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Journal of Bacteriology, December 2003, p. 6981-6984, Vol. 185, No. 23
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.23.6981-6984.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Crystal Structure of Bacillus subtilis {alpha}-Amylase in Complex with Acarbose

Masayuki Kagawa, Zui Fujimoto, Mitsuru Momma, Kenji Takase, and Hiroshi Mizuno*

Department of Biochemistry, National Institute of Agrobiological Sciences, Tsukuba, Ibaraki 305-8602, Japan

Received 19 June 2003/ Accepted 29 August 2003

The crystal structure of Bacillus subtilis {alpha}-amylase, in complex with the pseudotetrasaccharide inhibitor acarbose, revealed an hexasaccharide in the active site as a result of transglycosylation. After comparison with the known structure of the catalytic-site mutant complexed with the native substrate maltopentaose, it is suggested that the present structure represents a mimic intermediate in the initial stage of the catalytic process.

* Corresponding author. Mailing address: Department of Biochemistry, National Institute of Agrobiological Sciences, Tsukuba, Ibaraki 305-8602, Japan. Phone: 81-29-838-7010. Fax: 81-29-838-7408. E-mail: mizuno{at}affrc.go.jp.

Journal of Bacteriology, December 2003, p. 6981-6984, Vol. 185, No. 23
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.23.6981-6984.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Robert, X., Haser, R., Mori, H., Svensson, B., Aghajari, N. (2005). Oligosaccharide Binding to Barley {alpha}-Amylase 1. J. Biol. Chem. 280: 32968-32978 [Abstract] [Full Text]  


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