Small Angle X-ray Studies Reveal That Aspergillus niger Glucoamylase Has a Defined Extended Conformation and Can Form Dimers in Solution*

@article{Jrgensen2008SmallAX,
  title={Small Angle X-ray Studies Reveal That Aspergillus niger Glucoamylase Has a Defined Extended Conformation and Can Form Dimers in Solution*},
  author={A. J{\o}rgensen and J. N{\o}hr and J. Kastrup and M. Gajhede and B. Sigurskjold and J. Sauer and D. Svergun and B. Svensson and B. Vestergaard},
  journal={Journal of Biological Chemistry},
  year={2008},
  volume={283},
  pages={14772 - 14780}
}
  • A. Jørgensen, J. Nøhr, +6 authors B. Vestergaard
  • Published 2008
  • Medicine, Chemistry
  • Journal of Biological Chemistry
  • The industrially important glucoamylase 1 is an exo-acting glycosidase with substrate preference for α-1,4 and α-1,6 linkages at non-reducing ends of starch. It consists of a starch binding and a catalytic domain interspersed by a highly glycosylated polypeptide linker. The linker function is poorly understood and structurally undescribed, and data regarding domain organization and intramolecular functional cooperativity are conflicting or non-comprehensive. Here, we report a combined small… CONTINUE READING

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