Consejo Superior de Investigaciones Científicas, Estación Experimental del Zaidín, Department of Environmental Protection, Granada, Spain.
Department of Biochemistry and Molecular Biology II, Pharmacy School, Granada University, Granada, Spain.
Microb Biotechnol. 2024 Apr;17(4):e14404. doi: 10.1111/1751-7915.14404.
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.
酸性磷酸酶是在各种有机磷分子水解中起关键作用的酶。通过对不同环境中的遗传图谱和序列进行分析，发现了一种名为 FS6 的假定酸性磷酸酶。FS6 与 C 型酸性磷酸酶具有高度的序列相似性，并在其蛋白质序列中保留了超过 30%的共识残基。在大肠杆菌中产生的带有组氨酸标签的重组 FS6 表现出极端微生物特性，在 pH 值为 3.5 到 8.5 的较宽范围内有效发挥作用。该酶在 25 到 50°C 之间表现出最佳活性，其熔点为 51.6°C。通过各种底物测定了动力学参数，FS6 催化生理底物的反应效率至少比催化对硝基苯磷酸酯的反应效率高 100 倍。此外，FS6 在溶液中为十聚体，而与其家族中结晶蛋白的二聚体形式不同。
