Plant Physiol. Illumina
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Plant Physiology 84:541-544 (1987)
© 1987 American Society of Plant Biologists

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Metabolism and Enzymology

Indole-3-Ethanol Oxidase in Phycomyces blakesleeanus Bgff

Characterization of the Enzyme

Peter Schramm, Thomas Rausch and Willy Hilgenberg

Botanisches Institut der Johann Wolfgang Goethe Universität, Siesmayerstrasse 70, D-6000-Frankfurt, Federal Republic of Germany

Indole-3-ethanol oxidase (IEt oxidase) from Phycomyces blakesleeanus Bgff.(P.b.) is a 56 kD polypeptide as determined by gel filtration. The reaction products are indole-3-acetaldehyde (IAAld) and, possibly, H2O2. Enzyme activity (33-45% ammonium sulfate fraction) shows a broad pH optimum and simple Michaelis-Menten kinetics (Km 7 micromolar, Hill coefficient 0.95). Flavin adenine dinucleotide increases enzyme activity particularly under anaerobic conditions. Iodoacetate and HgCl2 drastically inhibit the enzyme. With IAAld, product inhibition is observed at micromolar concentrations. IAA and some other acidic substituted indoles reduce enzyme activity but only at higher concentrations.








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Copyright © 1987 by the American Society of Plant Biologists