Open AccessStructure of a Bacillus halmapalus family 13 α‐amylase, BHA, in complex with an acarbose‐derived nonasaccharide at 2.1 Å resolution
Author(s) -
Davies Gideon J.,
Brzozowski A. Marek,
Dauter Zbigniew,
Rasmussen Michael D.,
Borchert Torben V.,
Wilson Keith S.
Publication year - 2005
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s0907444904027118
Subject(s) - acarbose , chemistry , maltose , amylase , stereochemistry , starch , resolution (logic) , oligosaccharide , alpha amylase , enzyme , biochemistry , artificial intelligence , computer science
The enzymatic digestion of starch by α‐amylases is one of the key biotechnological reactions of recent times. In the search for industrial biocatalysts, the family GH13 α‐amylase BHA from Bacillus halmapalus has been cloned and expressed. The three‐dimensional structure at 2.1 Å 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.