Characterization of an extremophile bacterial acid phosphatase derived from metagenomics analysis.
Microb Biotechnol
; 17(4): e14404, 2024 Apr.
Article
em En
| MEDLINE
| ID: mdl-38588312
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.
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1
Base de dados:
MEDLINE
Assunto principal:
Fosfatase Ácida
/
Extremófilos
Idioma:
En
Ano de publicação:
2024
Tipo de documento:
Article