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Analysis of glycoside hydrolase family 98: Catalytic machinery, mechanism and a novel putative carbohydrate binding module
Author(s) -
Rigden Daniel J.
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.09.011
Subject(s) - glycoside hydrolase , carbohydrate binding module , biochemistry , computational biology , function (biology) , biology , hydrolase , domain (mathematical analysis) , chemistry , genetics , enzyme , stereochemistry , mathematical analysis , mathematics
Glycoside hydrolases (GHs) are diverse enzymes of biotechnological and medical importance. Bioinformatics contributes to our understanding of GH structure and function in various ways, including dissection of their typically modular structures and detection of the distant evolutionary relationships between families that often allow for prediction of catalytic sites. Here these twin strands are applied to the recently described GH98 family, the founder member of which is a blood group glycotope‐cleaving endo‐β‐galactosidase of potential medical importance from Clostridium perfringens . Three domains can be discerned including a central catalytic TIM barrel domain in which putative catalytic residues can be assigned. Distant homologies and domain contexts suggest that the N‐terminal domain is a novel carbohydrate binding module.