Glycosyl rotation and distortion by key residues in Endocellulase Cel6A from Theromobifida fusca.
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.
['Lu|Tao|T|', 'Zhang|Zuoming|Z|', 'Zhang|Chi|C|']
D000192:Actinomycetales D000595:Amino Acid Sequence D001426:Bacterial Proteins D002480:Cellulase D056004:Molecular Dynamics Simulation D008969:Molecular Sequence Data D012399:Rotation
endocellulase cellulose molecular dynamic simulations cellobiohydrolase hydrolysis mechanism