134357-96-3

Basic information

• Product Name: THREONINE, L-, [3H(G)]
• Synonyms: THREONINE, L-, [3H(G)]
• CAS NO: 134357-96-3
• Molecular Formula: C4H8NO3T
• Molecular Weight: 121.13
• Mol File: 134357-96-3.mol
• Article Data: 375

Chemical Properties

• Appearance: /
• CAS DataBase Reference: THREONINE, L-, [3H(G)](CAS DataBase Reference)
• NIST Chemistry Reference: THREONINE, L-, [3H(G)](134357-96-3)
• EPA Substance Registry System: THREONINE, L-, [3H(G)](134357-96-3)

Safety Data

• Hazardous Substances Data: 134357-96-3(Hazardous Substances Data)

Upstream product

• 72-19-5 rac-allo-threonine 
• 855223-97-1 N-methyl-threonine 
• 7732-18-5 water 
• 66-72-8 pyridoxal 
• 75-07-0 acetaldehyde 
• 56-40-6 glycine 
• 67-63-0 isopropyl alcohol 
• 1494680-68-0 ohmyungsamycin A 
• 7505-36-4 N-formyl-O-methyl-D^s-threonine 
• 153893-46-0 N-chloroacetyl-L-threonine 
• 98432-01-0 methyl 2-acetamido-3-oxobutanoate 
• 72-19-5 L-threonine 
• 2280-40-2 D-threonine amide 
• 72-19-5 DL-threonine 

Downstream Products

• 24809-87-8 N-carbamoyl-threonine 
• 13881-40-8 2-Brom-3-hydroxy-buttersaeure 
• 64419-93-8 (Z)-5-ethylidene-2-thioxoimidazolidin-4-one 
• 72-19-5 L-threonine 
• 24830-94-2 D-allo-threonine 
• 28954-12-3 (2S,3S)-2-amino-3-hydroxybutanoic acid 
• 6293-94-3 N-[(2,4-dichloro-phenoxy)-acetyl]-D_s-threonine 
• 157355-81-2 (((9H-fluoren-9-yl)methoxy)carbonyl)-D-threonine 
• 130674-54-3 (2R,3R)-2-N-(9-fluorenylmethyloxycarbonyl)-D-allothreonine 

Relevant articles and documents

Structural determination of stevastelins, novel depsipeptides from Penicillium sp.

Structures of novel immunosuppressants, stevastelin A, B and B31) were determined by their spectroscopic and chemical studies. Three stevastelins were shown to be cyclic depsipeptides composed of a fatty acid and three amino acid moieties. The sequence of these moieties was determined to be as 3,5-dihydroxy-2,4-dimethylstearylvalylthreonyl (or O-sulfonylthreonyl in stevastelin A)-O-acetylserine. Cyclic structures were shown to be formed by ester linkages between the carboxylic group of the O-acetylserine moiety and the 5-hydroxy group of the fatty acid moiety in stevastelin A and B, and the 3-hydroxy group of the fatty acid moiety in stevastelin B3.

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.

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Foxo3a Inhibitors of Microbial Origin, JBIR-141 and JBIR-142

JBIR-141 (1) and JBIR-142 (2) were discovered as potent Foxo3a inhibitors that consist of three quite unique substructures, a 1-((dimethylamino)ethyl)-5-methyl-4,5-dihydrooxazole-4-carboxylic acid that is originated from Ala-Thr amino acid residues, a 3-acetoxy-4-amino-7-(hydroxy(nitroso)amino)-2,2-dimethylheptanoic acid, and an α-acyl tetramic acid fused with a 2-methylpropan-1-ol moiety. Their structures involving absolute configurations were determined by spectroscopic data, chemical degradation, anisotropy methods, and LC-MS analyses of diastereomeric derivatives. Compounds 1 and 2 exhibited specific inhibition against Foxo3a transcriptional activity with IC50 values of 23.1 and 166.2 nM, respectively.

