Skip to main content
Log in

Evidence for two distinct phosphonate-degrading enzymes (C-P lyases) in Arthrobacter sp. GLP-1

  • Published:
Biodegradation Aims and scope Submit manuscript

Abstract

Arthrobacter sp. GLP-1 can utilize a wide range of organophosphonates as its sole source of phosphorus. The in-situ formation of sarcosine and methane from glyphosate and methanephosphonic acid respectively was studied. These two processes are differentially induced during phosphorus-deprivation. Methanephosphonic acid strongly inhibits glyphosate degradation (I50 10 μM), but glyphosate has very little effect on methane generation (I50 150 mM). The pattern of inhibition by other organophosphonates and organophosphonate analogues is also very different for the two systems. Degradation of glyphosate and methanephosphonic acid therefore represent distinct processes.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

Abbreviations

f.wt.:

fresh weight

MP-lyase:

methanephosphonate lyase

References

  • Amrhein N & Filner P (1973) cAMP in Chlamydomonas reinhardti: isolation and characterization. Proc. Nat. Acad. Sci. USA 70: 1099–1103

    Google Scholar 

  • Avila LZ, Loo SH & Frost JW (1987) Chemical and mutagenic analysis of aminomethylphosphonate biodegradation. J. Am. Chem. Soc. 109: 6758–6764

    Google Scholar 

  • Balthazor TM & Hallas LE (1986) Glyphosate-degrading microorganisms from industrial activated sludge. Appl. Env. Microbiol. 51: 432–434

    Google Scholar 

  • Bradford MM (1976) A rapid and sensitive method for microgram protein quantitation. Anal. Biochem. 72: 248–254

    Google Scholar 

  • Chen C, Ye Q, Zhu Z, Wanner BL & Walsh CT (1990) Molecular biology of carbon-phosphorous bond cleavage. Cloning and sequencing of the phn (psiD) genes involved in alkylphosphonate uptake and C-P lyase activity in Escherichia coli B. J. Biol. Chem. 265: 4461–4471

    Google Scholar 

  • Cook AM, Daughton CG & Alexander M (1978) Phosphonate utilization by bacteria. J. Bacteriol. 133: 85–90

    Google Scholar 

  • Cordeiro ML, Pompliano DL & Frost JW (1986) Degradation and detoxification of organophosphonates: Cleavage of the carbon to phosphorus bond. J. Am. Chem. Soc. 108: 332–334

    Google Scholar 

  • Frost JW, Loo S, Cordeiro ML & Li D (1987) Radical-based dephosphorylation and organophosphate biodegradation. J. Am. Chem. Soc. 109: 2166–2171

    Google Scholar 

  • Hilderbrand RL (1983) Foreword. In: Hilderbrand RL (Ed) The Role of Phosphonates in Living Systems. CRC Press, Boca Raton, Florida. 2–3

    Google Scholar 

  • Horiguchi M (1984) Chemistry of phosphonic and phosphinic acids. In: Hori T, Horiguchi M & Hayashi A (Eds) Biochemistry of Natural C-P Compounds. Maruzen, Kyoto. 8–22

    Google Scholar 

  • Horiguchi M & Kandatsu M (1959) Isolation of 2-aminoethane-phosphonic acid from rumen protozoa. Nature (London) 184: 901–902

    Google Scholar 

  • Kishore GM & Jacob GS (1987) Degradation of glyphosate by Pseudomonas sp. PG2982 via a sarcosine intermediate. J. Biol. Chem. 262: 12164–12168

    Google Scholar 

  • LaNauze JM, Coggins JR & Dixon HBF (1977) Aldolase-like imine formation in the mechanism of action of phosphono-acetaldehyde hydrolase. Biochem. J. 165: 409–411

    Google Scholar 

  • LaNauze JM, Rosenberg H & Shaw D (1970) The enzymic cleavage of the carbon-phosphorus bond. Purification and properties of phosphonatase. Biochim. Biophys. Acta 212: 332–350

    Google Scholar 

  • Lanzetta PA, Alvarez LJ, Reinach PS & Candia DA (1979) An improved assay for nanomole amounts of inorganic phosphate. Anal. Biochem. 100: 95–97

