24830-94-2

Usage

Uses

1. Used in Pharmaceutical Industry:
D(-)-allo-Threonine is used as a key intermediate for the synthesis of biologically active peptides and pharmaceutical compounds, such as thienamycin, due to its unique stereochemistry and presence in chiral and racemic syntheses.
2. Used in Research and Development:
D(-)-allo-Threonine is utilized as a research compound for the development of new drugs and therapies, particularly in the field of stereochemistry and peptide synthesis, as it contributes to the creation of novel chiral and racemic intermediates.
3. Used in Biochemical Studies:
As a constituent of biologically active peptides, D(-)-allo-Threonine is employed in biochemical studies to understand the structure, function, and interactions of these peptides in various biological processes.
4. Used in Drug Synthesis:
D(-)-allo-Threonine is used as a building block in the synthesis of various drugs, particularly those targeting specific biological pathways or receptors, due to its unique stereochemistry and ability to form chiral and racemic intermediates.

References

https://www.alfa.com/en/catalog/H27050/ http://www.sigmaaldrich.com/catalog/product/sigma/t9643?lang=en®ion=US

Purification Methods

Recrystallise D-allothreonine from aqueous EtOH or 50% EtOH. [Elliot J Chem Soc 62 1950, Birnbaum et al. J Biol Chem 194 455 1952, IR: Greenstein & Winitz The Chemistry of the Amino Acids J. Wiley, Vol 3 1961, Beilstein 4 IV 3170.]

InChI:InChI=1/C4H9NO3/c1-2(6)3(5)4(7)8/h2-3,6H,5H2,1H3,(H,7,8)/t2?,3-/m1/s1

Upstream product

• 72-19-5 rac-allo-threonine 
• 75-07-0 acetaldehyde 
• 56-40-6 glycine 
• 7732-18-5 water 
• 66-72-8 pyridoxal 
• 5431-93-6 ethyl 2-(acetylamino)-3-oxobutanoate 
• 64-19-7 acetic acid 
• 64-17-5 ethanol 
• 66508-93-8 ethyl 2-(hydroxyimino)-3-oxybutyrate 
• 108-24-7 acetic anhydride 
• 67-56-1 methanol 
• 5428-45-5 (+/-)-erythro-2-bromo-3-methoxy-butyric acid anilide 
• 7664-41-7 ammonia 
• 67-63-0 isopropyl alcohol 

Downstream Products

• 39994-75-7 (+/-) threonine methyl ester hydrochloride 
• 7537-02-2 threonine TMS 
• 56884-52-7 1-[6-anilino-5-hydroxy-2-(1-hydroxy-ethyl)-benzooxazol-4-yl]-ethanone 
• 3309-49-7 Cyclohexyloxycarbonyl-DL-threonin 
• 13881-40-8 2-Brom-3-hydroxy-buttersaeure 
• 3913-65-3 2-hydroxypropanal 
• 72-19-5 L-threonine 
• 72-19-5 D-threonine 
• 138-15-8 l-glutamic acid hydrochloride 
• 617-61-8 D-glutamic acid hydrochloride 
• 134124-43-9 N-Benzyl-N'-(1-carboxy-2-hydroxypropyl)urea 
• 92010-73-6 threonine di-p-fluorobenzoate 
• 86323-34-4 4-Nitro-benzoic acid 2-isopropoxycarbonyl-1-methyl-2-(4-nitro-benzoylamino)-ethyl ester 
• 86323-46-8 4-Nitro-benzoic acid 2-isopropoxycarbonyl-1-methyl-2-(4-nitro-benzoylamino)-ethyl ester 

Relevant academic research and scientific papers

Cβ-Selective Aldol Addition of d -Threonine Aldolase by Spatial Constraint of Aldehyde Binding

d-Threonine aldolase (DTA) is a useful biocatalyst that reversibly converts glycine and aldehyde to β-hydroxy-α-d-amino acid. However, low activity and poor diastereoselectivity limit its applications. Here we report DTA from Filomicrobium marinum (FmDTA) that shows much higher activity and Cβ-stereoselectivity in d-threonine production compared with those of other known DTAs. We determine the FmDTA structure at a 2.2 ? resolution and propose a DTA catalytic mechanism with a kernel of the Lys49 inner proton sink and metal ion in the aldol reaction cycle. The enzyme is rationally engineered to have high Cβ-stereoselectivity based on spatial constraint at the anti-specific aldehyde position in the mechanism, and the rational strategy is further applied to other DTAs for syn-production. The final FmDTAG179A/S312A variant exhibits a near-perfect 99.5% de value for d-threonine and maintains the de value above 93% even under kinetically unfavorable conditions. This study demonstrates how a detailed understanding of the reaction mechanism can be used for rational protein engineering.

