33511-69-2

Usage

Uses

Used in Biochemistry and Organic Chemistry Research:
(2S,3R)-3-Methylglutamic acid is used as a research tool for studying protein structure and function, providing insights into the mechanisms of enzyme catalysis and protein folding.
Used in Pharmaceutical Synthesis:
(2S,3R)-3-Methylglutamic acid is used as a building block in the synthesis of various pharmaceuticals and other bioactive molecules, contributing to the development of new drugs and therapeutic agents.
Used in Neurological Disorder Treatment:
(2S,3R)-3-Methylglutamic acid has potential therapeutic applications for treating neurological disorders and neurodegenerative diseases, offering a promising avenue for the development of novel treatments and interventions.

Upstream product

• 129397-27-9 (2S,3R)-2-Dibenzylamino-3-methyl-pentanedioic acid 
• 83855-20-3 Neopeptin A 
• 83855-21-4 Neopeptin B 
• 89838-29-9 Neopeptin C 
• 910548-21-9 (3R)-3-methyl-2-oxoglutarate 
• 566169-86-6 (2S,3R)-3-Methyl-5-oxo-pyrrolidine-2-carboxylic acid tert-butyl ester 
• 160006-16-6 isopentyl (3R,2'S,5'R)-3-<5'-isopropyl-3',6'-dimethoxy-2',5'-dihydropyrazin-2'-yl>butanoate 
• 160006-15-5 1-isopropyl 5-methyl (2S,3R)-3-methyl-N-(trifluoroacetyl)glutamate 
• 137569-36-9 (3R,2'S,5'S)-3-<1'-(t-butoxycarbonyl)-2'-(t-butyl)-3'-methyl-4'-oxo-5'-imidazolidinyl>butanoic acid 
• 63088-04-0 threo-β-methylglutamic acid 
• 89838-36-8 N-MePhe-N-MeAsn-HyGln-MeGlu 
• 89838-34-6 C₅₃H₈₃N₁₁O₂₀ 
• 129397-19-9 (2R,3S)-2-Dibenzylamino-3-methyl-pentanedioic acid di-tert-butyl ester 
• 566169-84-4 (2S,3R)-2-Amino-3-methyl-pentanedioic acid 1-tert-butyl ester 5-ethyl ester 

Relevant academic research and scientific papers

Temperature-Dependent Enantio- and Diastereodivergent Synthesis of Amino Acids with One or Multiple Chiral Centers

A general and facile methodology for temperature-dependent enantiodivergent and diastereodivergent synthesis of amino acids with one or multiple chiral centers was developed. Camphor-based tricyclic iminolactones attack electrophiles from the endo face at low temperature (-78 to -40 °C) and from the exo face at high temperature (-10 to 25 °C).

Optically pure 3 - methyl glutamic acid derivatives preparation method

The invention discloses a preparation method of an optically pure 3-methyl glutamic acid derivative. The optically pure 3-methyl glutamic acid derivative is obtained through asymmetric Michael addition and a hydrolysis reaction of camphor-derived tricycloiminolactone and crotonate. The preparation method of the optically pure 3-methyl glutamic acid derivative is high in stereoselectivity and yield of an obtained product, low in production cost, and high in product purity and enantiomeric excess.

Isolation and structural elucidation of callipeltins J-M: antifungal peptides from the marine sponge Latrunculia sp.

Continued investigation of the polar extracts of the marine sponge Latrunculia sp. has resulted in the discovery of callipeltins J-M. The new structures were determined by interpretation of their NMR and MS data. The stereochemistry of the unusual 3-methy

Stereospecific enzymatic transformation of α-ketoglutarate to (2S,3R)-3-methyl glutamate during acidic lipopeptide biosynthesis

