19488-41-6Relevant articles and documents
A One-Pot Method for Removal of Thioacetyl Group via Desulfurization under Ultraviolet Light to Synthesize Deoxyglycosides
Ge, Jian-Tao,Zhou, Lang,Luo, Tao,Lv, Jian,Dong, Hai
supporting information, p. 5903 - 5906 (2019/08/26)
We herein developed an efficient method for removing thioacetyl to synthesize acylated deoxy glycosides in a one-pot reaction, where the thioacetyl was selectively deacetylated by hydrazine hydrate in DMF within 2-5 min at room temperature, followed by de
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.
NON-PEPTIDE PEPTIDOMIMETICS
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, (2008/06/13)
Compounds are provided which are crossreactive with peptides such as those which bind G-protein-linked receptors, together with preparative and therapeutic methods therefor. The compounds have the general structure: STR1 wherein at least one of R 1, R 2, R. sub.3, R. sub.4, or R 5 comprises a functional group which is chemically similar to that found in the peptide of interest.