Criteria for Engineering Cutinases: Bioinformatics Analysis of Catalophores
Cutinases are bacterial and fungal enzymes that catalyze the hydrolysis of natural cutin, a three-dimensional inter-esterified polyester with epoxy-hydroxy fatty acids with chain lengths between 16 and 18 carbon atoms. Due to their ability to accept long chain substrates, cutinases are also effectiv...
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-06-01
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| Series: | Catalysts |
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| Online Access: | https://www.mdpi.com/2073-4344/11/7/784 |
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| author | Sara Fortuna Marco Cespugli Anamaria Todea Alessandro Pellis Lucia Gardossi |
| author_facet | Sara Fortuna Marco Cespugli Anamaria Todea Alessandro Pellis Lucia Gardossi |
| author_sort | Sara Fortuna |
| collection | DOAJ |
| description | Cutinases are bacterial and fungal enzymes that catalyze the hydrolysis of natural cutin, a three-dimensional inter-esterified polyester with epoxy-hydroxy fatty acids with chain lengths between 16 and 18 carbon atoms. Due to their ability to accept long chain substrates, cutinases are also effective in catalyzing in vitro both the degradation and synthesis of several synthetic polyesters and polyamides. Here, we present a bioinformatics study that intends to correlate the structural features of cutinases with their catalytic properties to provide rational basis for their effective exploitation, particularly in polymer synthesis and biodegradation. The bioinformatics study used the BioGPS method (Global Positioning System in Biological Space) that computed molecular descriptors based on Molecular Interaction Fields (MIFs) described in the GRID force field. The information was used to generate catalophores, spatial representations of the ability of each enzymatic active site to establish hydrophobic and electrostatic interactions. These tools were exploited for comparing cutinases to other serine-hydrolases enzymes, namely lipases, esterases, amidases and proteases, and for highlighting differences and similarities that might guide rational engineering strategies. Structural features of cutinases with their catalytic properties were correlated. The “catalophore” of cutinases indicate shared features with lipases and esterases. |
| first_indexed | 2024-03-10T10:00:20Z |
| format | Article |
| id | doaj.art-15bdd1c68af547acb290b19cf7f2ffc7 |
| institution | Directory Open Access Journal |
| issn | 2073-4344 |
| language | English |
| last_indexed | 2024-03-10T10:00:20Z |
| publishDate | 2021-06-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Catalysts |
| spelling | doaj.art-15bdd1c68af547acb290b19cf7f2ffc72023-11-22T01:58:57ZengMDPI AGCatalysts2073-43442021-06-0111778410.3390/catal11070784Criteria for Engineering Cutinases: Bioinformatics Analysis of CatalophoresSara Fortuna0Marco Cespugli1Anamaria Todea2Alessandro Pellis3Lucia Gardossi4Department of Chemical and Pharmaceutical Sciences, University of Trieste, Via L. Giorgieri 1, 34127 Trieste, ItalyDepartment of Chemical and Pharmaceutical Sciences, University of Trieste, Via L. Giorgieri 1, 34127 Trieste, ItalyDepartment of Chemical and Pharmaceutical Sciences, University of Trieste, Via L. Giorgieri 1, 34127 Trieste, ItalyDepartment of Agrobiotechnology, Institute of Environmental Biotechnology, University of Natural Resources and Life Sciences Vienna, Konrad Lorenz Strasse 20, 3430 Tulln an der Donau, AustriaDepartment of Chemical and Pharmaceutical Sciences, University of Trieste, Via L. Giorgieri 1, 34127 Trieste, ItalyCutinases are bacterial and fungal enzymes that catalyze the hydrolysis of natural cutin, a three-dimensional inter-esterified polyester with epoxy-hydroxy fatty acids with chain lengths between 16 and 18 carbon atoms. Due to their ability to accept long chain substrates, cutinases are also effective in catalyzing in vitro both the degradation and synthesis of several synthetic polyesters and polyamides. Here, we present a bioinformatics study that intends to correlate the structural features of cutinases with their catalytic properties to provide rational basis for their effective exploitation, particularly in polymer synthesis and biodegradation. The bioinformatics study used the BioGPS method (Global Positioning System in Biological Space) that computed molecular descriptors based on Molecular Interaction Fields (MIFs) described in the GRID force field. The information was used to generate catalophores, spatial representations of the ability of each enzymatic active site to establish hydrophobic and electrostatic interactions. These tools were exploited for comparing cutinases to other serine-hydrolases enzymes, namely lipases, esterases, amidases and proteases, and for highlighting differences and similarities that might guide rational engineering strategies. Structural features of cutinases with their catalytic properties were correlated. The “catalophore” of cutinases indicate shared features with lipases and esterases.https://www.mdpi.com/2073-4344/11/7/784cutinasesmolecular interaction fields descriptorscatalophoreserin hydrolases |
| spellingShingle | Sara Fortuna Marco Cespugli Anamaria Todea Alessandro Pellis Lucia Gardossi Criteria for Engineering Cutinases: Bioinformatics Analysis of Catalophores Catalysts cutinases molecular interaction fields descriptors catalophore serin hydrolases |
| title | Criteria for Engineering Cutinases: Bioinformatics Analysis of Catalophores |
| title_full | Criteria for Engineering Cutinases: Bioinformatics Analysis of Catalophores |
| title_fullStr | Criteria for Engineering Cutinases: Bioinformatics Analysis of Catalophores |
| title_full_unstemmed | Criteria for Engineering Cutinases: Bioinformatics Analysis of Catalophores |
| title_short | Criteria for Engineering Cutinases: Bioinformatics Analysis of Catalophores |
| title_sort | criteria for engineering cutinases bioinformatics analysis of catalophores |
| topic | cutinases molecular interaction fields descriptors catalophore serin hydrolases |
| url | https://www.mdpi.com/2073-4344/11/7/784 |
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