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.
Crystal structure of Bacillus subtilis alpha-amylase in complex with acarbose.,Kagawa M, Fujimoto Z, Momma M, Takase K, Mizuno H J Bacteriol. 2003 Dec;185(23):6981-4. PMID:14617662
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.