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

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.

• Authors: G McMullan, J P Quinn
• Journal: Journal of bacteriology (J Bacteriol) Vol. 176 Issue 2 Pg. 320-4 (Jan 1994) ISSN: 0021-9193 [Print] United States
• PMID: 8288524 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Metals
• Organophosphonates
• Phosphorus
• glyphosate
• Carbon
• Hydrolases
• phosphonoacetaldehyde hydrolase
• Isocitrate Lyase
• Phosphonoacetic Acid
• Glycine

Topics

• Carbon (deficiency, metabolism)
• Enzyme Induction
• Glycine (analogs & derivatives, pharmacology)
• Hydrolases (biosynthesis, drug effects, metabolism)
• Isocitrate Lyase (biosynthesis)
• Metals (pharmacology)
• Organophosphonates (pharmacology)
• Phosphonoacetic Acid (metabolism)
• Phosphorus (deficiency, metabolism)
• Pseudomonas fluorescens (enzymology, growth & development, metabolism)
• Substrate Specificity