54896-72-9

Upstream product

• 28607-46-7 (R)-phenylalanine benzyl ester p-toluenosulfonate 
• 3530-82-3 5-benzyl-hydantoin 
• 590-28-3 potassium cyanate 
• 673-06-3 D-(R)-phenylalanine 
• 37534-65-9 D-2-carbamoylamino-3-phenylpropionic acid 

Downstream Products

• 673-06-3 D-(R)-phenylalanine 
• 150-30-1 Phenylalanine 
• 1020666-20-9 tert-butyl 7-((R)-1-carboxy-2-phenylethyl)-6,8,10-trioxo-1,7,9-triaza-spiro[4.5]decane-1-carboxylate 
• 201231-65-4 (R)-4-Benzyl-3-[2-(triphenyl-λ⁵-phosphanylidene)-acetyl]-oxazolidin-2-one 
• 275378-91-1 ((R)-1-Hydroxymethyl-2-phenyl-ethyl)-urea 
• 184714-56-5 (R)-4-benzyl-3-(2-chloroacetyl)oxazolidin-2-one 
• 110905-24-3 (4R)-3-(bromoacetyl)-4-(phenylmethyl)-2-oxazolidinone 
• 40217-17-2 (R)-4-(phenylmethyl)-2-oxazolidinone 
• 275378-96-6 (R)-N-Carbamyl-phenylalanine methyl ester 
• 63-91-2 L-phenylalanine 
• 3530-82-3 5-benzyl-hydantoin 

Relevant academic research and scientific papers

Straightforward preparation of labeled potassium cyanate by ozonation and application to the synthesis of [13C] or [14C] ureidocarboxylic acids

The development of new efficient syntheses of labeled reagents is a great challenge. Avoidance of overcomplicated procedures, availability and cost of starting materials are important considerations in choosing the synthetic route. In this report, we desc

N-(Hydroxyaminocarbonyl)phenylalanine: A novel class of inhibitor for carboxypeptidase A

N-(Hydroxyaminocarbonyl)phenylalanine (1) was designed rationally as a new type of inhibitor for carboxypeptidase A (CPA). The designed inhibitor was readily prepared from phenylalnine benzyl ester in two steps and evaluated to find that rac-1 inhibits CP

N-carbamylamino alcohols as the precursors of oxazolidinones via nitrosation-deamination reaction

Oxazolidinones were effectively prepared from N-carbamylamino alcohols by treatment with nitrous acid, via N-nitroso compound as the intermediate. A new route to (R)-4-benzyloxazolidinone was developed starting from DL- phenylalanine, utilizing D-hydantoinase-catalyzed enantioselective hydrolysis of 5-benzylhydantoin under the dynamic kinetic resolution conditions, and the subsequent reduction to the precursor for the above-mentioned cyclization reaction, by taking advantage of the intermediates bearing an N-carbamylamino functionality.

New hydantoinases from thermophilic microorganisms - Synthesis of enantiomerically pure D-amino acids

A series of 14 D-α-amino acids were prepared in high chemical and optical yields from the corresponding racemic hydantoins by employing two novel hydantoinases from thermophilic microorganisms.

Mechanism of Asymmetric Production of L-Aromatic Amino Acids from the Corresponding Hydantoins by Flavobacterium sp.

The mechanism of asymmetric production of L-aromatic amino acids from the corresponding hydantoins by Flavobacterium sp.AJ-3912 was examined by investigating the properties of the enzymes involved in the hydrolysis of 5-substituted hydantoins corresponding to aromatic amino acids (AAH).The enzymatic hydrolysis of AAH by Flavobacterium sp.AJ-3912 consisted of the following two successive reactions; a hydrolytic ring opening reaction of DL-AAH to L- and D-form N-carbamyl aromatic amino acids (NCA), involving an enzyme (hydantoin hydrolase) followed by a hydrolytic cleaving reaction of the L-form NCA to L-aromatic amino acids involving another enzyme (N-carbamyl-L-aromatic amino acid hydrolase, abbreviated as L-NCA hydrolase).The ring opening reaction involving hydantoin hydrolase was not stereospecific, but the NCA cleaving reaction involving L-NCA hydrolase was completely L-specific.The pathway for the conversion of the by-produced D-form NCA to L-aromatic amino acids was as follows; conversion of D-form NCA to D-AAH through the reverse reaction of hydantoin hydrolase, and then conversion of the D-AAH to L-AAH through spontaneous racemization, followed by the successive hydrolysis of the L-AAH to L-aromatic amino acids by hydantoin hydrolase and L-NCA hydrolase.

Mechanism of Asymmetric Production of D-Amino Acids from the Corresponding Hydantoins by Pseudomonas sp.

The mechanism of asymmetric production of D-amino acids from the corresponding hydantoins by Pseudomonas sp.AJ-11220 was examined by investigating the properties of the enzymes involved in the hydrolysis of DL-5-substituted hydantoins.The enzymatic production of D-amino acids from the corresponding hydantoins by Pseudomonas sp.AJ-11220 involved the following two successive reactions; the D-isomer specific hydrolysis, i.e., the ring opening of D-5-substituted hydantoins to D-form N-carbamyl amino acids by an enzyme, D-hydantoin hydrolase (D-HYD hydrolase), followed by the D-isomer specific hydrolysis, i.e., the cleavage of N-carbamyl-D-amino acids to D-amino acids by an enzyme, N-carbamyl-D-amino acid hydrolase (D-NCA hydrolase).L-5-Substituted hydantoins not hydrolyzed by D-HYD hydrolase were converted to D-form 5-substituted hydantoins through spontaneous racemization under the enzymatic reaction conditions.It was proposed that almost all of the DL-5-substituted hydantoins were stoichiometrically and directly converted to the corresponding D-amino acids through the successive reactions of D-HYD hydrolase and D-NCA hydrolase in parallel with the spontaneous racemization of L-5-substituted hydantoins to those of DL-form.

Neuroleptic Activity of Chiral trans-Hexahydro-γ-carbolines

A series of trans-8-fluoro-5-(4-fluorophenyl)-2,3,4,4a,5,9b-hexahydro-1H-pyridoindoles with various N-2 substituents has been prepared and tested for neuroleptic activity (3H>spiroperidol binding and amphetamine antagonism).Several memb

Obtention d'amino acides optiquement actifs a l'aide d'hydantoinases

5-substituted hydantoines are intermediates in the Bucherer synthesis, the most widely used chemical synthesis of α-aminoacids.Enzymatic hydrolysis of these intermediates with hydantoinases leads to asymetric synthesis of optically active aminoacids.The enzymatic activities of two microbial strains are described: a Pseudomonas Sp. and an Arthrobacter globiformis, which catalyze the hydrolysis of a wide variety of hydantoines into D and L α-aminoacids respectively.In both cases, it was noticed that α-ureido (or 2-carbamoyl acids) are the reactive intermediates.Evidence is provided for the existence of a racemase.The experimental conditions for the culture of Arthrobacter are briefly described.