Glycosyl rotation and distortion by key residues in Endocellulase Cel6A from Theromobifida fusca

Tao Lu, Zuoming Zhang, Chi Zhang

Research output: Contribution to journalArticle

3 Scopus citations


Endocellulases are one kind of the important biodegrading cellulose enzymes. Experimental results show that a rotated and distorted preactivated structure exists before the substrate entering the transition state. The molecular dynamic simulation of endocellulase Cel6A models revealed a correlation between the rotation and distortion of pyranoside ring in-1 glycosyl unit of the substrate. The two key residues, Tyr73 and Ser189, in Cal6A cooperate to rotate and distort the pyranoside ring in the cellulose hydrolysis.

Original languageEnglish (US)
Pages (from-to)247-251
Number of pages5
Issue number3
StatePublished - Mar 1 2014



  • cellobiohydrolase
  • cellulose
  • endocellulase
  • hydrolysis mechanism
  • molecular dynamic simulations

ASJC Scopus subject areas

  • Biochemistry

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