1186-90-9

Usage

Uses

Used in Nutritional Supplements:
(2S,3R)-2-amino-3-hydroxy-butanedioic acid is used as a nutritional supplement to support overall health and well-being. It helps in protein synthesis, which is essential for muscle growth and repair, and contributes to the formation of collagen and elastin, promoting healthy skin and connective tissue.
Used in Skincare Products:
(2S,3R)-2-amino-3-hydroxy-butanedioic acid is used as an ingredient in skincare products for its role in collagen and elastin formation. It helps maintain skin elasticity and suppleness, reducing the appearance of wrinkles and fine lines.
Used in Pharmaceutical Industry:
(2S,3R)-2-amino-3-hydroxy-butanedioic acid is used in the pharmaceutical industry for its potential benefits in liver health and immune function. It may be included in formulations to support liver health and enhance immune response.
Used in Food and Beverage Industry:
(2S,3R)-2-amino-3-hydroxy-butanedioic acid is used as a food additive to enhance the nutritional value of various products. It can be added to protein-rich foods, such as meat, dairy, and eggs, to increase their amino acid content and support overall health.
Used in Research and Development:
(2S,3R)-2-amino-3-hydroxy-butanedioic acid is used in research and development for its potential applications in various fields, such as pharmaceuticals, nutraceuticals, and cosmetics. It is studied for its role in protein synthesis, neurotransmitter production, and other biological processes to develop new products and therapies.

InChI:InChI=1/C4H7NO5/c5-1(3(7)8)2(6)4(9)10/h1-2,6H,5H2,(H,7,8)(H,9,10)/t1-,2+/m0/s1

Upstream product

• 7403-74-9 lower-melting inactive 3-chloro-2-hydroxy-succinic acid 
• 2706-75-4 sodium glyoxylate 
• 141-36-6 DL-trans-epoxysuccinic acid 
• 51274-37-4 2,3-trans-epoxysuccinic acid 
• 92653-33-3 N-Benzoyl-erythro-β-hydroxy-L(S)-asparaginsaeure-diethylester 
• 4294-45-5 DL-threo-β-hydroxyaspartic acid 
• 252580-08-8 (4S,5S)-2-phenyloxazoline-4,5-dicarboxylic acid dimethyl ester 
• 683228-02-6 (4S,5S)-2-Methyl-4,5-dihydro-oxazole-4,5-dicarboxylic acid dimethyl ester 
• 7440-44-0 pyrographite 
• 17015-08-6 (2R,3R)-oxirane-2,3-dicarboxylic acid 
• 56-40-6 glycine 
• 298-12-4 Glyoxilic acid 
• 71653-06-0 3-hydroxyaspartic acid 

Downstream Products

• 471242-80-5 erythro-β-Hydroxy-DL-asparaginsaeuredimethylester 
• 771456-08-7 DL-erythro-3-Hydroxy-asparaginsaeure-4-methylester 
• 5753-30-0 erythro-β-hydroxy-D-aspartic acid 
• 7298-98-8 2-(S)-amino-3-(R)-hydroxysuccinic acid 
• 71653-06-0 3-hydroxyaspartic acid 
• 603-54-3 N,N-diphenylurea 
• 87-69-4 tartaric acid 
• 26462-24-8 N-Benzyloxycarbonyl-threo-hydroxy-L-aspartic acid 
• 19516-01-9 (2S,3S)-2-amino-4-(benzyloxy)-3-hydroxy-4-oxobutanoic acid 
• 162553-93-7 β-Benzyl D-threo-β-hydroxyaspartate 
• 84035-04-1 L-threo-β-OH-Asp(OMe)-OH 

Relevant academic research and scientific papers

Genomics-driven discovery of taiwachelin, a lipopeptide siderophore from Cupriavidus taiwanensis

A genome mining study led to the identification of a previously unrecognised siderophore biosynthesis gene cluster in the nitrogen-fixing bacterium Cupriavidus taiwanensis LMG19424. Based upon predicted structural residues, a convenient strategy for an NMR-assisted isolation of the associated metabolite was designed. The structure of the purified siderophore, taiwachelin, was fully characterized by spectroscopic methods and chemical derivatisation.

