Crystal structures of human pancreatic alpha-amylase in complex with carbohydrate and proteinaceous inhibitors. - Archive ouverte HAL Access content directly
Journal Articles Biochemical Journal Year : 2000

Crystal structures of human pancreatic alpha-amylase in complex with carbohydrate and proteinaceous inhibitors.

Abstract

Crystal structures of human pancreatic alpha-amylase (HPA) in complex with naturally occurring inhibitors have been solved. The tetrasaccharide acarbose and a pseudo-pentasaccharide of the trestatin family produced identical continuous electron densities corresponding to a pentasaccharide species, spanning the -3 to +2 subsites of the enzyme, presumably resulting from transglycosylation. Binding of the acarviosine core linked to a glucose residue at subsites -1 to +2 appears to be a critical part of the interaction process between alpha-amylases and trestatin-derived inhibitors. Two crystal forms, obtained at different values of pH, for the complex of HPA with the protein inhibitor from Phaseolus vulgaris (alpha-amylase inhibitor) have been solved. The flexible loop typical of the mammalian alpha-amylases was shown to exist in two different conformations, suggesting that loop closure is pH-sensitive. Structural information is provided for the important inhibitor residue, Arg-74, which has not been observed previously in structural analyses.
No file

Dates and versions

hal-01849230 , version 1 (25-07-2018)

Identifiers

  • HAL Id : hal-01849230 , version 1
  • PUBMED : 10657258

Cite

F Nahoum, G Roux, A Anton, P. Rouge, A Puigserver, et al.. Crystal structures of human pancreatic alpha-amylase in complex with carbohydrate and proteinaceous inhibitors.. Biochemical Journal, 2000, pp.201-8. ⟨hal-01849230⟩
18 View
0 Download

Altmetric

Share

Gmail Facebook X LinkedIn More