The acidic lipopeptides, including the calcium-dependent antibiotics (CDA), daptomycin, and A54145, are important macrocyclic peptide natural products produced by Streptomyces species. All three compounds contain a 3-methyl glutamate (3-MeGlu) as the penultimate C-terminal residue, which is important for bioactivity. Here, biochemical in vitro reconstitution of the 3-MeGlu biosynthetic pathway is presented, using exclusively enzymes from the CDA producer Streptomyces coelicolor. It is shown that the predicted 3-MeGlu methyltransferase GlmT and its homologues Dptl from the daptomycin producer Streptomyces roseosporus and Lptl from the A54145 producer Streptomyces fradiae do not methylate free glutamic acid, PCP-bound glutamate, or Glu-containing CDA in vitro. Instead, GlmT, Dptl, and Lptl are S-adenosyl methionine (SAM)-dependent α-ketoglutarate methyltransferases that catalyze the stereospecific methylation of α-ketoglutarate (αKG) leading to (3R)-3-methyl-2-oxoglutarate. Subsequent enzyme screening identified the branched chain amino acid transaminase IIvE (SCO5523) as an efficient catalyst for the transformation of (3R)-3-methyl-2-oxoglutarate into (2S,3R)-3-MeGlu. Comparison of reversed-phase HPLC retention time of dabsylated 3-MeGlu generated by the coupled enzymatic reaction with dabsylated synthetic standards confirmed complete stereocontrol during enzymatic catalysis. This stereospecific two-step conversion of αKG to (2S,3R)-3-MeGlu completes our understanding of the biosynthesis and incorporation of β-methylated amino acids into the nonribosomal lipopeptides. Finally, understanding this pathway may provide new possibilities for the production of modified peptides in engineered microbes.

Chemoenzymatic synthesis of glutamic acid analogues: Substrate specificity and synthetic applications of branched chain aminotransferase from Escherichia coli

(Chemical Equation Presented) A new route to α-keto acids is described, based on the ozonolysis of enol acetates obtained from α-substituted β-keto esters. Escherichia coli branched chain aminotransferase (BCAT) activity toward a variety of substituted 2-oxoglutaric acids was demonstrated analytically. BCAT was shown to have a broad substrate spectrum, complementary to that of aspartate aminotransferase, and to offer access to a variety of glutamic acid analogues. The usefulness of BCAT was demonstrated through the synthesis of several 3- and 4-substituted derivatives.

Polytheonamides A and B, highly cytotoxic, linear polypeptides with unprecedented structural features, from the marine sponge, Theonella swinhoei

Polytheonamides A and B are highly cytotoxic polypeptides with 48 amino acid residues isolated from the marine sponge, Theonella swinhoei. The structure of polytheonamide B was determined by spectral and chemical methods, especially extensive 2D NMR experiments, which resulted in the unprecedented polypeptide structure; the N-terminal glycine blocked with a 5,5-dimethyl-2-oxo-hexanoyl group, the presence of eight tert-leucine, three β-hydroxyvaline, six γ-N-methylasparagine, two γ-N-methyl-β-hydroxyasparagine, and β,β-dimethymethionine sulfoxide residues. More significantly, it has the sequence of alternating D-and L-amino acids. Polytheonamide A is an epimer of polytheonamide B differing only in the stereochemistry of the sulfoxide of the 44th residue.

A stereoselective synthesis of 3-substituted (S)-pyroglutamic and glutamic acids via OBO ester derivatives

(S)-Pyroglutamic acid is transformed to the Cbz-protected 4-methyl-2,6,7-trioxabicyclo[2.2.2] octane (OBO) ester. This ortho ester functionality is employed as a bulky steering group for stereoselective introduction of alkyl and aryl groups via 1,4-cuprate addition to 3,4-unsaturated pyroglutamates. After deprotection and ringopening, 3-substituted glutamic acids are obtained.

Glutamate transporter blockers: Enantiomerically pure (2S,3S)- and (2S,3R)-3-methyl glutamic acids

A short four-step synthesis of (2S,3R)- and (2S,3S)-3-methyl glutamic acids is reported; the (2S,3R) isomer presented a significant inhibitory effect on glutamate transport.

Synthesis of (2S,3R)- and (2S,3S)-3-Methylglutamic Acid

Arndt-Eistert homologation of suitably protected (2S,3S)-3-methylaspartic acid occurs with retention of configuration at C-3 to give, ultimately, (2S,3R)-3-methylglutamic acid. (2S,3R)-3-Methylglutamic acid was also prepared in good yield via the conjugate addition of the lithiated anion of the bis-lactim ether of cyclo-(R-Val-Gly) to methyl (E)-butenoate.The analogous reaction performed using isopentyl (Z)-butenoate ultimately gave (2S,3S)-3-methylglutamic acid.Both conjugate additions occured with high diastereoselectivity.

Resolution and regioselective protection of glutamic acid analogues. I- Resolution of diastereomeric α-boroxazolidone derivatives

Diastereomeric α-boroxazolidone γ-phenylethylamide (or γ-phenylethanolamide) derivatives of 2-, 3- or 4-substituted glutamic acid analogues have been separated by silicagel chromatography, resulting, after deprotection, in a practical method for the resolution of most of these unnatural amino acids.