Amino‐terminal sequence of ethylene‐induced bean leaf chitinase reveals similarities to sugar‐binding domains of wheat germ agglutinin

Abstract

Chitinase has been reported for many plant species. A role in plant defense has been suggested for plant chitinases, due to their ability to degrade fungal cell wall chitin. Increased levels of chitinase are induced in bean plants by the plant hormone ethylene [(1983) Planta 157, 22‐31]. The amino acid sequence of positions 1–30 of ethylene‐induced bean leaf chitinase was determined and found to possess considerable sequence homology to wheat germ agglutinin and hevein. The implication of a lectin‐related structure for the enzymatic specificity of chitinase is discussed.