Versatile Lipases from the Candida rugosa-like Family: A Mechanistic Insight Using Computational Approaches
| Autor: | Javier Rodríguez-Salarichs, María Jesús Martínez, Alicia Prieto, Jorge Barriuso, Mario García de Lacoba |
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| Přispěvatelé: | Ministerio de Economía y Competitividad (España), European Commission, Comunidad de Madrid, Rodríguez-Salarichs, Javier [0000-0002-2932-0142], Prieto, Alicia [0000-0002-5075-4025], Martínez, María Jesús [0000-0003-2166-1097], Barriuso, Jorge [0000-0003-0916-6560], Rodríguez-Salarichs, Javier, Prieto, Alicia, Martínez, María Jesús, Barriuso, Jorge |
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
General Chemical Engineering
In silico Library and Information Sciences 01 natural sciences Isozyme Ophiostoma Article Substrate Specificity 0103 physical sciences Sterol esterase Lipase Candida chemistry.chemical_classification 010304 chemical physics biology Chemistry Fatty acid General Chemistry Sterol Esterase Sterol 0104 chemical sciences Computer Science Applications Candida rugosa 010404 medicinal & biomolecular chemistry Enzyme Biochemistry Saccharomycetales biology.protein |
| Zdroj: | Journal of Chemical Information and Modeling Digital.CSIC. Repositorio Institucional del CSIC instname Digital.CSIC: Repositorio Institucional del CSIC Consejo Superior de Investigaciones Científicas (CSIC) |
| ISSN: | 1549-960X 1549-9596 |
| Popis: | 26 p.-5 fig. Lipases are enzymes able to catalyze the hydrolysis or synthesis of triglycerides, depending on the reaction conditions, whereas sterol esterases show the same ability on sterol esters. Structurally, both kinds of enzymes display an α/β-hydrolase fold, with a substrate-binding pocket formed by a hydrophobic cavity covered by a mobile lid. However, it has been reported that some lipases from the Candida rugosa-like family display wide substrate specificity on both triglycerides and sterol esters. Among them, enzymes with different biotechnological applications, such as the lipase isoenzymes produced by C. rugosa and the sterol esterase from Ophiostoma piceae, have been exhaustively characterized and their crystal structures are available. Differences in substrate affinity among these proteins have been attributed to changes in their hydrophobicity. In this work, we analyzed the full catalytic mechanisms of these proteins using molecular dynamics tools, gaining insight into their mechanistic properties. In addition, we developed an in silico protocol to predict the substrate specificity using C. rugosa and O. piceae lipases as model enzymes and triglycerides and cholesterol esters with different fatty acid chain lengths as model substrates. The protocol was validated by comparing the in silico results with those described in the literature. These results would be useful to perform virtual screening of substrates for enzymes of the C. rugosa-like family with unknown catalytic properties. This work was supported by the Spanish projects BIO2015-73697-JIN from MEICOMP co-financed with FEDER funds and RETOPROSOST2 S/2018/EMT-4459 from Comunidad de Madrid. The authors would also like to thank IBISBA1.0 project (H2020 730976) and the SusPlast-CSIC Interdisciplinary Platform for their support. |
| Databáze: | OpenAIRE |
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