14199-54-3Relevant articles and documents
Studies on the substrate specificity of a GDP-mannose pyrophosphorylase from Salmonella enterica
Zou, Lu,Zheng, Ruixiang Blake,Lowary, Todd L.
, p. 1219 - 1226 (2012/09/21)
A series of methoxy and deoxy derivatives of mannopyranose-1-phosphate (Manp-1P) were chemically synthesized, and their ability to be converted into the corresponding guanosine diphosphate mannopyranose (GDP-Manp) analogues by a pyrophosphorylase (GDP-ManPP) from Salmonella enterica was studied. Evaluation of methoxy analogues demonstrated that GDP-ManPP is intolerant of bulky substituents at the C-2, C-3, and C-4 positions, in turn suggesting that these positions are buried inside the enzyme active site. Additionally, both the 6-methoxy and 6-deoxy Manp-1P derivatives are good or moderate substrates for GDP-ManPP, thus indicating that the C-6 hydroxy group of the Manp-1P substrate is not required for binding to the enzyme. When taken into consideration with other previously published work, it appears that this enzyme has potential utility for the chemoenzymatic synthesis of GDP-Manp analogues, which are useful probes for studying enzymes that employ this sugar nucleotide as a substrate.
Synthesis of monomethyl derivatives of p-nitrophenyl α-d-gluco, galacto, and mannopyranosides and their hydrolytic properties against α-glycosidases
Hakamata, Wataru,Nishio, Toshiyuki,Sato, Reiko,Mochizuki, Takahiro,Tsuchiya, Kazuya,Yasuda, Maki,Oku, Tadatake
, p. 359 - 377 (2007/10/03)
All possible monomethyl derivatives of p-nitrophenyl α-D-gluco, galacto, and mannopyranosides were synthesized. Hydrolytic activities of α-glucosidase (rice), α-galactosidases (green coffee bean, Mortierella vinacea, and Aspergillus niger), and α-mannosidases (almond and jack bean) against them were elucidated. The 6-O-methyl galactopyranoside and mannopyranoside were hydrolyzed by the M. vinacea α-galactosidase and the almond and jack bean α-mannosidases, respectively, while these enzymes did not act on the 2-, 3-, and 4-O-methyl derivatives. On the other hand, rice α-glucosidase and green coffee bean and A. niger α-galactosidases had no hydrolyzing activities at all against the respective four monomethylated substrates.