Abstract:
:An enzyme with fatty acid alpha-oxidation activity (49 nkat mg(-1); substrate: lauric acid) was purified from germinating pea (Pisum sativum) by a five-step procedure to apparent homogeneity. The purified protein was found to be a 230-kD oligomer with two dominant subunits, i.e. a 50-kD subunit with NAD(+) oxidoreductase activity and a 70-kD subunit, homolog to a pathogen-induced oxygenase, which in turn shows significant homology to animal cyclooxygenase. On-line liquid chromatography-electrospray ionization-tandem mass spectrometry revealed rapid alpha-oxidation of palmitic acid incubated at 0 degrees C with the purified alpha-oxidation enzyme, leading to (R)-2-hydroperoxypalmitic acid as the major product together with (R)-2-hydroxypalmitic acid, 1-pentadecanal, and pentadecanoic acid. Inherent peroxidase activity of the 70-kD fraction decreased the amount of the (R)-2-hydroperoxy product rapidly and increased the level of (R)-2-hydroxypalmitic acid. Incubations at room temperature accelerated the decline toward the chain-shortened aldehyde. With the identification of the dual function alpha-dioxygenase-peroxidase (70-kD unit) and the related NAD(+) oxidoreductase (50-kD unit) we provided novel data to rationalize all steps of the classical scheme of alpha-oxidation in plants.
journal_name
Plant Physioljournal_title
Plant physiologyauthors
Saffert A,Hartmann-Schreier J,Schön A,Schreier Pdoi
10.1104/pp.123.4.1545subject
Has Abstractpub_date
2000-08-01 00:00:00pages
1545-52issue
4eissn
0032-0889issn
1532-2548journal_volume
123pub_type
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