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. 1993 Aug;102(4):1319–1324. doi: 10.1104/pp.102.4.1319

An in Vitro System of Indole-3-Acetic Acid Formation from Tryptophan in Maize (Zea mays) Coleoptile Extracts.

T Koshiba 1, H Matsuyama 1
PMCID: PMC158922  PMID: 12231908

Abstract

The formation of a product from tryptophan that had the same retention time as that of authentic indole-3-acetic acid (IAA) on high performance liquid chromatography was detected in crude extracts of maize (Zea mays) coleoptiles. The product was identified as IAA by mass spectrometry. The IAA-forming activity was co-purified with an indole-3-acetaldehyde (IAAld) oxidase activity by chromatography on hydrophobic and gel filtration (GPC-100) columns. During purification, the IAA-forming activity, rather than that of IAAld oxidase, decreased; but when hemoprotein obtained from the same tissue was added, activity recovered to the same level as that of IAAld oxidase. The promotive activity of the hemoprotein was confirmed by the result that the activity coincided with amounts of the hemoprotein after GPC-100 column chromatography. The hemoprotein was characterized and identified as a cytosolic ascorbate peroxidase (T. Koshiba [1993] Plant Cell Physiol [in press]). The reaction of the IAA-forming activity was apparently one step from tryptophan. The activity was inhibited by 2-mercaptoethanol. The optimum temperature for the IAA-forming system as well as for the IAAld oxidase was 50 to 60[deg]C, and the acitivity at 30[deg]C was one-third to one-half of that at 60[deg]C. The system did not discriminate the L- and D-enantiomers of tryptophan.

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Selected References

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  1. Acosta M., Casas J. L., Arnao M. B., Sabater F. 1-Aminocyclopropane-1-carboxylic acid as a substrate of peroxidase: conditions for oxygen consumption, hydroperoxide generation and ethylene production. Biochim Biophys Acta. 1991 Apr 29;1077(3):273–280. doi: 10.1016/0167-4838(91)90540-g. [DOI] [PubMed] [Google Scholar]
  2. Baldi B. G., Maher B. R., Slovin J. P., Cohen J. D. Stable Isotope Labeling, in Vivo, of d- and l-Tryptophan Pools in Lemna gibba and the Low Incorporation of Label into Indole-3-Acetic Acid. Plant Physiol. 1991 Apr;95(4):1203–1208. doi: 10.1104/pp.95.4.1203. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bialek K., Michalczuk L., Cohen J. D. Auxin Biosynthesis during Seed Germination in Phaseolus vulgaris. Plant Physiol. 1992 Sep;100(1):509–517. doi: 10.1104/pp.100.1.509. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bower P. J., Brown H. M., Purves W. K. Cucumber seedling indoleacetaldehyde oxidase. Plant Physiol. 1978 Jan;61(1):107–110. doi: 10.1104/pp.61.1.107. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Felsted R. L., Chu A. E., Chaykin S. Purification and properties of the aldehyde oxidases from hog and rabbit livers. J Biol Chem. 1973 Apr 10;248(7):2580–2587. [PubMed] [Google Scholar]
  6. Hall W. W., Krenitsky T. A. Aldehyde oxidase from rabbit liver: specificity toward purines and their analogs. Arch Biochem Biophys. 1986 Nov 15;251(1):36–46. doi: 10.1016/0003-9861(86)90048-2. [DOI] [PubMed] [Google Scholar]
  7. Lantican B. P., Muir R. M. Isolation and properties of the enzyme system forming indoleacetic Acid. Plant Physiol. 1967 Aug;42(8):1158–1160. doi: 10.1104/pp.42.8.1158. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Percival F. W., Purves W. K. Multiple amine oxidases in cucumber seedlings. Plant Physiol. 1974 Oct;54(4):601–607. doi: 10.1104/pp.54.4.601. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Phelps R. H., Sequeira L. Synthesis of Indoleacetic Acid via Tryptamine by a Cell-free System from Tobacco Terminal Buds. Plant Physiol. 1967 Aug;42(8):1161–1163. doi: 10.1104/pp.42.8.1161. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Purves W. K., Brown H. M. Indoleacetaldehyde in cucumber seedlings. Plant Physiol. 1978 Jan;61(1):104–106. doi: 10.1104/pp.61.1.104. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Riddle V. M., Mazelis M. Conversion of Tryptophan to Indoleacetamide and Further Conversion to Indoleacetic Acid by Plant Preparations. Plant Physiol. 1965 May;40(3):481–484. doi: 10.1104/pp.40.3.481. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Sherwin J. E., Purves W. K. Tryptophan as an auxin precursor in cucumber seedlings. Plant Physiol. 1969 Sep;44(9):1303–1309. doi: 10.1104/pp.44.9.1303. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Yoshihara S., Tatsumi K. Guinea pig liver aldehyde oxidase as a sulfoxide reductase: its purification and characterization. Arch Biochem Biophys. 1985 Oct;242(1):213–224. doi: 10.1016/0003-9861(85)90495-3. [DOI] [PubMed] [Google Scholar]
  14. Yoshihara S., Tatsumi K. Kinetic and inhibition studies on reduction of diphenyl sulfoxide by guinea pig liver aldehyde oxidase. Arch Biochem Biophys. 1986 Aug 15;249(1):8–14. doi: 10.1016/0003-9861(86)90554-0. [DOI] [PubMed] [Google Scholar]

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