TMC-89A and B, new proteasome inhibitors from Streptomyces sp. TC 1087

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High fermentative production of L-threonine from acetate by a Brevibacterium flavum stabilized strain transformed with a recombinant plasmid carrying the Escherichia coli thr operon.

Decrease in L-threonine productivity caused not only by plasmid-free segregation but also by plasmid deletion was observed in a Brevibacterium flavum L-threonine producer when transformed with a recombinant plasmid carrying Escherichia coli thr operon. However, a recombinant strain, HT-16, was stabilized by the addition of trimethoprim (a selective marker on the vector) at concentration of 1000 micrograms/ml, which was rather higher than the minimum inhibitory one, into the stock culture medium. Strain HT-16 produced 64.4 g/liter of L-threonine, 30% higher than that of the host strain, after 92 h of cultivation in a small jar fermentor using acetic acid as a carbon source without trimethoprim.

Asymmetric Synthesis of allo-Threonine and Threonine; the Use of a Chiral Pyridoxal-like Pyridinophane-Zinc Complex as an Enzyme Mimic

allo-Threonine and threonine having 88 and 74percent enantiomeric excess (e.e.), respectively, were obtained in 1.7:1 ratio, by a biomimetic aldol condensation between acetaldehyde and the zinc chelate of a Schiff base produced from glycine and a chiral, pyridoxal-like pyridinophane derivative (2).

Ulleungamides A and B, Modified α,β-Dehydropipecolic Acid Containing Cyclic Depsipeptides from Streptomyces sp. KCB13F003

Two novel cyclic depsipeptides, ulleungamides A (1) and B (2), were isolated from cultures of terrestrial Streptomyces sp. Their structures were determined by analyses of spectroscopic data and various chemical transformations, including modified Mosher's method, advanced Marfey's method, PGME, GITC derivatizations, and Snatzke's method. Ulleungamides were determined to be a new class of peptides bearing unprecedented units, such as 5-hydroxy-6-methyl-2,3-dehydropipecolic acid, 4,5-dihydroxy-6-methyl-2,3-dehydropipecolic acid, and amino-linked 2-isopropylsuccinic acid. Ulleungamide A displayed growth inhibitory activity against Staphylococcus aureus and Salmonella typhimurium without cytotoxicity.

A novel thyroglobulin-binding lectin from the brown alga Hizikia fusiformis and its antioxidant activities

A lectin (HFL) was isolated from the brown alga, Hizikia fusiformis, through ion exchange on cellulose DE52 and HPLC with a TSK-gel G4000PWXL column. SDS-PAGE showed that HFL had a molecular mass of 16.1 kDa. The HPLC (with a TSK-gel G4000PWXL column) indicated that HFL is a tetramer in its native state. The total carbohydrate content was 41%. Glucose, galactose and fucose were the monosaccharide units of HFL, and the normalized mol% values were 6, 14 and 80, respectively. HFL contains a large amount of the acidic amino acid, Asx. The β-elimination reaction suggested that the oligosaccharide and peptide moieties of HFL may belong to the N-glucosidic linkage. The amino acid sequences, of about five segments of HFL, were acquired by MALDI-TOF/TOF, and the sequences have no homology with other lectins. HFL was found to agglutinate sheep erythrocytes. The hemagglutination activity was inhibited by thyroglobulin, from bovine thyroid, but not by any of the monosaccharides tested. The lectin reaction was independent of the presence of the divalent cation Ca2+. HFL showed free radical scavenging activity against hydroxyl, DPPH and ABTS+ radicals.

