Structure and function of α-glucan debranching enzymes

Research output: Contribution to journalReview article

Abstract

α-Glucan debranching enzymes hydrolyse α-1,6-linkages in starch/glycogen, thereby, playing a central role in energy metabolism in all living organisms. They belong to glycoside hydrolase families GH13 and GH57 and several of these enzymes are industrially important. Nine GH13 subfamilies include α-glucan debranching enzymes; isoamylase and glycogen debranching enzymes (GH13_11); pullulanase type I/limit dextrinase (GH13_12–14); pullulan hydrolase (GH13_20); bifunctional glycogen debranching enzyme (GH13_25); oligo-1 and glucan-1,6-α-glucosidases (GH13_31); pullulanase type II (GH13_39); and α-amylase domains (GH13_41) in two-domain amylase–pullulanases. GH57 harbours type II pullulanases. Specificity differences, domain organisation, carbohydrate binding modules, sequence motifs, three-dimensional structures and specificity determinants are discussed. The phylogenetic analysis indicated that GH13_39 enzymes could represent a “missing link” between the strictly α-1,6-specific debranching enzymes and the enzymes with dual specificity and α-1,4-linkage preference.

Details

Authors
  • Marie Sofie Møller
  • Anette Henriksen
  • Birte Svensson
Organisations
External organisations
  • Technical University of Denmark
  • Novo Nordisk A/S
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Cell and Molecular Biology

Keywords

  • Carbohydrate binding modules, Domain architecture, Glycoside hydrolase family 13 subfamilies, Multi-domain three-dimensional structure, Phylogeny, Sequence motifs and determinants, Structure–function relationship, Substrate specificity
Original languageEnglish
Pages (from-to)2619-2641
Number of pages23
JournalCellular and Molecular Life Sciences
Volume73
Issue number14
Publication statusPublished - 2016 Jul 1
Publication categoryResearch
Peer-reviewedYes