@misc{10481/92392,
year = {2024},
month = {4},
url = {https://hdl.handle.net/10481/92392},
abstract = {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.},
organization = {Grants from the Ministry of Science through grants from the Plan Nacional 2021 (PID2021-123469OBI00)
and Transición Ecológica (TED2021129632BI00) and European Commission projects EJP soils (EJPSOIL862695) and PREPSOIL (HE/CL5SOILM/0102)},
publisher = {John Wiley & Sons},
title = {Characterization of an extremophile bacterial acid phosphatase derived from metagenomics analysis},
doi = {10.1111/1751-7915.14404},
author = {Recio Muñoz, María Isabel and de la Torre, Jesús and Daddaoua, Abdelali and Udaondo, Zulema and Duque, Estrella and Gavira Gallardo, José Antonio and López Sánchez, Carmen and Ramos, Juan Luis},
}