89595-64-2

Basic information

• Product Name: N-CARBAMYL-L-TRYPTOPHAN
• Synonyms: N-CARBAMYL-L-TRYPTOPHAN
• CAS NO: 89595-64-2
• Molecular Formula: C₁₂H₁₃N₃O₃
• Molecular Weight: 247.24992
• Mol File: 89595-64-2.mol

Chemical Properties

• Melting Point: 198 °C
• Boiling Point: 538.4±50.0 °C(Predicted)
• Appearance: /
• Density: 1.434±0.06 g/cm3(Predicted)
• Storage Temp.: −20°C
• PKA: 3.88±0.10(Predicted)
• CAS DataBase Reference: N-CARBAMYL-L-TRYPTOPHAN(CAS DataBase Reference)
• NIST Chemistry Reference: N-CARBAMYL-L-TRYPTOPHAN(89595-64-2)
• EPA Substance Registry System: N-CARBAMYL-L-TRYPTOPHAN(89595-64-2)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 89595-64-2(Hazardous Substances Data)

Upstream product

• 590-28-3 potassium cyanate 
• 73-22-3 L-Tryptophan 
• 108605-53-4 DL-5-indolylmethylhydantoin 
• 57-13-6 urea 

Downstream Products

• 40856-80-2 L-tryptophan hydantoin 
• 73-22-3 L-Tryptophan 

Relevant articles and documents

Docking and Linking of Fragments to Discover Jumonji Histone Demethylase Inhibitors

Development of tool molecules that inhibit Jumonji demethylases allows for the investigation of cancer-associated transcription. While scaffolds such as 2,4-pyridinedicarboxylic acid (2,4-PDCA) are potent inhibitors, they exhibit limited selectivity. To discover new inhibitors for the KDM4 demethylases, enzymes overexpressed in several cancers, we docked a library of 600a€ˉ000 fragments into the high-resolution structure of KDM4A. Among the most interesting chemotypes were the 5-aminosalicylates, which docked in two distinct but overlapping orientations. Docking poses informed the design of covalently linked fragment compounds, which were further derivatized. This combined approach improved affinity by ～3 log-orders to yield compound 35 (Ki = 43 nM). Several hybrid inhibitors were selective for KDM4C over the related enzymes FIH, KDM2A, and KDM6B while lacking selectivity against the KDM3 and KDM5 subfamilies. Cocrystal structures corroborated the docking predictions. This study extends the use of structure-based docking from fragment discovery to fragment linking optimization, yielding novel KDM4 inhibitors.

Efficient syntheses of 13C- and 14C-labelled 5-benzyl and 5-indolylmethyl L-hydantoins

Robust and straightforward methods are described for the first syntheses of highly pure 13C- and 14C-labelled L-5-benzylhydantoin (L-BH) and L-5-indolylmethylhydantoin (L-IMH) by cyclizing the amino acids L-phenylalanine and L-trypto

Rapid and efficient microwave-assisted synthesis of N-carbamoyl-L-amino acids

A rapid and efficient method for the synthesis of N-carbamoyl-L-amino acids is reported. The procedure, involving the reaction between urea and α-amino acids sodium salts, was performed under microwave conditions using an unmodified domestic microwave oven. A careful study of the operative conditions indicated proline (1d) as the less reactive substrate and phenylglycine (1e) as the more reactive one among all the α-amino acids tested. Substitution of urea with potassium cyanate produced a low conversion into the corresponding N-carbamoyl derivative, and a possible explanation of this result is reported. Copyright Taylor & Francis Group, LLC.

A new biocatalytic route to enantiopure N-carbamoyl amino acids by fast enzyme screening

The enantioselective enzymatic deamidation of (rac)-N-carbamoyl amino acid amides (Cbm-AA-NH2) to enantiopure (L)-N-carbamoyl amino acids (Cbm-AA-OH) is described for the first time. Via fast screening methods of biocatalysts several proteases like Chirazyme P1, Chirazyme P2 and Subtilisin were identified, which give conversions of up to 47% and >98% ee. This conversion is most productive on aliphatic and primary amino acids.

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.