EC Number   |
General Information |
Reference |
|---|
   3.2.1.156 | evolution |
the enzyme belongs to the glycoside hydrolase family 8, GH8 |
-, 752545 |
| 3.2.1.156 | more |
modeling of the three-dimensional structure of Rex8A shows an (alpha/alpha)6 barrel fold where the loops connecting the alpha-helices contour the active site. These loops, which show high sequence diversity among GH8 enzymes, shape a catalytic cleft with a -2 subsite that can accommodate methyl-glucuronic acid decorations. Putative proton donor is Glu70 and catalytic base is Asp265. Residues Leu320, His321, and Pro322 form the loop structure. Structural molecular modeling of Rex8A |
-, 752545 |
| 3.2.1.156 | more |
three conserved catalytic residues are Glu90, Asp148, and Asp286 |
-, 731182 |
| 3.2.1.156 | physiological function |
Rex8As are key enzymes in the efficient saccharification of heteroxylan into xylose, a major component of lignocellulosic substrates |
-, 753453 |
| 3.2.1.156 | physiological function |
the enzyme is involved in depolymerization of glucuronoxylan, a major component of the lignocellulosic substrates. Rex8A is a reducing-end xylose-releasing exo-oligoxylanase that efficiently hydrolyzes xylose from neutral and acidic xylooligosaccharides generated by the action of other xylanases also secreted by the strain. The hydrolytic ability of Rex8A on branched oligomers can be crucial for the complete depolymerization of highly substituted xylans, which is indispensable to accomplish biomass deconstruction and to generate efficient catalysts |
-, 752545 |