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Optical resolution by replacing crystallization of DL-threonine

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Studies on the Biosynthesis of Tabtoxin (Wildfire Toxin). Origin of the Carbonyl C-Atom of the β-Lactam Moiety from the C1-Pool

Re-isolation of Pseudomonas tabaci strain NCPPB 2730 from its host, the tobacco plant, led to an activation of the bacteria in order to produce the β-lactam dipeptide tabtoxin (Wildfire toxin, 1).Incorporation of several 14C-labelled amino acids, as well as L-methionine, L-- and L-aspartate, rac-glycerol, and acetate into isotabtoxin (2) demonstrated that the building blocks of tabtoxin (1) are L-threonine, L-aspartate, the Me group of L-methionine and a C2-unit derived from the C3-pool.The Me gruop of L-methionine provides the carbonyl C-atom of the β-lactam moiety.These findings represent a novel pathway in β-lactam biosynthesis.Mechanistic aspects with respect to the β-lactam ring formation are discussed.A biradical 16 is proposed as an intermediate during the cyclization of a N-formyl-α-amino ketone 15.

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Heterologous production of asperipin-2a: Proposal for sequential oxidative macrocyclization by a fungi-specific DUF3328 oxidase

Asperipin-2a is a ribosomally synthesized and post-translationally modified peptide isolated from Asperigillus flavus. Herein, we report the heterologous production of asperipin-2a and determination of its absolute structure. Notably, the characteristic bicyclic structure was likely constructed by a single oxidase containing the DUF3328 domain.

The chemistry of pyridomycin.

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A New Cyclic Peptide, Ascidiacyclamide, isolated from Ascidian

A new cytotoxic cyclic peptide, ascidiacyclamide, has been isolated from ascidian and its structure has been elucidated by n.m.r. spectroscopy.

Grassystatins A-C from marine cyanobacteria, potent cathepsin E inhibitors that reduce antigen presentation

In our efforts to exploremarine cyanobacteria as a source of novel bioactive compounds, we discovered a statine unit-containing linear decadepsipeptide, grassystatin A (1), which we screened against a diverse set of 59 proteases. We describe the structure

New conjugates of muramyl dipeptide and nor-muramyl dipeptide linked to tuftsin and retro-tuftsin derivatives significantly influence their biological activity

The synthesis and biological activity of new conjugates of muramyl dipeptide (MDP) and nor-muramyl dipeptide (nor-MDP) with tuftsin and retro-tuftsin derivatives containing isopeptide bond between e-amino group of lysine and carboxyl group of simple amino

Structural Diversity and Anticancer Activity of Marine-Derived Elastase Inhibitors: Key Features and Mechanisms Mediating the Antimetastatic Effects in Invasive Breast Cancer

Three new 3-amino-6-hydroxy-2-piperidone (Ahp)-containing cyclic depsipeptides, named loggerpeptins A–C (1–3), along with molassamide (4), were discovered from a marine cyanobacterium, extending the structural diversity of this prevalent scaffold of cyanobacterial serine protease inhibitors. Molassamide, which contains a 2-amino-butenoic (Abu) unit in the cyclic core, was the most potent and selective analogue against human neutrophil elastase (HNE). Given the growing evidence supporting the role of HNE in breast cancer progression and metastasis, we assessed the cellular effects of compounds 3 and 4 in the context of targeting invasive breast cancer. Both compounds inhibited cleavage of the elastase substrate CD40 in biochemical assays; however, only 4 exhibited significant cellular activity. As CD40 and other receptor proteolytic processing culminates in NFκB activation, we assessed the effects of 4 on the expression of target genes, including ICAM-1. ICAM-1 is also a direct target of elastase and, in our studies, compound 4 attenuated both elastase-induced ICAM-1 gene expression and ICAM-1 proteolytic processing by elastase, revealing a potential dual effect on migration through modulation of gene expression and proteolytic processing. Molassamide also specifically inhibited the elastase-mediated migration of highly invasive triple-negative breast cancer cells.

