Skip to main content
NCBI home page
Plant Physiology logoLink to Plant Physiology
. 1983 Jan;71(1):19–23. doi: 10.1104/pp.71.1.19

Purification and Characterization of a New Indole Oxygenase from the Leaves of Tecoma stans L

Satya P Kunapuli 1,1, Chelarkara S Vaidyanathan 1
PMCID: PMC1065978  PMID: 16662784

Abstract

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°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.

Full text

PDF
19

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Andrews P. The gel-filtration behaviour of proteins related to their molecular weights over a wide range. Biochem J. 1965 Sep;96(3):595–606. doi: 10.1042/bj0960595. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Chauhan Y. S., Rathore V. S., Garg G. K., Bhargava A. Detection of an indole oxidizing system in maize leaves. Biochem Biophys Res Commun. 1978 Aug 29;83(4):1237–1245. doi: 10.1016/0006-291x(78)91354-2. [DOI] [PubMed] [Google Scholar]
  3. DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
  4. Devereux Woods D. Indole formation by Bacterium coli: The action of washed suspensions of Bacterium coli on indole derivatives. Biochem J. 1935 Mar;29(3):649–655. doi: 10.1042/bj0290649. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Fujioka M., Wada H. The bacterial oxidation of indole. Biochim Biophys Acta. 1968 Apr 16;158(1):70–78. doi: 10.1016/0304-4165(68)90073-1. [DOI] [PubMed] [Google Scholar]
  6. Happold F. C., Hoyle L. The coli-tryptophan-indole reaction: Enzyme preparations and their action on tryptophan and some indole derivatives. Biochem J. 1935 Aug;29(8):1918–1926. doi: 10.1042/bj0291918. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. KNOX W. E., MEHLER A. H. The conversion of tryptophan to kynurenine in liver. I. The coupled tryptophan peroxidase-oxidase system forming formylkynurenine. J Biol Chem. 1950 Nov;187(1):419–430. [PubMed] [Google Scholar]
  8. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  9. NAIR P. M., VAIDYANATHAN C. S. AN INDOLE OXIDASE ISOLATED FROM THE LEAVES OF TECOMA STANS. Biochim Biophys Acta. 1964 Mar 9;81:496–506. doi: 10.1016/0926-6569(64)90134-8. [DOI] [PubMed] [Google Scholar]
  10. SPRINCE H. Biochemical aspects of indole metabolism in normal and schizophrenic subjects. Ann N Y Acad Sci. 1962 Jan 13;96:399–418. doi: 10.1111/j.1749-6632.1962.tb50134.x. [DOI] [PubMed] [Google Scholar]
  11. Stanley A. R., Spray R. S. The Photoelectric Determination of Indole in Bacterial Cultures. J Bacteriol. 1941 Feb;41(2):251–257. doi: 10.1128/jb.41.2.251-257.1941. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. TANAKA T., KNOX W. E. The nature and mechanism of the tryptophan pyrrolase (peroxidase-oxidase) reaction of Pseudomonas and of rat liver. J Biol Chem. 1959 May;234(5):1162–1170. [PubMed] [Google Scholar]
  13. Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]

Articles from Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES