Papers

Peer-reviewed Lead author
Nov, 2015

An inverting beta-1,2-mannosidase belonging to glycoside hydrolase family 130 from Dyadobacter fermentans

FEBS LETTERS
  • Takanori Nihira(Co-first)
  • ,
  • Kazuhiro Chiku(Co-first)
  • ,
  • Erika Suzuki
  • ,
  • Mamoru Nishimoto
  • ,
  • Shinya Fushinobu
  • ,
  • Motomitsu Kitaoka
  • ,
  • Ken'ichi Ohtsubo
  • ,
  • Hiroyuki Nakai

Volume
589
Number
23
First page
3604
Last page
3610
Language
English
Publishing type
Research paper (scientific journal)
DOI
10.1016/j.febslet.2015.10.008
Publisher
ELSEVIER SCIENCE BV

The glycoside hydrolase family (GH) 130 is composed of inverting phosphorylases that catalyze reversible phosphorolysis of beta-D-mannosides. Here we report a glycoside hydrolase as a new member of GH130. Dfer_3176 from Dyadobacter fermentans showed no synthetic activity using alpha-D-mannose 1-phosphate but it released alpha-D-mannose from beta-1,2-mannooligosaccharides with an inversion of the anomeric configuration, indicating that Dfer_3176 is a beta-1,2-mannosidase. Mutational analysis indicated that two glutamic acid residues are critical for the hydrolysis of beta-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 beta-D-mannosidic bond. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Link information
DOI
https://doi.org/10.1016/j.febslet.2015.10.008
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/26476324
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000367232100014&DestApp=WOS_CPL
Research Projects
Elucidation of the Novel Phosphorylase-Dependent Metabolisms of Glycosonjugates and Lipopolysaccharides
URL
http://www.febsletters.org/article/S0014-5793(15)00889-3/abstract
ID information
  • DOI : 10.1016/j.febslet.2015.10.008
  • ISSN : 0014-5793
  • eISSN : 1873-3468
  • Pubmed ID : 26476324
  • Web of Science ID : WOS:000367232100014

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