Comparison of ligninase-I and peroxidase-M2 from the white-rot fungus Phanerochaete chrysosporium.

@article{Paszczynski1986ComparisonOL,
  title={Comparison of ligninase-I and peroxidase-M2 from the white-rot fungus Phanerochaete chrysosporium.},
  author={Andrzej J. Paszczynski and V B Huynh and Ronald L. Crawford},
  journal={Archives of biochemistry and biophysics},
  year={1986},
  volume={244 2},
  pages={
          750-65
        }
}
Hybrid Mn-Peroxidase from the Ligninolytic Fungus Panus tigrinus 8/18. Isolation, Substrate Specificity, and Catalytic Cycle
TLDR
Study of absorption spectra of the intermediates of the catalytic cycle revealed that this Mn-peroxidase is able to complete the redox cycle, reducing one-electron oxidized intermediate (Compound II) by Mn2+, as well as by an organic substrate (hydroquinone).
Identification of a specific manganese peroxidase among ligninolytic enzymes secreted by Phanerochaete chrysosporium during wood decay
TLDR
It is suggested that the ligninolytic-enzyme-encoding genes that are expressed during solid substrate degradation differ from those expressed in liquid culture or are allelic variants of their liquid culture counterparts.
Manganese peroxidase from the basidiomycete Phanerochaete chrysosporium: spectral characterization of the oxidized states and the catalytic cycle.
TLDR
Spectroscopically characterize the oxidized states of MnP compounds I, II, and III and clarify the role of Mn in the catalytic cycle of the enzyme, indicating that Mn(II) serves as an obligatory substrate for MnP compound II, allowing the enzyme to complete its catalysttic cycle.
Overproduction of lignin-degrading enzymes by an isolate of Phanerochaete chrysosporium
TLDR
These properties make PSBL-1 very useful for isolation of large amounts of all ligninolytic enzymes for biochemical study, and they open the possibility of scale-up production for pratical use.
Lignin peroxidase-negative mutant of the white-rot basidiomycete Phanerochaete chrysosporium
TLDR
A lignin peroxidase-negative mutant (lip mutant) that showed 16% of the ligninolytic activity of the wild type is isolated and characterized, which appears to be a regulatory mutant that is defective in the production of all the lIGNinperoxidases.
Haloperoxidase reactions catalyzed by lignin peroxidase, an extracellular enzyme from the basidiomycete Phanerochaete chrysosporium
Lignin peroxidase (ligninase, LiP) an H/sub 2/O/sub 2/-dependent lignin-degrading heme enzyme from the basidiomycetous fungus Phanerochaete chrysosporium, catalyzes the oxidation of a variety of
Isolation and characterization of the second extracellular peroxidase of the white-rot fungus Coriolus hirsutus
TLDR
A second extracellular peroxidase of Coriolus hirsutus was purified to electrophoretic homogeneity using four chromatographic steps: DEAE-Sepharose, Sephacry S-200, Hitrap SP and Mono S column, and catalyzed the oxidation of a variety of monomeric lignin model compounds.
...
...

References

SHOWING 1-10 OF 28 REFERENCES
Enzymatic activities of an extracellular, manganese-dependent peroxidase from Phanerochaete chrysosporium
An extracellular peroxidase was purified by chromatofocusing column chromatography from the growth medium of ligninolytic cultures of the white-rot fungus Phanerochaete chrysosporium Burds BKM-1767.
Relationship between lignin degradation and production of reduced oxygen species by phanerochaete chrysosporium
TLDR
It is concluded that H2O2, and perhaps O2∸, are involved in lignin degradation; because these species are relatively unreactive per se, their role must be indirect.
Novel extracellular enzymes (ligninases) of Phanerochaete chrysosporium
TLDR
3 new spectrophotometric enzyme assays were developed for the study of microbial lignin-degrading enzymes and led to the discovery of an extracellular, aromatic methyl ether demethylase produced by the white-rot fungus Phanerochaete chrysosporium.
Free hydroxyl radical is not involved in an important reaction of lignin degradation by Phanerochaete chrysosporium Burds.
Hydroxyl radical (HO.) has been implicated in the degradation of lignin by Phanerochaete chrysosporium. This study assessed the possible involvement of HO. in degradation of lignin substructural
Ligninolytic enzyme production by Phanerochaete chrysosporium under conditions of nitrogen sufficiency
A lignin-degrading enzyme has been detected in culture supernatants of Phanerochaete chrysosporium strain INA-12 grown under non-limiting nitrogen conditions. Highest levels of enzyme activity were
THE MECHANISM OF AEROBIC OXIDASE REACTION CATALYZED BY PEROXIDASE.
...
...