Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10870300 | FEBS Letters | 2015 | 31 Pages |
Abstract
Carbohydrate esterase catalyzes the de-O or de-N-acylation of substituted saccharides in plant cell walls and thus has great potential for industrial biomass saccharification. We recently identified the putative carbohydrate esterase family 3 (CE3) from Talaromyces cellulolyticus. Here, we prepared the recombinant catalytic domain of the enzyme and crystallized it. The crystal structure was determined to 1.5Â Ã
resolution. From the structural analysis, it was elucidated that a n-octyl-β-d-glucopyranoside bound to near the catalytic triad (Ser10, Asp179 and His182) and was buried in the active site cavity. Site-directed mutagenesis showed that the N-terminal disulfide bond located near the catalytic triad is involved in the activity and structural stability of the enzyme.
Keywords
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Masahiro Watanabe, Harumi Fukada, Hiroyuki Inoue, Kazuhiko Ishikawa,