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Pyrococcus abyssi alkaline phosphatase: the dimer is the active form.

S Zappa1, J Boudrant, E R Kantrowitz

  • 1Laboratoire des Sciences du Génie Chimique, CNRS, INPL-ENSAIA, 2 avenue de la Forêt de Haye, B.P. 172, 54505 Vandoeuvre-lès-Nancy Cedex, France. szappa@cea.fr

Journal of Inorganic Biochemistry
|March 26, 2004
PubMed
Summary

The active form of Pyrococcus abyssi alkaline phosphatase (AP) is the homodimer. Its quaternary structure is influenced by pH, buffer composition, and bound metals, with acidic conditions and specific buffers favoring monomer formation.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Structural Biology

Background:

  • Alkaline phosphatases (APs) are non-specific phosphomonoesterases active under alkaline conditions.
  • APs are typically homodimeric metalloenzymes, but the necessity of this quaternary structure for activity is unclear.
  • Previous studies suggested Pyrococcus abyssi AP exists as both monomer and homodimer.

Purpose of the Study:

  • To determine the actual quaternary structure of P. abyssi AP in solution.
  • To identify factors controlling dimer assembly and dissociation.
  • To elucidate the relationship between quaternary structure and AP activity.

Main Methods:

  • Isolation of monomeric and dimeric forms of P. abyssi AP.
  • Analysis of quaternary structure under varying pH and buffer conditions.

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  • Investigation of metal ion involvement in quaternary structure stability.

    • Main Results:

    • P. abyssi AP quaternary structure is sensitive to pH, with acidic conditions favoring the monomer.
    • Buffer composition influences quaternary state; potassium phosphate allows both monomer and dimer, while Tris-HCl yields only the dimer.
    • Metal removal results in a monomeric form, which can be reactivated with variable efficiency.

    Conclusions:

    • The active form of P. abyssi AP is the homodimer.
    • pH, buffer type, and bound metals are critical for maintaining the homodimeric structure.
    • The monomeric form of P. abyssi AP is not enzymatically active.