Oxidation of indole-3-acetic acid to oxindole-3-acetic acid by an enzyme preparation from Zea mays.
Indole-3-acetic acid is oxidized to oxindole-3-acetic acid by Zea mays tissue extracts.  Shoot, root, and endosperm tissues have enzyme activities of 1 to 10 picomoles per hour per milligram protein.  The enzyme is heat labile, is soluble, and requires oxygen for activity.  Cofactors of mixed function oxygenase, peroxidase, and intermolecular dioxygenase are not stimulatory to enzymic activity.  A heat-stable, detergent-extractable component from corn enhances enzyme activity 6- to 10-fold.  This is the first demonstration of the in vitro enzymic oxidation of indole-3-acetic acid to oxindole-3-acetic acid in higher plants.
Reinecke
D M
DM
Department of Botany and Plant Pathology, Michigan State University, East Lansing 48824, USA.
Bandurski
R S
RS
D007210:Indoleacetic Acids / Q000378:metabolism*; D010084:Oxidation-Reduction; D000078183:Oxindoles; D010937:Plant Growth Regulators / Q000378:metabolism*; D010940:Plant Proteins / Q000302:isolation & purification / Q000378:metabolism; D018517:Plant Roots / Q000201:enzymology / Q000378:metabolism; D018520:Plant Shoots / Q000201:enzymology / Q000378:metabolism; D012639:Seeds / Q000201:enzymology / Q000378:metabolism; D003313:Zea mays / Q000201:enzymology* / Q000378:metabolism*
D007210:Indoleacetic Acids; D000078183:Oxindoles; D010937:Plant Growth Regulators; D010940:Plant Proteins; C003013:2-oxindole-3-acetic acid; C030737:indoleacetic acid