    Google Scholar 

  • Moore IK, Braymer HD & Larson AD (1983) Isolation of a Pseudomonas sp. which utilizes the phosphonate herbicide glyphosate. Appl. Env. Microbiol. 46: 316–320

    Google Scholar 

  • Murata K, Higaki N & Kimura A (1988) Detection of carbonphosphorus lyase activity in cell free extracts of Enterobacter aerogenes. Biochem. Biophys. Res. Commun. 157: 190–195

    Google Scholar 

  • Murata K, Higaki N & Kimura A (1989) A microbial carbonphosphorus bond cleavage enzyme requires two protein components for activity. J. Bacteriol. 171: 4504–4506

    Google Scholar 

  • Pipke R & Amrhein N (1988a) Degradation of the phosphonate herbicide glyphosate by Arthrobacter atrocyaneus ATCC 13752. Appl. Env. Microbiol. 54: 1293–1296

    Google Scholar 

  • Pipke R & Amrhein N (1988b) Carbon-phosphorus lyase activity in permeabilized cells of Arthrobacter sp. GLP-1. FEBS Lett. 236: 135–138

    Google Scholar 

  • Pipke R, Amrhein N, Jacob GS, Schaefer J & Kishore GM (1987a) Metabolism of glyphosate in an Arthrobacter sp. GLP-1. Eur. J. Biochem. 165: 267–273

    Google Scholar 

  • Pipke R, Schulz A & Amrhein N (1987b) Uptake of glyphosate by an Arthrobacter sp. Appl. Env. Microbiol. 53: 974–978

    Google Scholar 

  • Quinn JP, Peden JMM & Dick RE (1989) Carbon-phosphorus bond cleavage by Gram-positive and Gram-negative soil bacteria. Appl. Microbiol. Biotechnol. 31: 283–287

    Google Scholar 

  • Schowanek D & Verstraete W (1990) Phosphonate utilization by bacterial cultures and enrichments from environmental samples. Appl. Env. Microbiol. 56: 895–903

    Google Scholar 

  • Shames SL, Wackett LP, Labarge MS, Kuczkowski RL & Walsh CT (1987) Fragmentative and stereochemical isomerization probes for homolytic carbon to phosphorus bond scission catalyzed by bacterial carbon-phosphorus lyase. Bioorg. Chem. 15: 366–373

    Google Scholar 

  • Shinabarger DL & Braymer HD (1986) Glyphosate catabolism by Pseudomonas sp. strain PG2982. J. Bacteriol. 168: 702–707

    Google Scholar 

  • Shinabarger DL, Schmitt EK, Braymer HD & Larson AD (1984) Phosphonate utilization by the glyphosate-degrading Pseudomonas sp. strain PG2982. Appl. Env. Microbiol. 4: 1049–1050

    Google Scholar 

  • Talbot HW, Lohnson LM & Munnecke DM (1984) Glyphosate utilization by Pseudomonas sp. and Alcaligenes sp. isolated from environmental sources. Curr. Microbiol. 10: 255–260

    Google Scholar 

  • Wacket LP, Shames SL, Venditti CP & Walsh CT (1987) Bacterial carbon-phosphorus lyase: products, rates and regulation of phosphonic and phosphinic acid metabolism. J. Bacteriol. 19: 710–717

    Google Scholar 

  • Wanner BL (1987) Phosphate regulation of gene expression in Escherichia coli. In: Neidhart FC (Ed) Escherichia coli and Salmonella typhimurium Cellular and Molecular Biology, Vol 2 (pp 1326–1333). ASM, Washington

    Google Scholar 

  • Wanner BL & Boline JA (1990) Mapping and molecular cloning of the phn (psiD) locus for phosphonate utilization in Escherichia coli. J. Bacteriol. 172: 1186–1196

    Google Scholar 

  • Winkler KC & DeHaan PG (1948) On the action of sulfanilamide XII. A set of non-competitive sulfanilamide antagonists for Escherichia coli. Arch. Biochem. 18: 97–107

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Kertesz, M., Elgorriaga, A. & Amrhein, N. Evidence for two distinct phosphonate-degrading enzymes (C-P lyases) in Arthrobacter sp. GLP-1. Biodegradation 2, 53–59 (1991). https://doi.org/10.1007/BF00122425

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00122425

Key words

Navigation