ArticleBMC microbiology2025
Identification and characterization of alternative homologs of histidinol-phosphate phosphatase in Pseudomonas aeruginosa.
Article in BMC microbiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Accumulation of Histidine Reduce the Susceptibility of Vibrio splendidus Persister Cells to Tetracycline.Environmental microbiology reports · 2026Article
- Impact of Oil Spill Stress on Amino Acid Abundance inMetabolites · 2026Article
- Histidinol-Phosphate Phosphatase FoHis2 Is Essential for Growth, Stress Responses, and Full Virulence inJournal of fungi (Basel, Switzerland) · 2026Article
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Authors and funding
5 authors.
Funding
Abstract
HolPase is a crucial enzyme catalyzing dephosphorylation of L-histidinol-phosphate (Hol-P) to L-histidinol, usually the last and most difficult enzyme to be identified in histidine biosynthesis due to its complex origin and evolution. We previously reported that PA0335 encode a HolPase belonging to the HAD family and inactivation resulted incomplete L-histidine auxotrophy in Pseudomonas aeruginosa, suggesting the presence of alternate HolPase enzymes. In this study, the alternative homologs of PA0335 encoded HolPase were identified and primarily characterized in P. aeruginosa. PA3255 and PA1143 code phosphatase with side HolPase activity. PA0335 play a key role in histidine biosynthesis, PA3255 respond mainly for the residual growth when PA0335 HolPase is absence. Moreover, all three genes, especially for PA3255, are required for the resistance of PA to ciprofloxacin and meropenem, while PA3255 and PA0335 are required for the full virulence but inactivation of PA1143 increased the pathogens of P. aeruginosa. PA0335 and PA3255 could be used as targets for P. aeruginosa infection treatment separately or synergistically due to their participates in histidine auxotrophy, full virulence and obvious antibiotics resistance in P. aeruginosa. The relation and regulation of the three phosphatases with HolPase or side HolPase activity need further study.
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