The alpha-L-fucosidase from Sulfolobus solfataricus.
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 alpha-L-fucosidases involved in a variety of biological events in Bacteria and Eukarya. In Archaea the first alpha-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 beta and alpha 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.
Institute of Protein Biochemistry, Consiglio Nazionale delle Ricerche, Via P. Castellino 111, 80131 Naples, Italy. b.cobucciponzano@ibp.cnr.it
Beatrice
B
Cobucci-Ponzano
Fiorella
F
Conte
Mosè
M
Rossi
Marco
M
Moracci
D019843:Archaeal Proteins / Q000096:biosynthesis / Q000737:chemistry*; D001665:Binding Sites / Q000502:physiology; D002384:Catalysis; D018965:Frameshifting, Ribosomal / Q000502:physiology; D006358:Hot Temperature; D008956:Models, Chemical; D048229:Sulfolobus solfataricus / Q000201:enzymology* / Q000235:genetics; D005644:alpha-L-Fucosidase / Q000096:biosynthesis / Q000737:chemistry*
D019843:Archaeal Proteins; D005644:alpha-L-Fucosidase