Variochelins, Lipopeptide Siderophores from Variovorax boronicumulans Discovered by Genome Mining

Photoreactive siderophores have a major impact on the growth of planktonic organisms. To date, these molecules have mainly been reported from marine bacteria, although evidence is now accumulating that some terrestrial bacteria also harbor the biosynthetic potential for their production. In this paper, we describe the genomics-driven discovery and characterization of variochelins, lipopeptide siderophores from the bacterium Variovorax boronicumulans, which thrives in soil and freshwater habitats. Variochelins are different from most other lipopeptide siderophores in that their biosynthesis involves a polyketide synthase. We demonstrate that the ferric iron complex of variochelin A possesses photoreactive properties and present the MS-derived structures of two degradation products that emerge upon light exposure.

Isolation and amino acid sequence of a dehydratase acting on D-erythro-3- hydroxyaspartate from Pseudomonas sp. N99, and its application in the production of optically active 3-hydroxyaspartate

An enzyme catalyzing the ammonia-lyase reaction for the conversion of D-erythro-3-hydroxyaspartate to oxaloacetate was purified from the cell-free extract of a soil-isolated bacterium Pseudomonas sp. N99. The enzyme exhibited ammonia-lyase activity toward L-threo-3-hydroxyaspartate and D-erythro-3- hydroxyaspartate, but not toward other 3-hydroxyaspartate isomers. The deduced amino acid sequence of the enzyme, which belongs to the serine/ threonine dehydratase family, shows similarity to the sequence of L-threo-3-hydroxyaspartate ammonia- lyase (EC 4.3.1.16) from Pseudomonas sp. T62 (74%) and Saccharomyces cerevisiae (64%) and serine racemase from Schizosaccharomyces pombe (65%). These results suggest that the enzyme is similar to L-threo-3-hydroxyaspartate ammonia-lyase from Pseudomonas sp. T62, which does not act on D-erythro-3-hydroxyaspartate. We also then used the recombinant enzyme expressed in Escherichia coli to produce optically pure L-erythro-3-hydroxyaspartate and D-threo-3-hydroxyaspartate from the corresponding DL-racemic mixtures. The enzymatic resolution reported here is one of the simplest and the first enzymatic method that can be used for obtaining optically pure L-erythro-3-hydroxyaspartate.

Synthesis of 3-hydroxylated analogues of D-aspartic acid β-hydroxamate

The two isomers (2R,3R) and (2R,3S) of 3-hydroxy-D-aspartic acid β-hydroxamate were synthesised from diethyl tartrates via the corresponding diethyl 3-hydroxyaspartates.

Ambiguity of NRPS Structure Predictions: Four Bidentate Chelating Groups in the Siderophore Pacifibactin

Identified through a bioinformatics approach, a nonribosomal peptide synthetase gene cluster in Alcanivorax pacificus encodes the biosynthesis of the new siderophore pacifibactin. The structure of pacifibactin differs markedly from the bioinformatic prediction and contains four bidentate metal chelation sites, atypical for siderophores. Genome mining and structural characterization of pacifibactin is reported herein, as well as characterization of pacifibactin variants accessible due to a lack of adenylation domain fidelity during biosynthesis. A spectrophotometric titration of pacifibactin with Fe(III) and 13C NMR spectroscopy of the Ga(III)-pacifibactin complex establish 1:1 metal:pacifibactin coordination and reveal which of the bidentate binding groups are coordinated to the metal. The photoreaction of Fe(III)-pacifibactin, resulting from Fe(III) coordination of the β-hydroxyaspartic acid ligands, is reported.

Complete stereochemistry and preliminary structure-activity relationship of rakicidin A, a hypoxia-selective cytotoxin from micromonospora sp.

