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Glycosyl rotation and distortion by key residues in Endocellulase Cel6A from Theromobifida fusca.
- Source :
-
Glycobiology . Mar2014, Vol. 24 Issue 3, p247-251. 5p. - Publication Year :
- 2014
-
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. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 09596658
- Volume :
- 24
- Issue :
- 3
- Database :
- Academic Search Index
- Journal :
- Glycobiology
- Publication Type :
- Academic Journal
- Accession number :
- 94393473