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Título: | Characterization of an extremophile bacterial acid phosphatase derived from metagenomics analysis |
Autor: | Recio, Maria Isabel; Torre, Jesús de la; Daddaoua, Abdelali CSIC ORCID; Udaondo, Zulema CSIC ORCID; Duque, Estrella CSIC ORCID; Gavira Gallardo, J. A. CSIC ORCID ; López- Sánchez, Carmen; Ramos, Juan L. CSIC ORCID | Fecha de publicación: | 8-abr-2024 | Editor: | John Wiley & Sons | Citación: | Microbial Biotechnology 17: e14404 (2024) | Resumen: | Acid phosphatases are enzymes that play a crucial role in the hydrolysis of various organophosphorous molecules. A putative acid phosphatase called FS6 was identified using genetic profiles and sequences from different environments. FS6 showed high sequence similarity to type C acid phosphatases and retained more than 30% of consensus residues in its protein sequence. A histidine-tagged recombinant FS6 produced in Escherichia coli exhibited extremophile properties, functioning effectively in a broad pH range between 3.5 and 8.5. The enzyme demonstrated optimal activity at temperatures between 25 and 50°C, with a melting temperature of 51.6°C. Kinetic parameters were determined using various substrates, and the reaction catalysed by FS6 with physiological substrates was at least 100- fold more efficient than with p- nitrophenyl phosphate. Furthermore, FS6 was found to be a decamer in solution, unlike the dimeric forms of crystallized proteins in its family | Versión del editor: | https://doi.org/10.1111/1751-7915.14404 | URI: | http://hdl.handle.net/10261/355380 | ISSN: | 1751-7915 |
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