Biochemical Journal

Research article

Identification of the catalytic residues of the first family of β(1–3)glucanosyltransferases identified in fungi

Isabelle MOUYNA, Michel MONOD, Thierry FONTAINE, Bernard HENRISSAT, Barbara LÉCHENNE, Jean-Paul LATGÉ

Abstract

A new family of glycosylphosphatidylinositol-anchored β(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.

  • Aspergillus fumigatus
  • GEL protein family
  • GPI-anchored protein