title: Glycosyl rotation and distortion by key residues in Endocellulase Cel6A from Theromobifida fusca.
abstract: 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.
authors.affiliation: School of Biological Sciences, University of Nebraska-Lincoln, Lincoln, NE 68588, USA.
authors.forename: Tao
authors.initials: T
authors.lastname: Lu
authors.forename: Zuoming
authors.initials: Z
authors.lastname: Zhang
authors.forename: Chi
authors.initials: C
authors.lastname: Zhang
mesh_terms: D000192:Actinomycetales / Q000201:enzymology*; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D002480:Cellulase / Q000737:chemistry*; D056004:Molecular Dynamics Simulation; D008969:Molecular Sequence Data; D012399:Rotation
chemical_list: D001426:Bacterial Proteins; C407024:endoglucanase Cel5A; D002480:Cellulase
keywords: cellobiohydrolase; cellulose; endocellulase; hydrolysis mechanism; molecular dynamic simulations