Role of Tyr residues on the protein surface of cationic cell-wall-peroxidase (CWPO-C) from poplar: potential oxidation sites for oxidative polymerization of lignin.

@article{Sasaki2008RoleOT,
  title={Role of Tyr residues on the protein surface of cationic cell-wall-peroxidase (CWPO-C) from poplar: potential oxidation sites for oxidative polymerization of lignin.},
  author={Shinya Sasaki and Daisuke Nonaka and Hiroyuki Wariishi and Yuji Tsutsumi and Ryuichiro Kondo},
  journal={Phytochemistry},
  year={2008},
  volume={69 2},
  pages={348-55}
}
It was previously reported that an unique peroxidase isoenzyme, cationic cell-wall-bound peroxidase (CWPO-C), from poplar callus oxidizes sinapyl alcohol, ferrocytochrome c and synthetic lignin polymers, unlike other plant peroxidases. Here, the catalytic mechanism of CWPO-C was investigated using chemical modification and homology modeling. The simulated CWPO-C structure predicts that the entrance to the heme pocket of CWPO-C is the same size as those of other plant peroxidases, suggesting… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 14 extracted citations

The role of xylem class III peroxidases in lignification.

Journal of experimental botany • 2009
View 4 Excerpts
Highly Influenced

Similar Papers

Loading similar papers…