Sc. Hertel et al., PARTIAL-PURIFICATION AND CHARACTERIZATION OF A JASMONIC ACID CONJUGATE CLEAVING AMIDOHYDROLASE FROM THE FUNGUS BOTRYODIPLODIA-THEOBROMAE, FEBS letters, 407(1), 1997, pp. 105-110
A protein preparation from the mycelium of the tropical pathogenic fun
gus Botryodiplodia theobromae revealed a novel peptidase activity. Thi
s enzyme was capable of cleaving conjugates of jasmonic acid with alph
a-amino acids, The protein was enriched 108-fold by gel filtration, io
n 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 alpha-amino acids with (S)-configuration. (C) 1997 Federation
of European Biochemical Societies.