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Colorimetric Analysis of Alkaline Phosphatase Activity in S. aureus Biofilm
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Widespread promiscuous alkaline phosphatases underscore ancient microbial phosphite utilization.

Morito Sakuma1, Naoki Konno2,3, Sevan Gholipour1

  • 1Michael Smith Laboratories, Faculty of Science, University of British Columbia, Vancouver, BC V6T 1Z4, Canada.

Proceedings of the National Academy of Sciences of the United States of America
|December 4, 2025
PubMed
Summary
This summary is machine-generated.

Bacteria use alkaline phosphatase (PhoA) to oxidize phosphite (Pt) into phosphate, addressing phosphate scarcity. This overlooked PhoA function is widespread in bacteria and crucial for phosphorus cycling.

Keywords:
alkaline phosphatasephosphitephosphite oxidasesphosphorus metabolism

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Area of Science:

  • Microbiology
  • Biochemistry
  • Environmental Science

Background:

  • Phosphate is a vital nutrient, often scarce, limiting bacterial growth and biomolecule production.
  • Bacteria possess enzymes to utilize alternative phosphorus sources like phosphite (Pt) to overcome phosphate limitation.
  • The specific enzymes and microbial roles in phosphite oxidation and its impact on the phosphorus cycle are not fully understood.

Purpose of the Study:

  • To identify and characterize bacterial enzymes involved in phosphite (Pt) oxidation.
  • To investigate the evolutionary history and functional promiscuity of Pt-oxidizing enzymes, particularly alkaline phosphatase (PhoA).
  • To elucidate the role of microbial Pt oxidation in bacterial phosphate metabolism and the global phosphorus cycle.

Main Methods:

  • Bioinformatic analysis of Pt-oxidizing enzymes, including phosphite dehydrogenase (PtxD) and alkaline phosphatase (PhoA).
  • Comparative evolutionary analysis of PhoA and PtxD distribution across bacterial lineages.
  • Biochemical characterization of extant and reconstructed ancestral PhoA enzymes for Pt oxidation activity.
  • Site-directed mutagenesis to assess the impact of active-site residues on PhoA's Pt oxidase and native functions.

Main Results:

  • Alkaline phosphatase (PhoA) is widely distributed in bacteria, appearing early in evolution, while phosphite dehydrogenase (PtxD) emerged later in specific lineages.
  • Most tested PhoA enzymes, including ancestral forms, demonstrated phosphite oxidation activity.
  • Disrupting active-site residues in PhoA reduced its phosphite oxidase activity with only partial impact on its native function.

Conclusions:

  • PhoA possesses a promiscuous phosphite oxidation capability, representing an overlooked mechanism for bacterial phosphate acquisition.
  • This promiscuous function of PhoA plays a significant role in bacterial phosphate metabolism and phosphite cycling in ecosystems.
  • The widespread nature of PhoA suggests a substantial contribution to microbial phosphite oxidation in diverse environments.