid (VAN), Asparaginsaeure [German], Aspartate, Aspartate, L-, Aspartic acid, Aspartic acid (USP), Aspartic acid (VAN), Aspartic Acid [USAN:INN], Aspartic acid, L-, Aspartic acid, L- (8CI), Aspatofort, BRN 1723530, Butanedioic acid, amino-, (S)-, C00049, CCRIs 6181, CHEBI:17053, D00013, DL-Aspartic acid, homopolymer, EINECS 200-291-6, FEMA No. 3565, H-Asp-OH, HSDB 1430, L( )-Aminobernsteinsaeure, L-(+)-Aspartic acid, L-2-Aminobutanedioic acid, L-Aminosuccinic acid, L-Asparagic acid, L-Asparaginic acid, L-Asparaginsaeure, L-Asparaginsyra, L-Aspartate, L-Aspartic acid, L-Aspartic acid (9CI), L-Aspartic acid (JAN), L-Aspartic acid, homopolymer, L-Aspartinsaeure, NCGC00024499-01, nchembio816-comp6, NSC 3973, NSC3973, Poly-DL-succinimide, Polysuccinimide, Tocris-0214

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. Aspartic acid is a Non-Essential Amino Acid having an acidic carboxyl group on its side chain which can serve as both an acceptor and a donor of ammonia. It is converted to L-Asparagine by binding with ammonia. It forms Carbamyl-L-Aspartic acid which roles purine as well as pyrimidine biosynthesis. It has been shown to occur in enzyme sites including pepsin.
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