v5.1.0.3
Glycine data from LIS
Type | Active_site |
Description | The microbial degradation of cellulose and xylans requires several types of enzymes such as endoglucanases, cellobiohydrolases (exoglucanases), or xylanases [ , ]. Fungi and bacteria producesa spectrum of cellulolytic enzymes (cellulases) and xylanases which, on the basis of sequence similarities, can be classified into families. One of thesefamilies is known as the cellulase family E [ ] or as the glycosyl hydrolases family 9 []. Three conserved regions in these enzymes are centred on conserved residues which have been shown [, , ] to be important for the catalytic activity. Thefirst region contains the characteristic DAGD motif, where the C-terminal D acts as the catalytic base that extracts a proton from the nucleophilic water.The second region contains an active site histidine and the third one contains two catalytically important residues: an aspartate and a glutamate. The fullyconserved nucleophilic D forms H-bonds with the residues of the active-site loop, comprising of regions I and II, to bring it in the proper alignement.The fully conserved E acts as an acid that protonates the leaving group and stabilizes the positively-charged oxocarbonium transition-state.This entry represents the second conserved region containing a histidine. |
Short Name | Glyco_hydro_9_His_AS |