Structure of a Bacillus halmapalus family 13 alpha-amylase, BHA, in complex with an acarbose-derived nonasaccharide at 2.1 angstrom resolution

G J Davies, A M Brzozowski, Z Dauter, M D Rasmussen, T V Borchert, K S Wilson

Research output: Contribution to journalArticlepeer-review

Abstract

The enzymatic digestion of starch by alpha-amylases is one of the key biotechnological reactions of recent times. In the search for industrial biocatalysts, the family GH13 alpha-amylase BHA from Bacillus halmapalus has been cloned and expressed. The three-dimensional structure at 2.1 Angstrom resolution has been determined in complex with the (pseudo)tetrasaccharide inhibitor acarbose. Acarbose is found bound as a nonasaccharide transglycosylation product spanning the -6 to +3 subsites. Careful inspection of electron density suggests that the bound ligand could not have been formed through successive transglycosylations of acarbose and must also have featured maltose or maltooligosaccharides as an acceptor.

Original languageEnglish
Pages (from-to)190-193
Number of pages4
JournalActa Crystallographica. Section D, Biological Crystallography
Volume61
DOIs
Publication statusPublished - Feb 2005

Keywords

  • SPECIFICITY
  • INHIBITOR
  • REFINEMENT
  • EVOLUTION
  • SEQUENCE
  • ENZYMES
  • PROGRAM
  • DOMAIN

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