@article{PAR00008314,
  title = {{D}ioxygenase from {A}spergillus fumigatus {MC}8 : molecular modelling and in silico studies on enzyme-substrate interactions},
  author = {{R}oopesh, {K}. and {A}bhilash, {J}. and {H}aridas, {M}. and {S}abu, {A}. and {P}erraud {G}aime, {I}sabelle and {R}oussos, {S}evastianos and {A}ugur, {C}hristopher},
  editor = {},
  language = {{ENG}},
  abstract = {{F}lavoenzymes have been extensively studied for their structural and mechanistic properties because they find potential application as industrial biocatalysts. {T}hey are attractive for biocatalysis because of the selectivity, controllability and efficiency of their reactions. {S}ome of these enzymes catalyse the oxidative modification of protein substrates. {A}mong them oxygenases (monoxoygenases and dioxygenases) are of special interest because they are highly entantio as well as regio-selective and can be used for oxyfunctionalisation. {D}ioxygenase enzymes catalyse oxygenation reactions in which both dioxygen atoms are incorporated into the product. {A} dioxygenase enzyme purified from {A}spergillus fumigatus {MC}8 was subjected to protein digestion followed by peptide sequencing. {T}he sequence analysis of the peptide fragments resulted in identifying its match with that of an extracellular dioxygenase sequence from the same species of fungus existing in the protein database. {T}he sequence was submitted to protein homology/analogy recognition engine online server for homology modelling and the 3{D} structure was predicted. {S}ubsequently, the in silico studies of the enzyme-substrate (protein-ligand) interaction were carried out by using the method of molecular docking simulations wherein the modelled dioxygenase enzyme (protein) was docked with the substrates (ligands), catechin and epicatechin.},
  keywords = {dioxygenase ; peptide sequencing ; homology modelling ; molecular docking},
  booktitle = {},
  journal = {{M}olecular {S}imulation},
  volume = {38},
  numero = {2},
  pages = {144--151},
  ISSN = {0892-7022},
  year = {2012},
  DOI = {10.1080/08927022.2011.608672},
  URL = {https://www.documentation.ird.fr/hor/{PAR}00008314},
}