The complete stereochemistry of rakicidin A, a hypoxia-selective cytotoxin produced by Micromonospora sp., was unambiguously established by extensive chemical degradation and derivatization studies. During the PGME derivatization-based configurational analysis of 3-hydroxy-2,4,16-trimethylheptadecanoic acid, an irregular Δδ distribution was observed, which necessitated further acylation of the 3-hydroxy group to resolve the inconsistency. A hydrogenated derivative of rakicidin A, its ring-opened product, and two congeners with different alkyl chain lengths were tested for hypoxia-selective cytotoxicity. The results indicated that both the conjugated diene unit and appropriate chain length are essential for the unique activity of rakicidin A.

IMPROVED RESOLUTION OF beta -HYDROXY-DL-ASPARTIC ACID ON OPTICALLY ACTIVE RESIN CONTAINING L-LYSINE OR L-ORNITHINE. erythro

A series of experiments on column chromatography of the optically active resin containing L-lysine or L-ornithine were carried out with pyridinium acetate and ammonium acetate solvent systems as the eluents. threo- beta -Hydroxy-DL-aspartic acid was found to be resolved on the optically active resin containing L-lysine with ammonium acetate solvent system; erythro- beta -hydroxy-DL-aspartic acid could be resolved on that containing L-ornithine with pyridinium acetate solvent system. The threo or erthro racemate was resolved on a preparative scale, and the resolution including the complete characterization of enantiomers resolved was first accomplished.

Poecillastrin E, F, and G, cytotoxic chondropsin-type macrolides from a marine sponge Poecillastra sp.

Poecillastrin E (1), F (2), and G (3) were isolated from a marine sponge Poecillastra sp. as the cytotoxic constituents. Their planar structures were determined by analyzing the MS and NMR spectra. They are closely related to the known poecillastrin C (4). The absolute configuration of the β-hydroxyaspartic acid (OHAsp) residue was determined to be D-threo by Marfey's analysis of the hydrolysate. The mode of lactone ring formation of OHAsp residue in 1–3 was determined by selective reduction of the ester linkage followed by acid hydrolysis.

Stalobacin: Discovery of Novel Lipopeptide Antibiotics with Potent Antibacterial Activity against Multidrug-Resistant Bacteria

A novel lipopeptide antibiotic, stalobacin I (1), was discovered from a culture broth of an unidentified Gram-negative bacterium. Stalobacin I (1) had a unique chemical architecture composed of an upper and a lower half peptide sequence, which were linked via a hemiaminal methylene moiety. The sequence of 1 contained an unusual amino acid, carnosadine, 3,4-dihydroxyariginine, 3-hydroxyisoleucine, and 3-hydroxyaspartic acid, and a novel cyclopropyl fatty acid. The antibacterial activity of 1 against a broad range of drug-resistant Gram-positive bacteria was much stronger than those of last resort antibiotics such as vancomycin, linezolid, and telavancin (MIC 0.004-0.016 μg/mL). Furthermore, compound 1 induced a characteristic morphological change in Gram-positive and Gram-negative strains by inflating the bacterial cell body. The absolute configuration of a cyclopropyl amino acid, carnosadine, was determined by the synthetic study of its stereoisomers, which was an essential component for the strong activity of 1.

Rapid chemoenzymatic route to glutamate transporter inhibitor l-TFB-TBOA and related amino acids

The complex amino acid (l-threo)-3-[3-[4-(trifluoromethyl)benzoylamino]benzyloxy]aspartate (l-TFB-TBOA) and its derivatives are privileged compounds for studying the roles of excitatory amino acid transporters (EAATs) in regulation of glutamatergic neurotransmission, animal behavior, and in the pathogenesis of neurological diseases. The wide-spread use of l-TFB-TBOA stems from its high potency of EAAT inhibition and the lack of off-target binding to glutamate receptors. However, one of the main challenges in the evaluation of l-TFB-TBOA and its derivatives is the laborious synthesis of these compounds in stereoisomerically pure form. Here, we report an efficient and step-economic chemoenzymatic route that gives access to enantio- and diastereopure l-TFB-TBOA and its derivatives at multigram scale.