Two distinct alcohol dehydrogenase classes mediate bacterial 2‐hydroxyethylphosphonate catabolism
Francesca Piazza, Marianna Rodella, Nicholas Salanti, Giovanni Merici, Elisa Rossi, Claudio Rivetti, Florian Götzinger, Katharina Pallitsch, Alessio Peracchi · 2026
Read Two distinct alcohol dehydrogenase classes mediate bacterial 2‐hydroxyethylphosphonate catabolism by Francesca Piazza, Marianna Rodella, Nicholas Salanti, Giovanni Merici, Elisa Rossi, Claudio Rivetti, Florian Götzinger, Katharina Pallitsch, Alessio Peracchi (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/PMC13576164.txt.
Description
Francesca Piazza leads a 2026 study of how bacteria break down a natural phosphorus compound, 2-hydroxyethylphosphonate, often shortened to HEP. Phosphonates carry a direct carbon-phosphorus bond and serve microbes as a phosphorus source. The breakdown route for HEP was poorly mapped until now.
Gene analysis and lab work showed a dedicated pathway: HEP is first oxidised into an activated form that known enzymes can finish processing. Two unrelated enzyme families can run that key step, one kin to a known biosynthetic enzyme and one newly described, named PbfG. Both use zinc, yet they differ sharply in shape and efficiency, a case of convergent evolution. The new family worked faster and seemed specialised for the job. Related pathways for a sister compound often stay separate, the authors note.
Catalog record
| CREATOR | Francesca Piazza, Marianna Rodella, Nicholas Salanti, Giovanni Merici, Elisa Rossi, Claudio Rivetti, Florian Götzinger, Katharina Pallitsch, Alessio Peracchi |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 49 KB |
| LICENSE | https://creativecommons.org/licenses/by/4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |