PARTIAL-PURIFICATION AND CHARACTERIZATION OF A JASMONIC ACID CONJUGATE CLEAVING AMIDOHYDROLASE FROM THE FUNGUS BOTRYODIPLODIA-THEOBROMAE

Authors
HERTEL SC KNOFEL HD KRAMELL R MIERSCH O
Citation
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
Citations number
32
Categorie Soggetti
Biophysics,Biology
Journal title
FEBS letters → ACNP
ISSN journal
00145793
Volume
407
Issue
1
Year of publication
1997
Pages
105 - 110
Database
ISI
SICI code
0014-5793(1997)407:1<105:PACOAJ>2.0.ZU;2-5
Abstract
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.