Zobrazeno 1 - 10
of 88
pro vyhledávání: '"S. Pengthaisong"'
Autor:
Suwadee Chokchaisiri, Jaggaiah N. Gorantla, Santhi Maniganda, Lukana Ngiwsara, Jisnuson Svasti, Phannee Sawangareetrakul, S. Pengthaisong, James R. Ketudat Cairns, Prasat Kittakoop
Publikováno v:
ACS Omega
ACS Omega, Vol 6, Iss 39, Pp 25710-25719 (2021)
ACS Omega, Vol 6, Iss 39, Pp 25710-25719 (2021)
α-Glucosyl triazoles have rarely been tested as α-glucosidase inhibitors, partly due to inefficient synthesis of their precursor α-d-glucosylazide (αGA1). Glycosynthase enzymes, made by nucleophile mutations of retaining β-glucosidases, produce
Autor:
S. Pengthaisong, Jongjit Treekoon, Jaggaiah N. Gorantla, Rung-Yi Lai, James R. Ketudat-Cairns, Thitima Pewklang, Anyanee Kamkaew, Kantapat Chansaenpak
Publikováno v:
Organicbiomolecular chemistry. 19(26)
Compared with normal cells, cancer cells usually exhibit an increase in glucose uptake as part of the Warburg effect. To take advantage of this hallmark of cancer, glucose transporters could be a good candidate for cancer targeting. Herein, we report
Autor:
Vinich Promarak, Sunaree Choknud, Jaggaiah N. Gorantla, S. Pengthaisong, Teadkait Kaewpuang, James R. Ketudat Cairns, Tanaporn Manyum
Publikováno v:
RSC Advances. 9:6211-6220
The production of analytical amounts of azido sugars is used as a means of verifying catalytic acid/base mutations of retaining glycosidase, but application of this process to preparative synthesis has not been reported. The catalytic acid/base mutan
Autor:
Bodee Nutho, S. Pengthaisong, Anupong Tankrathok, Thanyada Rungrotmongkol, James R. Ketudat Cairns, Supot Hannongbua, Vannajan Sanghiran Lee
Publikováno v:
Biomolecules
Volume 10
Issue 6
Biomolecules, Vol 10, Iss 907, p 907 (2020)
Volume 10
Issue 6
Biomolecules, Vol 10, Iss 907, p 907 (2020)
&beta
Glucosidases and &beta
mannosidases hydrolyze substrates that differ only in the epimer of the nonreducing terminal sugar moiety, but most such enzymes show a strong preference for one activity or the other. Rice Os3BGlu7 and Os7BGlu2
Glucosidases and &beta
mannosidases hydrolyze substrates that differ only in the epimer of the nonreducing terminal sugar moiety, but most such enzymes show a strong preference for one activity or the other. Rice Os3BGlu7 and Os7BGlu2
Publikováno v:
Journal of Applied Science. 16:37-46
Publikováno v:
Archives of Biochemistry and Biophysics. 706:108924
Glycosynthases are glycoside hydrolase mutants that can synthesize oligosaccharides or glycosides from an inverted donor without hydrolysis of the products. Although glycosynthases have been characterized from a variety of glycoside hydrolase (GH) fa
Akademický článek
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Autor:
Hideaki Tanaka, Spencer J. Williams, Imogen Breen, S. Pengthaisong, Genji Kurisu, Sompong Sansenya, Liang Wu, Chomphunuch Songsiriritthigul, Gideon J. Davies, Risa Mutoh, James R. Ketudat Cairns, Yanling Hua, Anupong Tankrathok, Ratana Charoenwattanasatien
Publikováno v:
ACS Chemical Biology
Human glucosylcerebrosidase 2 (GBA2) of the CAZy family GH116 is responsible for the breakdown of glycosphingolipids on the cytoplasmic face of the endoplasmic reticulum and Golgi apparatus. Genetic defects in GBA2 result in spastic paraplegia and ce
Autor:
S. Pengthaisong, Supaporn Baiya, Maria Hrmova, Javier Iglesias-Fernández, Carme Rovira, Robert Robinson, Spencer J. Williams, James R. Ketudat Cairns, Rohan J. Williams, Z. Hakki, Anupong Tankrathok
Publikováno v:
ACS Catalysis. 5:6041-6051
Hydrolysis of β-d-mannosides by β-mannosidases typically proceeds via a B2,5 transition state conformation for the pyranoside ring, while that of β-d-glucosides by β-glucosidases proceeds through a distinct 4H3 transition state conformation. Howe
Akademický článek
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