Identification of the catalytic residues of the first family of beta(1-3)glucanosyltransferases identified in fungi

Isabelle Mouyna (1) , Michel Monod (2) , Thierry Fontaine (1) , Bernard Henrissat (3) , Barbara Léchenne (2) , Jean-Paul Latge (1)

1 Aspergillus
2 CHUV - Centre Hospitalier Universitaire Vaudois = Lausanne University Hospital [Lausanne]
3 AFMB - Architecture et fonction des macromolécules biologiques

A new family of glycosylphosphatidylinositol-anchored beta(1-3)glucanosyltransferases (Gelp), recently identified and characterized in the filamentous fungus Aspergillus fumigatus, showed functional similarity to the Gas/Phr/Epd protein families, which are involved in yeast morphogenesis. Sequence comparisons and hydrophobic cluster analysis (HCA) showed that all the Gas/Phr/Epd/Gel proteins belong to a new family of glycosylhydrolases, family 72. We confirmed by site-directed mutagenesis and biochemical analysis that the two conserved glutamate residues (the putative catalytic residues of this family, as determined by HCA) are involved in the active site of this family of glycosylhydrolases.

Domaines: Sciences du Vivant [q-bio]; Mycologie; Biologie cellulaire

Isabelle Mouyna, Michel Monod, Thierry Fontaine, Bernard Henrissat, Barbara Léchenne, et al.. Identification of the catalytic residues of the first family of beta(1-3)glucanosyltransferases identified in fungi. Biochemical Journal, 2000, 347 (3), pp.741-747. ⟨10.1042/bj3470741⟩. ⟨pasteur-01711043⟩