23644-17-9Relevant articles and documents
Hydrolytic activity of α-galactosidases against deoxy derivatives of p- nitrophenyl α-D-galactopyranoside
Hakamata, Wataru,Nishio, Toshiyuki,Oku, Tadatake
, p. 107 - 115 (2007/10/03)
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.