Structure of a Bacillus halmapalus family 13 ά-amylase, BHA, in complex with an acarbose-derived nonasaccharide at 2.1 A resolution
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.
- Research Organization:
- Brookhaven National Lab. (BNL), Upton, NY (United States). National Synchrotron Light Source
- Sponsoring Organization:
- Doe - Office Of Science
- DOE Contract Number:
- DE-AC02-98CH10886
- OSTI ID:
- 959552
- Report Number(s):
- BNL-82538-2009-JA; TRN: US201016%%696
- Journal Information:
- Acta Crystallographica Section D: Biological Crystallography, Vol. 61
- Country of Publication:
- United States
- Language:
- English
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