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Dioxygenase from Aspergillus fumigatus MC8: molecular modelling and in silico studies on enzyme-substrate interactions

Krishnankutty, Roopesh LU ; Abhilash, Joseph; Haridas, M.; Sabu, Abdulhameed; Isabelle, Perraud Gaime; Roussos, Sevastianos and Augur, Christopher (2012) In Molecular Simulation 38(2). p.144-151
Abstract
Flavoenzymes have been extensively studied for their structural and mechanistic properties because they find potential application as industrial biocatalysts. They are attractive for biocatalysis because of the selectivity, controllability and efficiency of their reactions. Some of these enzymes catalyse the oxidative modification of protein substrates. Among 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. Dioxygenase enzymes catalyse oxygenation reactions in which both dioxygen atoms are incorporated into the product. A dioxygenase enzyme purified from Aspergillus fumigatus MC8 was subjected to protein digestion... (More)
Flavoenzymes have been extensively studied for their structural and mechanistic properties because they find potential application as industrial biocatalysts. They are attractive for biocatalysis because of the selectivity, controllability and efficiency of their reactions. Some of these enzymes catalyse the oxidative modification of protein substrates. Among 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. Dioxygenase enzymes catalyse oxygenation reactions in which both dioxygen atoms are incorporated into the product. A dioxygenase enzyme purified from Aspergillus fumigatus MC8 was subjected to protein digestion followed by peptide sequencing. The 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. The sequence was submitted to protein homology/analogy recognition engine online server for homology modelling and the 3D structure was predicted. Subsequently, 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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
dioxygenase, peptide sequencing, homology modelling, molecular docking
in
Molecular Simulation
volume
38
issue
2
pages
144 - 151
publisher
Taylor & Francis
external identifiers
  • wos:000298376100009
  • scopus:84856305187
ISSN
0892-7022
DOI
10.1080/08927022.2011.608672
language
English
LU publication?
yes
id
1869c5d6-2655-4418-804e-230d6e6a2c32 (old id 2333648)
date added to LUP
2012-02-02 14:27:10
date last changed
2017-01-01 03:37:27
@article{1869c5d6-2655-4418-804e-230d6e6a2c32,
  abstract     = {Flavoenzymes have been extensively studied for their structural and mechanistic properties because they find potential application as industrial biocatalysts. They are attractive for biocatalysis because of the selectivity, controllability and efficiency of their reactions. Some of these enzymes catalyse the oxidative modification of protein substrates. Among 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. Dioxygenase enzymes catalyse oxygenation reactions in which both dioxygen atoms are incorporated into the product. A dioxygenase enzyme purified from Aspergillus fumigatus MC8 was subjected to protein digestion followed by peptide sequencing. The 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. The sequence was submitted to protein homology/analogy recognition engine online server for homology modelling and the 3D structure was predicted. Subsequently, 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.},
  author       = {Krishnankutty, Roopesh and Abhilash, Joseph and Haridas, M. and Sabu, Abdulhameed and Isabelle, Perraud Gaime and Roussos, Sevastianos and Augur, Christopher},
  issn         = {0892-7022},
  keyword      = {dioxygenase,peptide sequencing,homology modelling,molecular docking},
  language     = {eng},
  number       = {2},
  pages        = {144--151},
  publisher    = {Taylor & Francis},
  series       = {Molecular Simulation},
  title        = {Dioxygenase from Aspergillus fumigatus MC8: molecular modelling and in silico studies on enzyme-substrate interactions},
  url          = {http://dx.doi.org/10.1080/08927022.2011.608672},
  volume       = {38},
  year         = {2012},
}