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A β-mannan utilization locus in Bacteroides ovatus involves a GH36 α-galactosidase active on galactomannans.

Authors
  • Reddy, Sumitha K1
  • Bågenholm, Viktoria1
  • Pudlo, Nicholas A2
  • Bouraoui, Hanene1
  • Koropatkin, Nicole M2
  • Martens, Eric C2
  • Stålbrand, Henrik1
  • 1 Department of Biochemistry and Structural Biology, Lund University, Sweden. , (Sweden)
  • 2 Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, MI, USA.
Type
Published Article
Journal
FEBS letters
Publication Date
Jul 01, 2016
Volume
590
Issue
14
Pages
2106–2118
Identifiers
DOI: 10.1002/1873-3468.12250
PMID: 27288925
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

The Bacova_02091 gene in the β-mannan utilization locus of Bacteroides ovatus encodes a family GH36 α-galactosidase (BoGal36A), transcriptionally upregulated during growth on galactomannan. Characterization of recombinant BoGal36A reveals unique properties compared to other GH36 α-galactosidases, which preferentially hydrolyse terminal α-galactose in raffinose family oligosaccharides. BoGal36A prefers hydrolysing internal galactose substitutions from intact and depolymerized galactomannan. BoGal36A efficiently releases (> 90%) galactose from guar and locust bean galactomannans, resulting in precipitation of the polysaccharides. As compared to other GH36 structures, the BoGal36A 3D model displays a loop deletion, resulting in a wider active site cleft which likely can accommodate a galactose-substituted polymannose backbone. © 2016 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.

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