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Phylogenetic analysis of family 6 glycoside hydrolases
Biopolymers, 2005AbstractMultiple sequence alignment separates members of glycoside hydrolase Family 6 into eight subfamilies: one of mainly actinobacterial endoglucanases (EGs), one of ascomycotal EGs, one of chytridiomycotal EGs and cellobiohydrolases (CBHs), one of actinobacterial and proteobacterial CBHs, one of chytridiomycotal CBHs, two of ascomycotal CBHs, and ...
Blake, Mertz +4 more
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Catalytic strategies of glycoside hydrolases
2018Glycoside hydrolases (GHs) are enzymes that catalyze the hydrolysis of the glycosidic bond between two carbohydrate residues or a carbohydrate unit linked to a non-carbohydrate aglycon unit. Despite years of research dedicated to GHs, there are still several mechanistic details, relevant for individual GH enzymes, that remain to be investigated.
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Classification of glycoside hydrolases and glycosyltransferases from hyperthermophiles
2001Publisher Summary Glycoside hydrolases and glycosyltransferases are widespread groups of carbohydrate-active enzymes present in virtually all organisms and are involved, respectively, in the hydrolysis and in the biosynthesis of glycosidic bonds between carbohydrates or between a carbohydrate and a noncarbohydrate moiety.
B, Henrissat, P M, Coutinho
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Immunization with Dextransucrases and Glycosidic Hydrolases
Journal of Dental Research, 1972J A, Hayashi, I L, Shklair, A N, Bahn
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Structural insights into β-1,3-glucan cleavage by a glycoside hydrolase family
Nature Chemical Biology, 2020Camila R. Santos +18 more
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An overview on glycoside hydrolases and glycosyltransferases
Zeitschrift für Naturforschung CMaria Elena Ortiz-Soto, Jürgen Seibel
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Novel glycoside hydrolases from thermophilic fungi
2012The present invention relates to isolated polypeptides having cellulolytic activity or hemicellulolytic activity and polynucleotides encoding the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides.
Lange, Lene, Busk, Peter Kamp
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