Comparison of the domain-level organization of starch hydrolases and related enzymes

H. M. Jespersen, E. A. MacGregor, M. R. Sierks, B. Svensson

Research output: Contribution to journalArticlepeer-review

196 Scopus citations

Abstract

Structure-prediction and hydrophobic-cluster analysis of several starch hydrolases and related enzymes indicated the organization of eleven domain types. Most enzymes possess a catalytic (β/α)8-barrel and a smaller C-terminal domain as seen in crystal structures of α-amylase and cyclodextrin glucanotransferase. Some also have a starch-granule-binding domain. Enzymes breaking or forming endo-α-1,6 linkages contain domains N-terminal to the (β/α)8-barrel.

Original languageEnglish (US)
Pages (from-to)51-55
Number of pages5
JournalBiochemical Journal
Volume280
Issue number1
DOIs
StatePublished - 1991
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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