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Partial purification and characterization of a jasmonic acid conjugate cleaving amidohydrolase from the fungus Botryodiplodia theobromae
Author(s) -
Hertel Silvia C,
Knöfel Hans-Dieter,
Kramell Robert,
Miersch Otto
Publication year - 1997
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/s0014-5793(97)00307-4
Subject(s) - conjugate , jasmonic acid , fungus , amidohydrolase , chemistry , botany , biology , biochemistry , hydrolysis , mathematical analysis , mathematics , gene
A protein preparation from the mycelium of the tropical pathogenic fungus Botryodiplodia theobromae revealed a novel peptidase activity. This enzyme was capable of cleaving conjugates of jasmonic acid with α‐amino acids. The protein was enriched 108‐fold by gel filtration, ion exchange and hydrophobic interaction chromatography. The enzyme was found to be a glycoprotein with a molecular mass of about 107 kDa. The amidohydrolase seems to be very specific with regard to (−)‐jasmonic acid and α‐amino acids with ( S )‐configuration.