Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10748051 | Biochemical and Biophysical Research Communications | 2016 | 5 Pages |
Abstract
We previously reported the crystal structure of an acetyl esterase (TcAE206) belonging to carbohydrate esterase family 3 from Talaromyces cellulolyticus. In this study, we solved the crystal structure of an S10A mutant of TcAE206 complexed with an acetate ion. The acetate ion was stabilized by three hydrogen bonds in the oxyanion hole instead of a water molecule as in the structure of wild-type TcAE206. Furthermore, the catalytic triad residue His182 moved 0.8Â Ã
toward the acetate ion upon substrate entering the active site, suggesting that this movement is necessary for completion of the catalytic reaction.
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Biochemistry
Authors
Keiko Uechi, Saori Kamachi, Hironaga Akita, Shouhei Mine, Masahiro Watanabe,