Applied Microbiology and Biotechnology

, Volume 101, Issue 1, pp 139–145 | Cite as

Another example of enzymatic promiscuity: the polyphosphate kinase of Streptomyces lividans is endowed with phospholipase D activity

  • Catherine Esnault
  • Denis Leiber
  • Claire Toffano-Nioche
  • Zahra Tanfin
  • Marie-Joelle Virolle
Biotechnologically relevant enzymes and proteins


Polyphosphate kinases (PPK) from different bacteria, including that of Streptomyces lividans, were shown to contain the typical HKD motif present in phospholipase D (PLD) and showed structural similarities to the latter. This observation prompted us to investigate the PLD activity of PPK of S. lividans, in vitro. The ability of PPK to catalyze the hydrolysis of phosphatidylcholine (PC), the PLD substrate, was assessed by the quantification of [3H]phosphatidic acid (PA) released from [3H]PC-labeled ELT3 cell membranes. Basal cell membrane PLD activity as well as GTPγS-activated PLD activity was higher in the presence than in absence of PPK. After abolition of the basal PLD activity of the membranes by heat or tryptic treatment, the addition of PPK to cell membranes was still accompanied by an increased production of PA demonstrating that PPK also bears a PLD activity. PLD activity of PPK was also assessed by the production of choline from hydrolysis of 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) in the presence of the Amplex Red reagent and compared to two commercial PLD enzymes. These data demonstrated that PPK is endowed with a weak but clearly detectable PLD activity. The question of the biological signification, if any, of this enzymatic promiscuity is discussed.


Polyphosphate kinase Phospholipase D Promiscuous enzyme Lipid droplets 



This work was financed by the University Paris-Sud, the University Pierre and Marie Curie, and the CNRS. Dr. Bruno Collinet is acknowledged for helpful discussions.

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.

Ethical statements

This article does not contain any studies with human participants or animals performed by any of the authors.


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Copyright information

© Springer-Verlag Berlin Heidelberg 2016

Authors and Affiliations

  • Catherine Esnault
    • 1
    • 2
  • Denis Leiber
    • 3
  • Claire Toffano-Nioche
    • 4
  • Zahra Tanfin
    • 5
  • Marie-Joelle Virolle
    • 1
  1. 1.Institute of Integrative Biology of the Cell (I2BC), Group “Energetic Metabolism of Streptomyces”, CEA, CNRSUniversity of Paris-Sud, INRA, University Paris-SaclayGif-sur-Yvette CedexFrance
  2. 2.Sorbonne Universities, UPMC University of Paris 06ParisFrance
  3. 3.INSERM U1063University of AngersAngersFrance
  4. 4.Institute of Integrative Biology of the Cell (I2BC), Group “RNA Sequence, Structure & Function”, CEA, CNRSUniversity of Paris-Sud, INRA, University Paris-SaclayGif-sur-Yvette CedexFrance
  5. 5.Institut de Biologie Animale, Intégrative et Cellulaire (IBAIC), INSERM U1174University of Paris-SudOrsay CedexFrance

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