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Amino‐terminal sequence of ethylene‐induced bean leaf chitinase reveals similarities to sugar‐binding domains of wheat germ agglutinin
Author(s) -
Lucas John,
Menschen Agnes,
Lottspeich Fritz,
Voegeli Urs,
Boiler Thomas
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80152-6
Subject(s) - chitinase , biology , wheat germ agglutinin , biochemistry , amino acid , agglutinin , chitin , sugar , cell wall , peptide sequence , ethylene , enzyme , botany , lectin , gene , chitosan , catalysis
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.