Peptide bond hydrolysis catalyzed by the Wells-Dawson Zr(α 2-P2W17O61)2 polyoxometalate

In this paper we report the first example of peptide hydrolysis catalyzed by a polyoxometalate complex. A series of metal-substituted Wells-Dawson polyoxometalates were synthesized, and their hydrolytic activity toward the peptide bond in glycylglycine (GG) was examined. Among these, the Zr(IV)- and Hf(IV)-substituted ones were the most reactive. Detailed kinetic studies were performed with the Zr(IV)-substituted Wells-Dawson type polyoxometalate K 15H[Zr(α2-P2W17O 61)2]·25H2O which was shown to act as a catalyst for the hydrolysis of the peptide bond in GG. The speciation of K 15H[Zr(α2-P2W17O 61)2]·25H2O which is highly dependent on the pD, concentration, and temperature of the solution, was fully determined with the help of 31P NMR spectroscopy and its influence on the GG hydrolysis rate was examined. The highest reaction rate (kobs = 9.2 (±0.2) × 10-5 min-1) was observed at pD 5.0 and 60 °C. A 10-fold excess of GG was hydrolyzed in the presence of K 15H[Zr(α2-P2W17O 61)2]·25H2O proving the principles of catalysis. 13C NMR data suggested the coordination of GG to the Zr(IV) center in K15H[Zr(α2-P2W 17O61)2]·25H2O via its N-terminal amine group and amide carbonyl oxygen. These findings were confirmed by the inactivity of K15H[Zr(α2-P2W 17O61)2]·25H2O toward the N-blocked analogue acetamidoglycylglycinate and the inhibitory effect of oxalic, malic, and citric acid. Triglycine, tetraglycine, and pentaglycine were also fully hydrolyzed in the presence of K15H[Zr(α2- P2W17O61)2]·25H2O yielding glycine as the final product of hydrolysis. K15H[Zr(α 2-P2W17O61)2] ·25H2O also exhibited hydrolytic activity toward a series of other dipeptides.

Preparation of optically active allothreonine by separating from a diastereoisomeric mixture with threonine

A simple procedure is described to obtain D-and L-allothreonine (D-and L-aThr). A mixture of N-acetyl-D-allothreonine (Ac-D-aThr) and N-acetyl-L-threonine (Ac-L-Thr) was converted to a mixture of their ammonium salts and then treated with ethanol to precipitate ammonium N-acetyl-L- threoninate (Ac-L-Thr.NH3) as the less-soluble diastereoisomeric salt. After separating Ac-L-Thr.NH3 by filtration, Ac-D-aThr obtained from the filtrate was hydrolyzed in hydrochloric acid to give D-aThr of 80% de, recrystallized from water to give D-aThr of >99% de. L-aThr was obtained from a mixture of the ammonium salts of Ac-L-aThr and Ac-D-Thr in a similar manner.

Single-Cell-Based Screening and Engineering of d -Amino Acid Amidohydrolases Using Artificial Amidophenol Substrates and Microbial Biosensors

Enantiomerically pure d-amino acids are important intermediates as chiral building blocks for peptidomimetics and semisynthetic antibiotics. Here, a transcriptional factor-based screening strategy was used for the rapid screening of d-stereospecific amino acid amidase via an enzyme-specific amidophenol substrate. We used a d-threonine amidophenyl derivative to produce 2-aminophenol that serves as a putative enzyme indicator in the presence of d-threonine amidases. Comparative analyses of known bacterial species indicated that several Bacillus strains produce amidase and form putative indicators in culture media. The estimated amidase was cloned and subjected to rapid directed evolution through biosensor cells. Consequently, we characterized the F119A mutation that significantly improved the catalytic activity toward d-alanine, d-threonine, and d-glutamate. Its beneficial effects were confirmed by higher conversions and recurrent applications of the mutant enzyme, compared to the wild-type. This study showed that rapid directed evolution with biosensors coupled to designed substrates is useful to develop biocatalytic processes.

Cyclic Tetrapeptides with Synergistic Antifungal Activity from the Fungus Aspergillus westerdijkiae Using LC-MS/MS-Based Molecular Networking

Fungal natural products play a prominent role in the development of pharmaceuticalagents. Two new cyclic tetrapeptides (CTPs), westertide A (1) and B (2), with eight known compounds (3-10) were isolated from the fungus Aspergillus westerdijkiae guided by

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.