Arginine and ornithine oxidation catalyzed by lentil seedling copper-amine oxidase.
The oxidation of L-ornithine and L-arginine catalyzed by lentil (Lens esculenta) seedling copper-amine oxidase has been investigated by polarographic techniques, optical spectroscopy, and capillary electrophoresis. Both L-ornithine and L-arginine were found to be poor substrates for lentil amine oxidase. L-Ornithine was oxidized to glutamate-5-semialdehyde and ammonia, in similar manner as usual substrates. Glutamate-5-semialdehyde spontaneously cyclizes to delta1-pyrroline-5-carboxylic acid. Arginine is oxidized by an unusual mechanism yielding glutamate-5-semialdehyde, ammonia, and urea as reaction products.
Medda
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Department of Sciences Applied to Biosystems, University of Cagliari, Italy.
Padiglia
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Lorrai
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Finazzi Agrò
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A
Floris
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G
D006631:Amine Oxidase (Copper-Containing) / Q000302:isolation & purification / Q000378:metabolism*; D000641:Ammonia / Q000378:metabolism; D001120:Arginine / Q000378:metabolism*; D007887:Fabaceae / Q000201:enzymology*; D007700:Kinetics; D015394:Molecular Structure; D009952:Ornithine / Q000378:metabolism*; D010084:Oxidation-Reduction; D010101:Oxygen Consumption; D010946:Plants, Medicinal; D013053:Spectrophotometry
D000641:Ammonia; D001120:Arginine; D009952:Ornithine; D006631:Amine Oxidase (Copper-Containing)