Noncovalently Functionalized Commodity Polymers as Tailor-Made Additives for Stereoselective Crystallization

Stereoselective inhibition of the nucleation and crystal growth of one enantiomer aided by “tailor-made” polymeric additives is an efficient method to obtain enantiopure compounds. However, the conventional preparation of polymeric additives from chiral monomers are laborious and limited in structures, which impedes their rapid optimization and applicability. Herein, we report a “plug-and-play” strategy to facilitate synthesis by using commercially available achiral polymers as the platform to attach various chiral small molecules as the recognition side-chains through non-covalent interactions. A library of supramolecular polymers made up of two vinyl polymers and six small molecules were applied with seeds in the selective crystallization of seven racemates in different solvents. They showed good to excellent stereoselectivity in yielding crystals with high enantiomeric purities in conglomerates and racemic compound forming systems. This convenient, low-cost modular synthesis strategy of polymeric additives will allow for high-efficient, economical resolution of various racemates on different scales.

Mechanism of eukaryotic serine racemase-catalyzed serine dehydration

Eukaryotic serine racemase (SR) is a pyridoxal 5′-phosphate enzyme belonging to the Fold-type II group, which catalyzes serine racemization and is responsible for the synthesis of D-Ser, a co-agonist of the N-methyl-D-aspartate receptor. In addition to racemization, SR catalyzes the dehydration of D- and L-Ser to pyruvate and ammonia. The bifuctionality of SR is thought to be important for D-Ser homeostasis. SR catalyzes the racemization of D- and L-Ser with almost the same efficiency. In contrast, the rate of L-Ser dehydration catalyzed by SR is much higher than that of D-Ser dehydration. This has caused the argument that SR does not catalyze the direct D-Ser dehydration and that D-Ser is first converted to L-Ser, then dehydrated. In this study, we investigated the substrate and solvent isotope effect of dehydration of D- and L-Ser catalyzed by SR from Dictyostelium discoideum (DdSR) and demonstrated that the enzyme catalyzes direct D-Ser dehydration. Kinetic studies of dehydration of four Thr isomers catalyzed by D. discoideum and mouse SRs suggest that SR discriminates the substrate configuration at C3 but not at C2. This is probably the reason for the difference in efficiency between L- and D-Ser dehydration catalyzed by SR.

Synthesis of the Siderophore Coelichelin and Its Utility as a Probe in the Study of Bacterial Metal Sensing and Response

A convergent total synthesis of the siderophore coelichelin is described. The synthetic route also provided access to acetyl coelichelin and other congeners of the parent siderophore. The synthetic products were evaluated for their ability to bind ferric iron and promote growth of a siderophore-deficient strain of the Gram-negative bacterium Pseudomonas aeruginosa under iron restriction conditions. The results of these studies indicate coelichelin and several derivatives serve as ferric iron delivery vehicles for P. aeruginosa.

Chemical structure of cichorinotoxin, a cyclic lipodepsipeptide that is produced by Pseudomonas cichorii and causes varnish spots on lettuce

Pseudomonas cichorii, which causes varnish spots on lettuce and seriously damages lettuce production during the summer season in the highland areas of Japan (e.g., Nagano and Iwate prefectures) was isolated. The structure of a toxin produced by this organism was analyzed based on the detailed evaluation of its 2D NMR and FABMS spectra, and this compound has not been reported previously. We propose the name cichorinotoxin for this toxin. In conjunction with the D or L configurations of each amino acid, which were determined by Marfey’s method, we propose the structure of cichorinotoxin to be as follows: 3-hydroxydecanoyl-(Z)-dhThr1-D-Pro2-D-Ala3-D-Ala4-D-Ala5-D-Val6-D-Ala7-(Z)-dhThr8-Ala9-Val10-D-Ile11-Ser12-Ala13-Val14-Ala15-Val16-(Z)-dhThr17-D-alloThr18-Ala19-L-Dab20-Ser21-Val22, and an ester linkage is present between D-alloThr18 and Val22 (dhThr: 2-aminobut-2-enoic acid; Dab: 2,4-diaminobutanoic acid). Thus, the toxin is a lipodepsipeptide with 22 amino acids. The mono- and tetraacetate derivatives and two alkaline hydrolysates, compounds A and B, were prepared. We discuss here the structure–activity relationships between the derivatives and their necrotic activities toward lettuce.

