ArticlemSphere2019
Functional Metagenomics Reveals a New Catalytic Domain, the Metallo-β-Lactamase Superfamily Domain, Associated with Phytase Activity.
Article in mSphere, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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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.
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- Inositol phosphates as an overlooked phosphorous source in marine ecosystems.The ISME journal · 2025Article
- Phosphorus dynamics and sustainable agriculture: The role of microbial solubilization and innovations in nutrient management.Current research in microbial sciences · 2025Article
- Structural and functional profile of phytases across the domains of life.Current research in structural biology · 2024Review
- Origin, Diversity, and Multiple Roles of Enzymes with Metallo-β-Lactamase Fold from Different Organisms.Cells · 2023Review
- Functional Metagenomics Approach for the Discovery of Novel Genes Encoding Phosphatase Activity.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Characterisation of a soil MINPP phytase with remarkable long-term stability and activity from Acinetobacter sp.PloS one · 2022Article
- Improved sensitivity, accuracy and prediction provided by a high-performance liquid chromatography screen for the isolation of phytase-harbouring organisms from environmental samples.Microbial biotechnology · 2021Article
- Fungal phytases: from genes to applications.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2020Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Inositol-6-phosphate, also known as phytic acid, is a phosphorus source that plays several important roles in the phosphorus cycle and in cell metabolism. The known characterized enzymes responsible for its degradation, the phytases, are mostly derived from cultured individual microorganisms. The catalytic signatures of phytases are restricted to the molecular domains of four protein superfamilies: histidine phosphatases, protein tyrosine phosphatases, the purple acid phosphatases and the β-propeller phosphatases. During function-based screening of previously generated forest soil metagenomic libraries for
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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.