Structure and function of α-glucan debranching enzymes
(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.
(Less)
- author
- Møller, Marie Sofie LU ; Henriksen, Anette and Svensson, Birte
- organization
- publishing date
- 2016-07-01
- 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
- Birkhäuser
- external identifiers
-
- scopus:84965052610
- pmid:27137180
- wos:000378934000003
- 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
- 2024-09-06 22:52:14
@article{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}}, 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}}, language = {{eng}}, month = {{07}}, number = {{14}}, pages = {{2619--2641}}, publisher = {{Birkhäuser}}, 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}}, doi = {{10.1007/s00018-016-2241-y}}, volume = {{73}}, year = {{2016}}, }