Partial purification and characterization of a jasmonic acid conjugate cleaving amidohydrolase from the fungus Botryodiplodia theobromae.
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 alpha-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 alpha-amino acids with (S)-configuration.
Hertel
S C
SC
Institute of Plant Biochemistry, Halle/Saale, Germany.
Knöfel
H D
HD
Kramell
R
R
Miersch
O
O
D000581:Amidohydrolases / Q000302:isolation & purification / Q000378:metabolism*; D000596:Amino Acids / Q000737:chemistry / Q000378:metabolism*; D002957:Citrus / Q000382:microbiology; D003517:Cyclopentanes / Q000737:chemistry / Q000378:metabolism*; D003904:Mitosporic Fungi / Q000201:enzymology*; D054883:Oxylipins; D010937:Plant Growth Regulators / Q000737:chemistry / Q000378:metabolism*; D013379:Substrate Specificity
D000596:Amino Acids; D003517:Cyclopentanes; D054883:Oxylipins; D010937:Plant Growth Regulators; C011006:jasmonic acid; D000581:Amidohydrolases