Heterologous Expression of Pleurotus eryngii Peroxidase Confirms Its Ability To Oxidize Mn2+ and Different Aromatic Substrates
AUTOR(ES)
Ruiz-Dueñas, Francisco Javier
FONTE
American Society for Microbiology
RESUMO
A versatile ligninolytic peroxidase has been cloned from Pleurotus eryngii and its allelic variant MnPL2 expressed in Aspergillus nidulans, with properties similar to those of the mature enzyme from P. eryngii. These include the ability to oxidize Mn2+ and aromatic substrates, confirming that this is a new peroxidase type sharing catalytic properties of lignin peroxidase and manganese peroxidase.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=91631Documentos Relacionados
- Laccase isoenzymes of Pleurotus eryngii: characterization, catalytic properties, and participation in activation of molecular oxygen and Mn2+ oxidation.
- Lignocellulose Affects Mn2+ Regulation of Peroxidase Transcript Levels in Solid-State Cultures of Pleurotus ostreatus
- Laccase-Catalyzed Oxidation of Mn2+ in the Presence of Natural Mn3+ Chelators as a Novel Source of Extracellular H2O2 Production and Its Impact on Manganese Peroxidase
- Regulation of Peroxidase Transcript Levels in Liquid Cultures of the Ligninolytic Fungus Pleurotus eryngii
- Mn2+ and Co2+ toxicity in chlorophyll biosynthesis