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An inverting β‐1,2‐mannosidase belonging to glycoside hydrolase family 130 from Dyadobacter fermentans
Author(s) -
Nihira Takanori,
Chiku Kazuhiro,
Suzuki Erika,
Nishimoto Mamoru,
Fushinobu Shinya,
Kitaoka Motomitsu,
Ohtsubo Ken'ichi,
Nakai Hiroyuki
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.10.008
Subject(s) - phosphorolysis , glycoside hydrolase , chemistry , mannosidase , hydrolysis , mannose , anomer , stereochemistry , hydrolase , biochemistry , enzyme , purine nucleoside phosphorylase , purine
The glycoside hydrolase family (GH) 130 is composed of inverting phosphorylases that catalyze reversible phosphorolysis of β‐ d ‐mannosides. Here we report a glycoside hydrolase as a new member of GH130. Dfer_3176 from Dyadobacter fermentans showed no synthetic activity using α‐ d ‐mannose 1‐phosphate but it released α‐ d ‐mannose from β‐1,2‐mannooligosaccharides with an inversion of the anomeric configuration, indicating that Dfer_3176 is a β‐1,2‐mannosidase. Mutational analysis indicated that two glutamic acid residues are critical for the hydrolysis of β‐1,2‐mannotriose. The two residues are not conserved among GH130 phosphorylases and are predicted to assist the nucleophilic attack of a water molecule in the hydrolysis of the β‐ d ‐mannosidic bond.