23655-56-3

Upstream product

• 100-02-7 4-nitro-phenol 
• 75828-75-0 1,3,4,6-Tetra-O-acetyl-2-desoxy-α/β-D-lyxo-hexopyranose 
• 3068-32-4 1-bromo-2,3,4,6-tetra-O-acetyl-D-galactopyranose 
• 25878-60-8 D-galactose pentaacetate 
• 6605-32-9 1,3,4,6-tetra-O-acetyl-2-deoxy-α-D-lyxo-hexopyranose 

Downstream Products

• 23644-17-9 p-nitrophenyl 2-deoxy-α-D-xylo-hexopyranoside 

Relevant academic research and scientific papers

Facile TMSOTf-catalyzed preparation of 2-deoxy α-O-aryl-D-glycosides from glycosyl acetates

2-Deoxy a-O-aryl glycosides were conveniently obtained by reaction of 2-deoxy-glycosyl acetates with phenols in the presence of TMSOTf as the promoter. The current method provides the O-aryl glycosides with good to excellent yields, and sole alpha selecti

Hydrolytic activity of α-galactosidases against deoxy derivatives of p- nitrophenyl α-D-galactopyranoside

The four possible monodeoxy derivatives of p-nitrophenyl (PNP) α-D- galactopyranoside were synthesized, and hydrolytic activities of the α- galactosidase of green coffee bean, Mortierella vinacea and Aspergillus niger against them were elucidated. The 2- and 6-deoxy substrates were hydrolyzed by the enzymes from green coffee bean and M. vinacea, while they scarcely acted on the 3- and 4-deoxy compounds. On the other hand, A. niger α- galactosidase hydrolyzed only the 2-deoxy compound in these deoxy substrates, and the activity was very high. These results indicate that the presence of two hydroxyl groups (OH-3 and -4) is essential for the compounds to act as substrates for the enzymes of green coffee bean and M. vinacea, while the three hydroxyl groups (OH-3, -4, and -6) are necessary for the activity of the A. niger enzyme. The kinetic parameters (K(m) and V(max)) of the enzymes for the hydrolysis of PNP α-D-galactopyranoside and its deoxy derivatives were obtained from kinetic studies. (C) 2000 Elsevier Science Ltd.