期刊
CELLULAR AND MOLECULAR LIFE SCIENCES
卷 73, 期 14, 页码 2619-2641出版社
SPRINGER BASEL AG
DOI: 10.1007/s00018-016-2241-y
关键词
Substrate specificity; Glycoside hydrolase family 13 subfamilies; Domain architecture; Multi-domain three-dimensional structure; Sequence motifs and determinants; Structure-function relationship; Carbohydrate binding modules; Phylogeny
资金
- Danish Council for Independent Research Technology and Production Sciences
- Sapere Aude-Research Talent grant from the Danish Council for Independent Research Technology and Production Sciences
alpha-Glucan debranching enzymes hydrolyse alpha-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 alpha-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-alpha-glucosidases (GH13_31); pullulanase type II (GH13_39); and alpha-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 alpha-1,6-specific debranching enzymes and the enzymes with dual specificity and alpha-1,4-linkage preference.
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