Abstract
L-tryptophan dehydrogenase (TDH) is a newly found enzyme involved in the metabolism of indole compounds in plants. The substrate specificity of TDH was investigated in extracts prepared fromPisum sativum andProsopis juliflora. The enzyme activity was detected in both plants either in the oxidative or the reductive direction. The occurrence of other dehydrogenases specific to amino acids was also investigated in the experimental plants:e. g. glutamate dehydrogenase was found to be 1.7 to 5.0 times more active than TDH, whereas no activity for phenylalanine dehydrogenase was detected. In pea plants activity of alanine dehydrogenase could be shown as well. In addition to pea and mesquite TDH was also found in wheat, maize, and tomato seedlings, whereas no activity was detected in brassicaceous plants.
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Abbreviations
- L-trp:
-
L-tryptophan
- TAT:
-
tryptophan amino transferase
- GDH:
-
glutamate dehydrogenase
- TDH:
-
tryptophan dehydrogenase
- IPyA:
-
indol-3-ylpyruvic acid
- L-glu:
-
L-glutamate
- L-ala:
-
L-alanine
- L-phe:
-
L-phenylalanine
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Ebeid, M.M., Dimova, S. & Kutáček, M. Substrate specificity of L-tryptophan dehydrogenase and its distribution in plants. Biol Plant 27, 413–416 (1985). https://doi.org/10.1007/BF02879891
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DOI: https://doi.org/10.1007/BF02879891