Plant Physiol. Drug Metab Dispos
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Plant Physiology 84:826-829 (1987)
© 1987 American Society of Plant Biologists

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Metabolism and Enzymology

Oxidation of Indole-3-Acetic Acid-Amino Acid Conjugates by Horseradish Peroxidase

Ro Dong Park and Chang Kyu Park

Department of Agricultural Chemistry, Chonnam National University, Kwangju, 500, Korea, Department of Agricultural Chemistry, Seoul National University, Suwon, 170, Korea

The stability of 21 amino acid conjugates of indole-3-acetic acid (IAA) toward horseradish peroxidase (HRP) was studied. The IAA conjugates of Arg, Ile, Leu, Tyr, and Val were oxidized readily by peroxidase. Those of Ala, {beta}-Ala, Asp, Cys, Gln, Glu, Gly, and Lys were not degraded and their recovery was above 92% after 1 hour incubation with HRP. A correlation between the stability of IAA conjugates toward peroxidase-catalyzed oxidation and the hydrophobicity of the amino acid moiety conjugated to IAA was demonstrated. Polar amino acid conjugates of IAA are more resistant to HRP-catalyzed oxidation.








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Copyright © 1987 by the American Society of Plant Biologists