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Limits of Versatility of Versatile Peroxidase.

Doriv KnopDana LevinsonArik MakovitzkiAvi AgamiElad LererAvishai MimranOded YardenYitzhak Hadar
Published in: Applied and environmental microbiology (2016)
VP1 is a member of the ligninolytic heme peroxidase gene family of the white rot fungus Pleurotus ostreatus and plays a fundamental role in biodegradation. This enzyme exhibits a versatile nature, as it can oxidize different substrates under altered environmental conditions. VPs are highly interesting enzymes due to the fact that they contain unique active sites that are responsible for direct oxidation of various aromatic compounds, including lignin, in addition to the well-known Mn(2+) binding active site. This study demonstrates the limits of versatility of P. ostreatus VP1, which harbors multiple active sites, exhibiting a broad range of enzymatic activities, but they perform differently under distinct conditions. The versatility of P. ostreatus and its enzymes is an advantageous factor in the fungal ability to adapt to changing environments. This trait expands the possibilities for the potential utilization of P. ostreatus and other white rot fungi.
Keyphrases
  • hydrogen peroxide
  • human health
  • nitric oxide
  • ionic liquid
  • transcription factor
  • genome wide
  • disease virus
  • risk assessment
  • room temperature
  • metal organic framework
  • dna binding