Structure and function of α-glucan debranching enzymes

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Bibtex

@article{d7abaf471e5b4373a8aab07b5936c2ec,
title = "Structure and function of α-glucan debranching enzymes",
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.",
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",
author = "M{\o}ller, {Marie Sofie} and Anette Henriksen and Birte Svensson",
year = "2016",
month = "7",
day = "1",
doi = "10.1007/s00018-016-2241-y",
language = "English",
volume = "73",
pages = "2619--2641",
journal = "Cellular and Molecular Life Sciences",
issn = "1420-9071",
publisher = "Birkha{\"u}ser",
number = "14",

}