Computational study of the mechanism of a polyurethane esterase A (PueA) from Pseudomonas chlororaphis
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Título
Computational study of the mechanism of a polyurethane esterase A (PueA) from Pseudomonas chlororaphisFecha de publicación
2024Editor
Royal Society of ChemistryISSN
1359-6640; 1364-5498Cita bibliográfica
WIDEREK, Katarzyna, et al. Computational study of the mechanism of a polyurethane esterase A (PueA) from Pseudomonas chlororaphis. Faraday Discussions, 2024.Tipo de documento
info:eu-repo/semantics/articleVersión
info:eu-repo/semantics/publishedVersionPalabras clave / Materias
Resumen
The effective management of plastic waste has become a global imperative, given our reliance on a linear model in which plastics are manufactured, used once, and then discarded. This has led to the pervasive accumulation ... [+]
The effective management of plastic waste has become a global imperative, given our reliance on a linear model in which plastics are manufactured, used once, and then discarded. This has led to the pervasive accumulation of plastic debris in landfills and environmental contamination. Recognizing this issue, numerous initiatives are underway to address the environmental repercussions associated with plastic disposal. In this study, we investigate the possible molecular mechanism of polyurethane esterase A (PueA), which has been previously identified as responsible for the degradation of a polyester polyurethane (PU) sample in Pseudomonas chlororaphis, as an effort to develop enzymatic biodegradation solutions. After generating the unsolved 3D structure of the protein by AlphaFold2 from its known genome, the enzymatic hydrolysis of the same model PU compound previously used in experiments has been explored employing QM/MM molecular dynamics simulations. This required a preliminary analysis of the 3D structure of the apo-enzyme, identifying the putative active site, and the search for the optimal protein–substrate binding site. Finally, the resulting free energy landscape indicates that wild-type PueA can degrade PU chains, although with low-level activity. The reaction takes place by a characteristic four-step path of the serine hydrolases, involving an acylation followed by a diacylation step. Energetics and structural analysis of the evolution of the active site along the reaction suggests that PueA can be considered a promising protein scaffold for further development to achieve efficient biodegradation of PU. [-]
Publicado en
Faraday Discussions, 2024Entidad financiadora
Ministerio de Ciencia, Innovación y Universidades | Generalitat Valenciana | Universitat Jaume I | Ministerio de Ciencia e Innovación and Fondo Social Europeo | European Regional Development Fund
Código del proyecto o subvención
PID2021-123332OB-C21 | CIPROM/2021/079 | UJI-B2021-71 | RYC2020-030596-I | IDIFEDER/2021/02
Derechos de acceso
info:eu-repo/semantics/openAccess
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