 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 1]](en5069fig1mag.jpg)
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Figure 1
(a) The covalent glycosyl-enzyme intermediate of a retaining glycosidase is normally intercepted by water. Under some circumstances, it is instead intercepted by another sugar in a transglycosylation reaction; such a mechanism gives rise to the many elongated forms of acarbose seen in amylase structures. (b) The structure of the pseudo-tetrasaccharide inhibitor acarbose. (c) The nonasaccharide observed in BHA (this work) and (d) that previously observed on the BA2 α-amylase (Brzozowski et al., 2000  ). |
![[Figure 1]](en5069fig1.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
