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In silico identification of catalytic residues and domain fold of the family GH119 sharing the catalytic machinery with the α‐amylase family GH57
Author(s) -
Janeček Štefan,
Kuchtová Andrea
Publication year - 2012
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.2012.07.020
Subject(s) - in silico , chemistry , bacillus circulans , glycoside hydrolase , catalysis , amylase , stereochemistry , biochemistry , enzyme , gene
The glycoside hydrolase family 119 (GH119) contains the α‐amylase from Bacillus circulans and five other hypothetical proteins. Until now, nothing has been reported on the catalytic residues and catalytic‐domain fold of GH119. Based on a detailed in silico analysis involving sequence comparison in combination with BLAST searches and structural modelling, an unambiguous relationship was revealed between the families GH119 and GH57. This includes sharing the catalytic residues, i.e. Glu231 and Asp373 as catalytic nucleophile and proton donor, respectively, in the predicted catalytic (β/α) 7 ‐barrel domain of GH119 B. circulans α‐amylase. The GH57 and GH119 families may thus define a new CAZy clan.