Biochemical studies of the alpha-oxidation in pea (Pisum sativum)
Project management at the University of Würzburg:
An enzyme with fatty acid alpha-oxidation activity was purified from germinating pea (Pisum sativum) to apparent electrophoretic homogeneity. The purified protein was found to be a 230 kD oligomer with to subunits, i.e. a 50 kD subunit with NAD oxidoreductase activity and a 70 kD subunit, homolog to a pathogen-induced oxygenase (PIOX). LC-ESI-MS/MS analysis revealed rapid alpha-oxidation of palmitic acid incubated with the 70 kD subunit, leading to (R)-2-hydroperoxypalmitic acid as the major product together with (R)-2-hydroxypalmitic acid, 1-pentadecanal, and pentadecanoic acid. The kinteic data af a number of substrates were determined.
Projekt period: from 01.1998 to 12.2000
DFG ,Granting date: 01.10.1997