90899-85-7

Basic information

• Product Name: N-CARBAMYL-L-TYROSINE CRYSTALLINE
• Synonyms: N-CARBAMYL-L-TYROSINE CRYSTALLINE;N-carbamoyl-tyrosine
• CAS NO: 90899-85-7
• Molecular Formula: C₁₀H₁₂N₂O₄
• Molecular Weight: 224.21328
• Mol File: 90899-85-7.mol
• Article Data: 3

Chemical Properties

• Boiling Point: 481.4°Cat760mmHg
• Flash Point: 244.9°C
• Appearance: /
• Density: 1.416g/cm³
• Vapor Pressure: 4.45E-10mmHg at 25°C
• Refractive Index: 1.62
• CAS DataBase Reference: N-CARBAMYL-L-TYROSINE CRYSTALLINE(CAS DataBase Reference)
• NIST Chemistry Reference: N-CARBAMYL-L-TYROSINE CRYSTALLINE(90899-85-7)
• EPA Substance Registry System: N-CARBAMYL-L-TYROSINE CRYSTALLINE(90899-85-7)

Safety Data

• Hazardous Substances Data: 90899-85-7(Hazardous Substances Data)

Usage

InChI:InChI=1/C10H12N2O4/c11-10(16)12-8(9(14)15)5-6-1-3-7(13)4-2-6/h1-4,8,13H,5H2,(H,14,15)(H3,11,12,16)/t8-/m0/s1

Upstream product

• 590-28-3 potassium cyanate 
• 60-18-4 L-tyrosine 
• 57-13-6 urea 
• 58942-04-4 5-(4-hydroxy-benzyl)-imidazolidine-2,4-dione 

Downstream Products

• 1529780-90-2 (S)-3-(4-hydroxyphenyl)-2-(2-oxopyrimidin-1(2H)-yl)propionic acid methyl ester 
• 60-18-4 L-tyrosine 
• 3415-08-5 L-tyrosine N-carboxyanhydride 

Relevant articles and documents

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.

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.