Indole-3-acetic Acid Synthesis in Tumorous and Nontumorous Species of Nicotiana

Синтез индол-3-уксусной кислоты у опухолевых и неопухолевых видов Nicotiana
Shih‐Tung Liu, Charles D. Katz, C.A. Knight
1978-05-01

Nicotiana speciesindole-3-acetic acid synthesisindolepyruvic acid pathwaytryptophan aminotransferasetumorous and nontumorous plants
The synthesis of indole-3-acetic acid (IAA) in the enzyme extracts of Nicotiana glauca, Nicotiana langsdorffii, their F1 hybrid, their amphidiploid hybrid, and the nontumorous mutant of the hybrid was investigated. Tryptamine, a possible precursor of IAA biosynthesis in Nicotiana tabacum, was not found in the callus tissue of N. glauca, N. langsdorffii, and their F1 hybrid.In petiole slices, the synthesis of IAA progressively increased during 5 hours of incubation in [(14)C]tryptophan. The rate of synthesis was about equal in the hybrid and N. langsdorffii but lower in N. glauca on either a cell or fresh weight basis. It was also found that tryptophan was about 25 times more efficient than tryptamine in promoting synthesis of IAA in petiole slices.It was found that indoleacetaldehyde oxidase, indoleacetaldehyde reductase, and tryptophan aminotransferase activities were present in all of the species examined; however, tryptophan decarboxylase activity was not found. The tryptophan aminotransferase activity in N. glauca, N. langsdorffii, and the nontumorous mutant required alpha-ketoglutaric acid and pyridoxal 5-phosphate whereas the addition of pyridoxal 5-phosphate seemed not to increase the enzyme activity in tumor plants.The tryptophan aminotransferase in the amphidiploid hybrid was partially purified by acetone precipitation. The enzyme activity had a temperature optimum at 49 C and a pH optimum at 8.9. It is suggested that there is an indolepyruvic acid pathway in the synthesis of IAA in the Nicotiana species examined.
1
IAA synthesis from radiolabeled tryptophan increased progressively during five hours of petiole-slice incubation; rates were similar in the hybrid and N. langsdorffii but lower in N. glauca.
2
Indoleacetaldehyde oxidase, indoleacetaldehyde reductase, and tryptophan aminotransferase activities occurred in all examined species, whereas tryptophan decarboxylase activity was undetectable.
3
The findings support an indolepyruvic acid pathway for IAA biosynthesis in the investigated Nicotiana species; aminotransferase activity in the amphidiploid hybrid had optima at 49°C and pH 8.9.
4
Tryptamine was absent from callus tissues of Nicotiana glauca, N. langsdorffii, and their F1 hybrid, arguing against its essential role as an IAA precursor.
5
Tryptophan was approximately 25 times more efficient than tryptamine at promoting IAA synthesis in petiole slices.

Indole-3-acetic acid synthesis in enzyme extracts and petiole tissues of tumorous and nontumorous Nicotiana species and hybrids

IAA biosynthetic pathways, precursor utilization, and associated enzyme activities across Nicotiana species, hybrids, and a nontumorous mutant

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1978-05-01
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Shih‐Tung Liu
Charles D. Katz
C.A. Knight
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