Extremophiles

, Volume 12, Issue 1, pp 61–68

The α-l-fucosidase from Sulfolobus solfataricus

  • Beatrice Cobucci-Ponzano
  • Fiorella Conte
  • Mosè Rossi
  • Marco Moracci
Review

DOI: 10.1007/s00792-007-0105-y

Cite this article as:
Cobucci-Ponzano, B., Conte, F., Rossi, M. et al. Extremophiles (2008) 12: 61. doi:10.1007/s00792-007-0105-y
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Abstract

Glycoside hydrolases form hyperthermophilic archaea are interesting model systems for the study of catalysis at high temperatures and, at the moment, their detailed enzymological characterization is the only approach to define their role in vivo. Family 29 of glycoside hydrolases classification groups α-l-fucosidases involved in a variety of biological events in Bacteria and Eukarya. In Archaea the first α-l-fucosidase was identified in Sulfolobus solfataricus as interrupted gene expressed by programmed −1 frameshifting. In this review, we describe the identification of the catalytic residues of the archaeal enzyme, by means of the chemical rescue strategy. The intrinsic stability of the hyperthermophilic enzyme allowed the use of this method, which resulted of general applicability for β and α glycoside hydrolases. In addition, the presence in the active site of the archaeal enzyme of a triad of catalytic residues is a rather uncommon feature among the glycoside hydrolases and suggested that in family 29 slightly different catalytic machineries coexist.

Keywords

Glycoside hydrolaseChemical rescueNucleophileAcid/baseCatalytic triad

Copyright information

© Springer 2007

Authors and Affiliations

  • Beatrice Cobucci-Ponzano
    • 1
  • Fiorella Conte
    • 1
  • Mosè Rossi
    • 1
    • 2
  • Marco Moracci
    • 1
  1. 1.Institute of Protein BiochemistryConsiglio Nazionale delle RicercheNaplesItaly
  2. 2.Dipartimento di Biologia Strutturale e FunzionaleUniversità di Napoli “Federico II”NaplesItaly