Open AccessPurification and Characterization of a New Indole Oxygenase from the Leaves of Tecoma stans L
Author(s) -
Satya P. Kunapuli,
C.S. Vaidyanathan
Publication year - 1983
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.71.1.19
Subject(s) - anthranilic acid , indole test , oxygenase , enzyme , chemistry , biochemistry , heme , tryptophan , heme oxygenase , stereochemistry , amino acid
A new indole oxygenase from the leaves of Tecoma stans was isolated and purified to homogenity. The purified enzyme system catalyzes the conversion of indole to anthranilic acid. It is optimally active at pH 5.2 and 30 degrees C. Two moles of oxygen are consumed and one mole of anthranilic acid is formed for every mole of indole oxidized. Dialysis resulted in complete loss of the activity. The inactive enzyme could be reactivated by the addition of concentrated dialysate. The enzyme is not inhibited by copper-specific chelators, non-heme iron chelators or atebrin. It is not a cuproflavoprotein, unlike the other indole oxygenases and oxidases.