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Marine Biology

, Volume 136, Issue 1, pp 115–127 | Cite as

The enzymes involved in synthesis and utilization of carbamylphosphate in the deep-sea tube worm Riftia pachyptila

  • V. Simon
  • C. Purcarea
  • K. Sun
  • J. Joseph
  • G. Frebourg
  • J.-P. Lechaire
  • F. Gaill
  • G. Hervé
Article

Abstract

 The obligate symbiosis of the deep-sea tube worm Riftia pachyptila with a sulphur-oxidizing bacterium raises important questions concerning its metabolism and metabolic exchanges. In this study, the presence and properties of the enzymes synthesizing and utilizing carbamylphosphate in the arginine and pyrimidine nucleotide pathways were investigated in this worm. The results show that the ammonium-dependent carbamylphosphate synthetase and ornithine transcarbamylase, enzymes involved in the arginine pathway, are present in all body parts of the worm. In contrast, the glutamine-dependent carbamylphosphate synthetase and aspartate transcarbamylase, enzymes involved in the de novo pathway for pyrimidine nucleotides biosynthesis, are present only in the trophosome, the symbiont-harbouring tissue. Although the bacterial nature of these enzymes is not unambigously established, these results strongly suggest that the de novo biosynthesis of pyrimidine nucleotides is limited to the trophosome, the organ where the production of metabolic energy takes place, while the other parts of the worm's body rely on the salvage pathway for the production of the pyrimidine triphosphate nucleotides.

Keywords

Enzyme Arginine Pyrimidine Body Part Ornithine 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag Berlin Heidelberg 2000

Authors and Affiliations

  • V. Simon
    • 1
  • C. Purcarea
    • 1
  • K. Sun
    • 1
  • J. Joseph
    • 1
  • G. Frebourg
    • 2
  • J.-P. Lechaire
    • 2
  • F. Gaill
    • 2
  • G. Hervé
    • 1
  1. 1.Laboratoire de Biochimie des Signaux Régulateurs Cellulaires et Moléculaires, UMR 7631, CNRS, Université Pierre et Marie Curie, 96 Boulevard Raspail, F-75006 Paris, France e-mail: gherve@ccr.jussieu.fr Fax: 0033 (0)1 42 22 13-98FR
  2. 2.Laboratoire de Biologie Marine, INSU–CNRS UPR 9042 Roscoff, UPMC, 7 quai Saint Bernard, F-75252 Paris, FranceFR

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