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Structure and function of α-glucan debranching enzymes

Møller, Marie Sofie LU ; Henriksen, Anette and Svensson, Birte (2016) In Cellular and Molecular Life Sciences 73(14). p.2619-2641
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,... (More)

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.

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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
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
in
Cellular and Molecular Life Sciences
volume
73
issue
14
pages
23 pages
publisher
Birkhaüser
external identifiers
  • Scopus:84965052610
ISSN
1420-682X
DOI
10.1007/s00018-016-2241-y
language
English
LU publication?
yes
id
d7abaf47-1e5b-4373-a8aa-b07b5936c2ec
date added to LUP
2016-09-29 08:47:11
date last changed
2016-10-21 12:39:34
@misc{d7abaf47-1e5b-4373-a8aa-b07b5936c2ec,
  abstract     = {<p>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.</p>},
  author       = {Møller, Marie Sofie and Henriksen, Anette and Svensson, Birte},
  issn         = {1420-682X},
  keyword      = {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},
  language     = {eng},
  month        = {07},
  number       = {14},
  pages        = {2619--2641},
  publisher    = {ARRAY(0x8e37560)},
  series       = {Cellular and Molecular Life Sciences},
  title        = {Structure and function of α-glucan debranching enzymes},
  url          = {http://dx.doi.org/10.1007/s00018-016-2241-y},
  volume       = {73},
  year         = {2016},
}