Crystal structure of an acetyl esterase complexed with acetate ion provides insights into the catalytic mechanism

Biochem Biophys Res Commun. 2016 Aug 26;477(3):383-7. doi: 10.1016/j.bbrc.2016.06.093. Epub 2016 Jun 18.


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 0.8 Å toward the acetate ion upon substrate entering the active site, suggesting that this movement is necessary for completion of the catalytic reaction.

Keywords: Acetyl esterase; Carbohydrate esterase family 3; Catalytic triad; Oxyanion hole; SGNH-hydrolase; Talaromyces cellulolyticus.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetates / chemistry*
  • Acetylesterase / chemistry*
  • Amino Acid Sequence
  • Catalysis
  • Crystallography, X-Ray
  • Sequence Homology, Amino Acid
  • Substrate Specificity
  • Talaromyces / enzymology


  • Acetates
  • Acetylesterase