80-68-2 Usage
Description
DL-Threonine, also known as Threonine, is an essential polar α-amino acid with the chemical formula HO2CCH(NH2)CH(OH)CH3. It is one of the two proteinogenic amino acids bearing an alcohol group and has two chiral centers, resulting in four optical isomers: D-threonine, L-threonine, D-doxylthreonine, and L-doxylthreonine. The L-threonine isomer is the one that constitutes proteins, while the other isomers cannot be used. DL-Threonine appears as a white crystalline or crystalline powder, odorless with a slightly sweet taste, and has a stable chemical property.
Uses
Used in Biochemical Research:
DL-Threonine is used as a polar essential amino acid for biochemical research, serving as a precursor of glycine and used in the biosynthesis of proteins.
Used in Nutrition Enhancement:
DL-Threonine is used as a nutrition enhancer, playing a key role in regulating levels of other amino acids and supporting muscle tissue maintenance and growth.
Used in Animal Feed Industry:
DL-Threonine is used as an additive to animal feed, improving the health or production of animals by providing an essential amino acid that cannot be synthesized de novo in higher animals.
Used in Agriculture:
DL-Threonine is used in agriculture as a chelator of metal cations to improve the absorption of minerals from supplements and fertilizers, enhancing plant growth and health.
Used in Food Industry:
DL-Threonine can be co-used with other amino acids in various cereals, such as rice, wheat flour, barley, oats, and corn, to improve the nutritional value and enhance the flavor of the food products.
Used in Pharmaceutical Industry:
DL-Threonine can be used for the separation to obtain L-threonine, which is further used in the preparation of amino acid infusions and integrated amino acid preparations for medical purposes.
Occurrence:
Foods high in threonine include cottage cheese, poultry, fish, meat, lentils, black turtle beans, and sesame seeds.
Content analysis
It is the same as the content analysis method of "DL-alanine". Every mL of 0.1mol/L perchloric acid solution is equivalent to 11.91 mg of DL-threonine (C4H9NO3).
Toxicity
L-type: LD50: 26mmol/kg (rat, intraperitoneal injection); D-type: LD50 45mmol/kg (rat, intraperitoneal injection). It can be safely applied to food products (FDA, §172.320, 2000).
History
Threonine was discovered as the last of the 20 common proteinogenic amino acids in the 1930s by William Cumming Rose.
Biosynthesis
As an essential amino acid, threonine is not synthesized in humans, hence we must ingest threonine in the form of threoninecontaining proteins. In plants and microorganisms, threonine is synthesized from aspartic acid via α-aspartyl-semialdehyde and homoserine. Homoserine undergoes O-phosphorylation; this phosphate ester undergoes hydrolysis concomitant with relocation of the OH group. Enzymes involved in a typical biosynthesis of threonine include : aspartokinase β-aspartate semialdehyde dehydrogenase homoserine dehydrogenase homoserine kinase threonine synthase.
Synthesis Reference(s)
Tetrahedron Letters, 32, p. 1031, 1991 DOI: 10.1016/S0040-4039(00)74479-0The Journal of Organic Chemistry, 63, p. 3499, 1998 DOI: 10.1021/jo9722717
Metabolism
Threonine is metabolized in two ways: It is converted to pyruvate via threonine dehydrogenase. An intermediate in this pathway can undergo thiolysis with CoA to produce acetyl-CoA and glycine. In humans, it is converted to α-ketobutyrate in a less common pathway via the enzyme serine dehydratase, and thereby enters the pathway leading to succinyl-CoA..
Stereoisomerism
Threonine is one of two proteinogenic amino acids with two chiral centers. Threonine can exist in four possible stereo isomers with the following configurations: (2S,3R), (2R,3S), (2S,3S) and (2R,3R). However, the name L-threonine is used for one single diastereomer, (2S,3R)-2-amino-3-hydroxybutanoic acid. The second stereoisomer (2S,3S), which is rarely present in nature, is called L-allo-threonine. The two stereo isomers (2R,3S)- and (2R,3R)-2-amino-3-hydroxy butanoic acid are only of minor importance.
Check Digit Verification of cas no
The CAS Registry Mumber 80-68-2 includes 5 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 2 digits, 8 and 0 respectively; the second part has 2 digits, 6 and 8 respectively.
Calculate Digit Verification of CAS Registry Number 80-68:
(4*8)+(3*0)+(2*6)+(1*8)=52
52 % 10 = 2
So 80-68-2 is a valid CAS Registry Number.
InChI:InChI=1/C4H9NO3/c1-2(6)3(5)4(7)8/h2-3,6H,5H2,1H3,(H,7,8)
80-68-2Relevant articles and documents
Preparation and purification method of amino acid compound
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Paragraph 0066; 0067, (2018/06/21)
The invention relates to the field of industrial organic synthesis, in particular to a preparation and purification method of an amino acid compound. The method comprises the following steps that (1)alpha-amino nitrile compounds or hydantoin compounds or mixtures thereof are heated to react to obtain alpha-amino acid salt under the condition that volatile alkali and a suitable solvent exist; (2)after the alpha-amino acid salt obtained in step (1) is distilled, the alpha-amino acid salt is recrystallized in an organic solvent to obtain the alpha-amino acid compound. According to the method, reaction conditions are mild, materials can be recycled, and introduction of metal ions and use of ammonium carbonate salt are avoided, so that post-treatment is simple and no waste salt is generated.
Ohmyungsamycins A and B: Cytotoxic and antimicrobial cyclic peptides produced by Streptomyces sp. from a volcanic island
Um, Soohyun,Choi, Tae Joon,Kim, Heegyu,Kim, Byung Yong,Kim, Seong-Hwan,Lee, Sang Kook,Oh, Ki-Bong,Shin, Jongheon,Oh, Dong-Chan
, p. 12321 - 12329 (2014/01/17)
Ohmyungsamycins A and B (1 and 2), which are new cyclic peptides, were isolated from a marine bacterial strain belonging to the Streptomyces genus collected from a sand beach on Jeju, a volcanic island in the Republic of Korea. Based on the interpretation of the NMR, UV, and IR spectroscopic and MS data, the planar structures of 1 and 2 were elucidated as cyclic depsipeptides bearing unusual amino acid units, including N-methyl-4-methoxytrytophan, β-hydroxyphenylalanine, and N,N-dimethylvaline. The absolute configurations of the α-carbons of the amino acid residues were determined using the advanced Marfey's method. The configurations of the additional stereogenic centers at the β-carbons of the threonine, N-methylthreonine, and β-hydroxyphenylalanine units were assigned by GITC (2,3,4,6-tetra-O-acetyl- β-d-glucopyranosyl isothiocyanate) derivatization and the modified Mosher's method. We have developed a new method utilizing PGME (phenylglycine methyl ester) derivatization coupled with chromatographic analysis to determine the absolute configuration of N,N-dimethylvaline. Our first successful establishment of the absolute configuration of N,N-dimethylvaline using PGME will provide a general and convenient analytical method for determining the absolute configurations of amino acids with fully substituted amine groups. Ohmyungsamycins A and B showed significant inhibitory activities against diverse cancer cells as well as antibacterial effects.
Compositions and Methods for Binding Lysophosphatidic Acid
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, (2009/06/27)
Compositions and methods for making and using anti-LPA agents, for example, monoclonal antibodies, are described.
