21016-88-6

Basic information

• Product Name: 1-(2-O,3-O-Diacetyl-β-D-arabinofuranosyl)uracil
• Synonyms: 1-(2-O,3-O-Diacetyl-β-D-arabinofuranosyl)uracil;2',3'-di-O-acetyl-1-beta-D-arabinofuranosyluracil;2',3'-O-Ac-uridine
• CAS NO: 21016-88-6
• Molecular Formula: C₁₃H₁₆N₂O₈
• Molecular Weight: 328.27474
• Mol File: 21016-88-6.mol
• Article Data: 4

Chemical Properties

• Appearance: /
• CAS DataBase Reference: 1-(2-O,3-O-Diacetyl-β-D-arabinofuranosyl)uracil(CAS DataBase Reference)
• NIST Chemistry Reference: 1-(2-O,3-O-Diacetyl-β-D-arabinofuranosyl)uracil(21016-88-6)
• EPA Substance Registry System: 1-(2-O,3-O-Diacetyl-β-D-arabinofuranosyl)uracil(21016-88-6)

Safety Data

• Hazardous Substances Data: 21016-88-6(Hazardous Substances Data)

Upstream product

• 14057-18-2 1-(2,3,5-tri-O-acetyl-β-D-arabinofuranosyl)uracil 
• 87418-73-3 5'-O-monomethoxytritylarabinouridine 
• 87875-12-5 Acetic acid (2R,3R,4S,5R)-4-acetoxy-5-(2,4-dioxo-3,4-dihydro-2H-pyrimidin-1-yl)-2-[(4-methoxy-phenyl)-diphenyl-methoxymethyl]-tetrahydro-furan-3-yl ester 

Downstream Products

• 122591-39-3 C₄₅H₄₆N₅O₁₆P 
• 14057-18-2 1-(2,3,5-tri-O-acetyl-β-D-arabinofuranosyl)uracil 
• 117626-83-2 Sodium; {[(2R,3S,4S,5R)-5-(5-bromo-2,4-dioxo-3,4-dihydro-2H-pyrimidin-1-yl)-3,4-dihydroxy-tetrahydro-furan-2-ylmethoxy]-hydroxy-phosphoryl}-acetate 

Relevant articles and documents

Immobilization of neutral protease from Bacillus subtilis for regioselective hydrolysis of acetylated nucleosides: Application to capecitabine synthesis

This paper describes the immobilization of the neutral protease from Bacillus subtilis and its application in the regioselective hydrolysis of acetylated nucleosides, including building blocks useful for the preparation of anticancer products. Regarding the immobilization study, different results have been obtained depending on the immobilization procedure. Epoxy hydrophobic carriers gave a poorly stable derivative that released almost 50% of the immobilized protein under the required reaction conditions. On the contrary, covalent immobilization on a differently activated hydrophilic carrier (agarose) resulted in very stable enzyme derivatives. In an attempt to explain the obtained enzyme immobilization results, the hypothetical localization of lysines on the enzyme surface was predicted in a 3D structure model of B. subtilis protease N built in silico by using the structure of Staphylococcus aureus metalloproteinase as the template. The immobilized enzyme shown a high regioselectivity in the hydrolysis of different peracetylated nucleosides. A stable enzyme derivative was obtained and successfully used in the development of efficient preparative bioprocesses for the hydrolysis of acetylated nucleosides, giving new intermediates for the synthesis of capecitabine in high yield.

A versatile synthesis of 5'-fenctionalized nucleosides through regioselective enzymatic hydrolysis of their peracetylated precursors

We describe a chemo-enzymatic synthesis of modified nucleosides through lipase-catalyzed hydrolysis of their peracetylated precursors. It was found from screening of a large number of substrates that these enzymesregioselectivities were affected by the sugar and the nucleobase structures. By selecting the best enzyme for each substrate in terms of activity and regioselectivity, we prepared a small library of differently monodeprotecled purine and pyrimidine nucleosides useful as intermediates for the synthesis of high-value nucleosides and mononucleotides. By this approach, the chemo-enzymatic preparation of doxifluridine (14) and uridine 5'-monophosphate (5'-UMP, 15) from peracetylated uridine 1 was carried out. Elimination of many of the processing stages associated with existing methods was achieved, and higher yields and products of increased purity were generated. Wiley-VCH Verlag GmbH & Co. KGaA.