Common and distant structural characteristics of Feruloyl esterase families from Aspergillus oryzae
| Autor: | Gianni Panagiotou, Valeria Mapelli, Lisbeth Olsson, D.B.R.K. Gupta Udatha |
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| Přispěvatelé: | Udatha, D, Mapelli, V, Panagiotou, G, Olsson, L |
| Jazyk: | angličtina |
| Rok vydání: | 2012 |
| Předmět: |
Pectin
Applied Microbiology Aspergillus oryzae SECONDARY-STRUCTURE Fungal Protein Gene Expression lcsh:Medicine Yeast and Fungal Models Plant Science Biochemistry 3-DIMENSIONAL PROFILES Substrate Specificity chemistry.chemical_compound ANALOGOUS ENZYMES Feruloyl esterase Carboxylic Ester Hydrolases - Chemistry CIRCULAR-DICHROISM SPECTRA Molecular Cell Biology Macromolecular Structure Analysis Lignin lcsh:Science chemistry.chemical_classification Fungal protein Multidisciplinary biology food and beverages Recombinant Proteins Enzymes ENZYME EVOLUTION Pharmacophore Research Article Biotechnology Protein Structure food.ingredient Molecular Sequence Data Plant Pathogens BIOLOGY 3 DIMENSIONS PENICILLIUM-EXPANSUM Fungal Proteins Structure-Activity Relationship food Model Organisms Carboxylic Ester Hydrolase Aspergillus Oryzae - Enzymology PROTEIN-STRUCTURE PREDICTION Hemicellulose Amino Acid Sequence Biology Fungal Proteins - Chemistry lcsh:R Proteins Computational Biology Plant Pathology biology.organism_classification Enzyme chemistry SIGNAL PEPTIDES I-TASSER Enzyme Structure lcsh:Q Carboxylic Ester Hydrolases |
| Zdroj: | PLoS ONE, Vol 7, Iss 6, p e39473 (2012) PLoS ONE Udatha, D B R K G, Mapelli, V, Panagiotou, G & Olsson, L 2012, ' Common and Distant Structural Characteristics of Feruloyl Esterase Families from Aspergillus oryzae ', P L o S One, vol. 7, no. 6, pp. e39473 . https://doi.org/10.1371/journal.pone.0039473 |
| DOI: | 10.1371/journal.pone.0039473 |
| Popis: | Background: Feruloyl esterases (FAEs) are important biomass degrading accessory enzymes due to their capability of cleaving the ester links between hemicellulose and pectin to aromatic compounds of lignin, thus enhancing the accessibility of plant tissues to cellulolytic and hemicellulolytic enzymes. FAEs have gained increased attention in the area of biocatalytic transformations for the synthesis of value added compounds with medicinal and nutritional applications. Following the increasing attention on these enzymes, a novel descriptor based classification system has been proposed for FAEs resulting into 12 distinct families and pharmacophore models for three FAE sub-families have been developed. Methodology/Principal Findings: The feruloylome of Aspergillus oryzae contains 13 predicted FAEs belonging to six sub-families based on our recently developed descriptor-based classification system. The three-dimensional structures of the 13 FAEs were modeled for structural analysis of the feruloylome. The three genes coding for three enzymes, viz., A.O.2, A.O.8 and A.O.10 from the feruloylome of A. oryzae, representing sub-families with unknown functional features, were heterologously expressed in Pichia pastoris, characterized for substrate specificity and structural characterization through CD spectroscopy. Common feature-based pharamacophore models were developed according to substrate specificity characteristics of the three enzymes. The active site residues were identified for the three expressed FAEs by determining the titration curves of amino acid residues as a function of the pH by applying molecular simulations. Conclusions/Significance: Our findings on the structure-function relationships and substrate specificity of the FAEs of A. oryzae will be instrumental for further understanding of the FAE families in the novel classification system. The developed pharmacophore models could be applied for virtual screening of compound databases for short listing the putative substrates prior to docking studies or for post-processing docking results to remove false positives. Our study exemplifies how computational predictions can complement to the information obtained through experimental methods. © 2012 Udatha et al. published_or_final_version |
| Databáze: | OpenAIRE |
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