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Structural consequences of neopullulanase mutations

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Author

Summary, in English

Bacillus stearothermophilus neopullulanase (NPL) structure was modeled based on Aspergillus oryzae alpha-amylase (TAA) to understand the structure-function relationships of this pullulan hydrolyzing enzyme. The NPL structure seems to consist of a central (alpha/beta)(8) barrel to which the other domains are attached. The immediate surroundings of the NPL catalytic site were found to have very similar structure to TAA. The more distant sites are different due to the stereochemical requirements of accommodating in the substrate alpha-1,6-linkages at every third position instead of alpha-1,4-linkages. The substrate binding cleft is wider than in alpha-amylases. The NPL structure, function, substrate binding and the consequences of mutations were discussed based on the modeled structure.

Publishing year

1996

Language

English

Pages

195-200

Publication/Series

BBA - Protein Structure and Molecular Enzymology

Volume

1295

Issue

2

Document type

Journal article

Publisher

Elsevier

Topic

  • Medical Genetics

Keywords

  • neopullulanase
  • structure-function relationship
  • molecular modeling
  • substrate binding
  • active site
  • (B-stearothermophilus)
  • (A-oryzae)

Status

Published

ISBN/ISSN/Other

  • ISSN: 0167-4838