Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Toerroenen, A.; Rouvinen, J.
    Structural and functional properties of low molecular weight endo-1,4-beta-xylanases (1997), J. Biotechnol., 57, 137-149.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.8 Niallia circulans
-
-
-
3.2.1.8 Trichoderma harzianum
-
-
-
3.2.1.8 Trichoderma reesei
-
 2 xylanases
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.2.1.8 (Xylbeta(1-4))n + H2O = (Xylbeta(1-4))n-m + (Xylbeta(1-4))m the catalytic residues are two conserved Glu residues, which are located opposite to each other in an open active site cleft. The catalytic mechanism resembles that of lysozyme. The role of one glutamate is to act as an acid/base catalyst whereas the other is a nucleophile and stabilizes the reaction intermediate Niallia circulans
a
3.2.1.8 (Xylbeta(1-4))n + H2O = (Xylbeta(1-4))n-m + (Xylbeta(1-4))m the catalytic residues are two conserved Glu residues, which are located opposite to each other in an open active site cleft. The catalytic mechanism resembles that of lysozyme. The role of one glutamate is to act as an acid/base catalyst whereas the other is a nucleophile and stabilizes the reaction intermediate Trichoderma harzianum
a
3.2.1.8 (Xylbeta(1-4))n + H2O = (Xylbeta(1-4))n-m + (Xylbeta(1-4))m the catalytic residues are two conserved Glu residues, which are located opposite to each other in an open active site cleft. The catalytic mechanism resembles that of lysozyme. The role of one glutamate is to act as an acid/base catalyst whereas the other is a nucleophile and stabilizes the reaction intermediate Trichoderma reesei
a