264610-64-2

Upstream product

• 1005-56-7 phenylcarbonochloridothioate 
• 86420-70-4 methyl 2-O-benzoyl-4,6-O-benzylidene-α-D-galactopyranoside 
• 64552-06-3 methyl 4,6-O-benzylidene-α-D-galactopyranoside 
• 3396-99-4 methyl α-D-galactopyranoside 
• 100-52-7 benzaldehyde 

Downstream Products

• 264611-81-6 methyl 2-O-benzoyl-3-deoxy-4,6-O-benzylidene-α-D-xylo-hexopyranoside 
• 129185-20-2 Methyl-2,4,6-tri-O-benzoyl-3-desoxy-α-D-xylo-hexopyranosid 
• 264610-65-3 1-O-Acetyl-2,4,6-tri-O-benzoyl-3-desoxy-α,β-D-xylo-hexopyranose 
• 264610-66-4 p-nitrophenyl 2,4,6-tri-O-benzoyl-3-deoxy-α-D-xylo-hexopyranoside 

Relevant academic research and scientific papers

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.