Premium
Active Site Protonation of 1‐Azafagomine in Glucosidases Studied by Solid‐State NMR Spectroscopy
Author(s) -
Sivertsen Astrid C.,
Gasior Magdalena,
Bjerring Morten,
Hansen Steen U.,
Lopez Lopez Oscar,
Nielsen Niels C.,
Bols Mikael
Publication year - 2007
Publication title -
european journal of organic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 1434-193X
DOI - 10.1002/ejoc.200600816
Subject(s) - chemistry , protonation , anomer , chemical shift , aspergillus niger , nuclear magnetic resonance spectroscopy , active site , spectroscopy , stereochemistry , enzyme , organic chemistry , biochemistry , ion , physics , quantum mechanics
Protonation of an azasugar inhibitor inside the active site of a glycosidase has been studied by solid‐state NMR spectroscopy. By measuring 13 C chemical shifts of azafagomine bound to yeast α‐glucosidase, almond β‐glucosidase, and Aspergillus niger glucoamylase, and 15 N chemical shift ofazafagomine bound to β‐glucosidase, we find evidence for an N1‐protonation of azafagomine inside β‐glucosidase. For α‐glucosidase and glucoamylase the corresponding chemical shifts are similar to those of the non‐protonated inhibitor, which shows that charge stabilization at anomeric position is not occurring in these enzymes.(© Wiley‐VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2007)