Self-Reporting Inhibitors: A Single Crystallization Process To Obtain Two Optically Pure Enantiomers

Collection of two optically pure enantiomers in a single crystallization process can significantly increase the chiral separation efficiency but this is difficult to realize. Now a self-reporting strategy is presented for visualizing the crystallization process by a dyed self-assembled inhibitor made from the copolymers with tri(ethylene glycol)-grafting polymethylsiloxane as the main chain and poly(N6-methacryloyl-l-lysine) as side chains. When applied with seeds together for the fractional crystallization of conglomerates, the inhibitors can label the formation of the secondary crystals and guide the complete separation process of two enantiomers with colorless crystals as the first product and red crystals as the second. This method leads to high optical purity of d/l-Asn?H2O (99.9 % ee for d-crystals and 99.5 % for l-crystals) in a single crystallization process. It requires a small amount of additives and shows excellent recyclability.

Preparation and purification method of amino acid compound

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.

A α - amino acid compound synthesis and purification method

The invention relates to a synthesis and purification method for an alpha-amino acid compound. The synthesis and purification method is characterized by comprising the following steps: (1) adding substituted alpha-amino nitrile or a substituted hydantoin-based compound into alkali M(OH)x or metal oxide MxO, adding water or an alcohol and water mixed solvent, and heating for reaction to obtain alpha-amino acid salt; (2) adding ammonium carbonate or ammonium bicarbonate or introducing carbon dioxide into the solution in the step (1), separating to obtain filter liquor and precipitates MxHyCO3, performing reduced pressure concentration on the filter liquor, and recrystallizing in an alcohol solvent to obtain the alpha-amino acid compound (I). The synthesis and purification method for the alpha-amino acid compound is simple, the yield and purity of the obtained alpha-amino acid compound are high; furthermore, recycling utilization and cleaning production of materials can be realized; the synthesis and purification method is especially suitable for synthesis of the alpha-amino acid compound with high water solubility.

Cloning and characterization of D-threonine aldolase from the green alga Chlamydomonas reinhardtii

D-Threonine aldolase (DTA) catalyzes the pyridoxal 5’-phosphate (PLP)-dependent interconversion of D-threonine and glycine plus acetaldehyde. The enzyme is a powerful tool for the stereospecific synthesis of various β-hydroxy amino acids in synthetic organic chemistry. In this study, DTA from the green alga Chlamydomonas reinhardtii was discovered and characterized, representing the first report to describe the existence of eukaryotic DTA. DTA was overexpressed in recombinant Escherichia coli BL21 (DE3) cells; the specific activity of the enzyme in the cell-free extract was 0.8 U/mg. The recombinant enzyme was purified to homogeneity by ammonium sulfate fractionation, DEAE-Sepharose, and Mono Q column chromatographies (purified enzyme 7.0 U/mg). For the cleavage reaction, the optimal temperature and pH were 70?°C and pH 8.4, respectively. The enzyme demonstrated 90% of residual activity at 50?°C for 1?h. The enzyme catalyzed the synthesis of D- and D-allo threonine from a mixture of glycine and acetaldehyde (the diastereomer excess of D-threonine was 18%). DTA was activated by several divalent metal ions, including manganese, and was inhibited by PLP enzyme inhibitors and metalloenzyme inhibitors.

A new d-threonine aldolase as a promising biocatalyst for highly stereoselective preparation of chiral aromatic β-hydroxy-α-amino acids

d-Threonine aldolase is an enzyme belonging to the glycine-dependent aldolases, and it catalyzes the reversible aldol reaction of glycine and acetaldehyde to give d-threonine and/or d-allo-threonine. In this study, a putative d-threonine aldolase gene from Delftia sp. RIT313 was cloned and expressed in Escherichia coli BL21 (DE3). The purified enzyme (DrDTA, 47 KDa) exhibited 21.3 U mg-1 activity for the aldol addition of glycine and acetaldehyde in MES-NaOH buffer (pH 6.0) at 50 °C. Both pyridoxal 5′-phosphate and metal ions were needed for the reaction, and the existence of the metal ions enhanced the stability of the enzyme. It was found that the conversion and Cβ-stereoselectivity were dramatically influenced by the reaction temperature, co-solvent, amount of enzyme and reaction time, and it is possible to enable the reaction under kinetic control to retain suitable conversion and high stereoselectivity at the β-carbon, thus tackling the "Cβ-stereoselectivity problem". DrDTA showed high activity toward aromatic aldehydes with electron-withdrawing substituents. Under the optimized reaction conditions, phenylserines with a 2′-fluoro- or 3′-nitro-substituent were obtained with >90% conversion and >90% de. In addition, dl-threo-phenylserine and dl-threo-4-(methylsulfonyl)phenylserine were efficiently resolved with an excellent enantiomeric excess value (ee, >99%) using a whole cell biocatalyst in a two-phase system at 1.0 M and 0.3 M, respectively, the highest substrate concentration reported so far. These results suggested that DrDTA might be a promising biocatalyst for producing chiral aromatic β-hydroxy-α-amino acids.