LIS - Legume Information System
Information about legume traits for crop improvement
GlycineMine
v5.1.0.3
Glycine data from LIS
v5.1.0.3
Glycine data from LIS
| Type | Homologous_superfamily |
| Description | The microbial degradation of cellulose and xylans requires several types of enzyme such as endoglucanases (EC 3.2.1.4), cellobiohydrolases (EC 3.2.1.91)(exoglucanases), or xylanases (EC 3.2.1.8) [ ]. Structurally, cellulases and xylanases generally consist of a catalytic domain and a conserved region of ~100 amino acid residues, the carbohydrate-binding module 2 (CBM2) []. It is found either at the N-terminal or at the C-terminal extremity of these enzymes.CBM2 can be classified in 2 subfamilies according to substrate specificities: CBM2a which binds cellulose and CBM2b which interacts specifically with xylan. Like other CBM domains CBM2 is a β-sheet domain containing a planar facewhich interacts with its ligand via a hydrophobic strip of aromatic residues [ ]. In family 2a this hydrophobic surface consists of threetryptophan residues, which are all required for binding soluble and insoluble forms of cellulose []. In family 2b only 2 surface-exposed tryptophans areconserved and the first one is oriented differently. It is therefore not well oriented to interact with cellulose but is ideal for binding xylan [].This entry recognises both CBM2 subfamilies. |
| Short Name | CBM2_carb-bd_dom_sf |
