The importance of the Abn2 calcium cluster in the endo-1,5-arabinanase activity from Bacillus subtilis

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3 Citations (Scopus)

Abstract

Arabinanase is a glycosyl hydrolase that is able to cleave the glycosidic bonds of α-1,5-L-arabinan, releasing arabino-oligosaccharides and L-arabinose. The enzyme has two domains, an N-terminal catalytic domain with a characteristic β-propeller fold and a C-terminal domain whose function is unknown. A calcium ion, located near the catalytic site, serves to stabilize the N-terminal domain, but it has also been proposed to play a key role in the enzyme mechanism. The present work describes the structure of an inactive mutant of the wild-type enzyme (H318Q) and in which the calcium ion has been adventitiously replaced by nickel. These structural studies, together with functional and modelling studies, clearly support the role of the calcium ion in the overall reaction mechanism.

Original languageEnglish
Pages (from-to)505-13
Number of pages9
JournalJournal Of Biological Inorganic Chemistry
Volume19
Issue number4-5
DOIs
Publication statusPublished - Jun 2014

Keywords

  • Bacillus subtilis
  • Calcium
  • Catalysis
  • Catalytic Domain
  • Crystallography, X-Ray
  • Glycoside Hydrolases
  • Models, Molecular
  • Mutagenesis, Site-Directed
  • Substrate Specificity
  • Journal Article
  • Research Support, Non-U.S. Gov't

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