Bacterial nonspecific acid phosphohydrolases: Physiology, evolution and use as tools in microbial biotechnology

G. M. Rossolini, S. Schippa, M. L. Riccio, F. Berlutti, L. E. Macaskie, M. C. Thaller

Research output: Contribution to journalArticlepeer-review


Bacterial nonspecific acid phosphohydrolases (NSAPs) are secreted enzymes, produced as soluble periplasmic proteins or as membrane-bound lipoproteins, that are usually able to dephosphorylate a broad array of structurally unrelated substrates and exhibit optimal catalytic activity at acidic to neutral pH values. Bacterial NSAPs are monomeric or oligomeric proteins containing polypeptide components with an M(r) of 25-30 kDa. On the basis of amino acid sequence relatedness, three different molecular families of NSAPs can be distinguished, indicated as molecular class A, B and C, respectively. Members of each class share some common biophysical and functional features, but may also exhibit functional differences. NSAPs have been detected in several microbial taxa, and enzymes of different classes can be produced by the same bacterial species. Structural and phyletic relationships exist among the various bacterial NSAPs and some other bacterial and eucaryotic phosphohydrolases. Current knowledge on bacterial NSAPs is reviewed, together with analytical tools that may be useful for their characterization. An overview is also presented concerning the use of bacterial NSAPs in biotechnology.

Original languageEnglish
Pages (from-to)833-850
Number of pages18
JournalCellular and Molecular Life Sciences
Issue number8
Publication statusPublished - 1998


  • Acid phosphohydrolases
  • Bacteria
  • Genetics
  • Microbial biotechnology
  • Molecular evolution
  • Physiology

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Cell Biology

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