ArticleMicrobial biotechnology2024
Characterization of an extremophile bacterial acid phosphatase derived from metagenomics analysis.
Article in Microbial biotechnology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
6 citing papers in PubMed.
- Development of advanced bioinformatic profiles to improve the detection and functional understanding of fungal acid phosphatases.Applied and environmental microbiology · 2026Article
- Eco-technological potential of salinity-driven functional specialization in Indian solar salterns revealed by integrated culturomics and whole-metagenome profiling.BMC microbiology · 2026Article
- A Biotechnological Approach to Enzyme-Based Fertilisers: Immobilisation of Acid Phosphatases.Microbial biotechnology · 2026Article
- The distribution and kinetics of phosphatase activity in European agricultural soils under long-term tillage reduction practices.Sustainable microbiology · 2026Article
- Thermotolerant class A acid phosphatase active across broad pH range and diverse substrates.Protein science : a publication of the Protein Society · 2025Article
- Characterization of an extremophile bacterial acid phosphatase derived from metagenomics analysis.Microbial biotechnology · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
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.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.