Crystal structure of Bacillus subtilis alpha-amylase in complex with acarbose.
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.
Kagawa
Masayuki
M
Department of Biochemistry, National Institute of Agrobiological Sciences, Tsukuba, Ibaraki 305-8602, Japan.
Fujimoto
Zui
Z
Momma
Mitsuru
M
Takase
Kenji
K
Mizuno
Hiroshi
H
D020909:Acarbose / Q000737:chemistry* / Q000378:metabolism; D001412:Bacillus subtilis / Q000201:enzymology*; D001665:Binding Sites; D018360:Crystallography, X-Ray; D006031:Glycosylation; D008958:Models, Molecular; D000516:alpha-Amylases / Q000737:chemistry* / Q000378:metabolism
D000516:alpha-Amylases; D020909:Acarbose