Microbial Tyrosinases: A Novel Enzyme, Structural Features, and Applications

  title={Microbial Tyrosinases: A Novel Enzyme, Structural Features, and Applications},
  author={Pragati Agarwal and Mukta Singh and Jyoti Singh and R.P. Singh},
  journal={Applied Microbiology and Bioengineering},
Considerations Regarding Activity Determinants of Fungal Polyphenol Oxidases Based on Mutational and Structural Studies
The crystal structure of a TtPPO variant, determined at 1.55 Å resolution, represents the second known structure of an ascomycete PPO and improves current understanding of structure-function relations of microbial PPOs, which is a prerequisite for the engineering of biocatalysts of desired properties.
New tyrosinases with a broad spectrum of action against contaminants of emerging concern: Insights from in silico analyses
Ciliates, including those caring tyrosinase genes within their genomes are fast-growing unicellular microeukaryotes that can be efficiently culturable at large-scales under in vitro conditions, should be regarded as potential low-cost sources for the production of relevant biotechnological molecules.
New tyrosinases with putative action against contaminants of emerging concern
Six tyrosinase homologs were identified and characterized from the genomes of four widespread freshwater ciliates using bioinformatics and a virtual screening was performed to calculate binding energies between 3D models of these homologicals and contaminants of emerging concern (CECs), as an indirect approach to identify likely and unlikely targets for tyosinases.
A Novel Tyrosinase from Armillaria ostoyae with Comparable Monophenolase and Diphenolase Activities Suffers Substrate Inhibition
The results indicated that this novel tyrosinase from Armillaria ostoyaestrain C18/9 (AoTyr) could be a potential candidate for the industrial biosynthesis of catechols.
Effectivity of tyrosinase purification by membrane techniques versus fractionation by salting out
It was shown that tyrosinase can be pre-purified by selected membranes yielding the enzyme quality at least comparable to that after double salting-out method but in one device.


Enzymological characterization of EpoA, a laccase-like phenol oxidase produced by Streptomyces griseus.
EpoA-like activities were detected in cell extracts of 8/40 environmental actinomycetes strains, which suggests that similar oxidases are widely distributed among this group of bacteria.
New insights into the active site structure and catalytic mechanism of tyrosinase and its related proteins
Tyrosinases are widely distributed in nature. They are copper‐containing oxidases belonging to the type 3 copper protein family, together with catechol oxidases and haemocyanins. Tyrosinases are
Bacterial tyrosinases.
Molecular and biochemical characterization of a distinct tyrosinase involved in melanin production from Aeromonas media
The results suggest that TyrA is the first reported distinct tyrosinase involved in melanin production in the genus Aeromonas, and it encodes a 518 amino acid protein with little similarities to other reported tyosinases.
Molecular Cloning and Characteristic Features of a Novel Extracellular Tyrosinase from Aspergillus niger PA2
Aspergillus niger PA2, a novel strain isolated from waste effluents of food industry, is a potential extracellular tyrosinase producer. Enzyme activity and L-DOPA production were maximum when glucose
Crystal structure of Agaricus bisporus mushroom tyrosinase: identity of the tetramer subunits and interaction with tropolone.
The first structure of the full fungal tyrosinase complex from the mushroom Agaricus bisporus is presented, explaining how calcium ions stabilize the tetrameric state of the enzyme.
Purification and characterization of a tyrosinase from Streptomyces glaucescens.
The purification of a tyrosinase from cell-free extracts of Streptomyces glaucescens is described, and the enzyme obtained is homogeneous according to the criteria of ultracentrifuge analysis and polyacrylamide gel electrophoresis, which shows optimal activity at pH 6.8.