In vitro characterization of a phosphate starvation-independent carbon- phosphorus bond cleavage activity in Pseudomonas fluorescens 23F

G. McMullan*, J. P. Quinn

*Corresponding author for this work

Research output: Contribution to journalArticle

46 Citations (Scopus)

Abstract

A novel, metal-dependent, carbon-phosphorus bond cleavage activity, provisionally named phosphonoacetate hydrolase, was detected in crude extracts of Pseudomonas fluorescens 23F, an environmental isolate able to utilize phosphonoacetate as the sole carbon and phosphorus source. The activity showed unique specificity toward this substrate; its organic product, acetate, was apparently metabolized by the glyoxylate cycle enzymes of the host cell. Unlike phosphonatase, which was also detected in crude extracts of P. fluorescens 23F, phosphonoacetate hydrolase was inducible only in the presence of its sole substrate and did not require phosphate starvation.

Original languageEnglish
Pages (from-to)320-324
Number of pages5
JournalJournal of Bacteriology
Volume176
Issue number2
Publication statusPublished - 1994

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Immunology

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