Abstract
Two forms of L-tryptophan aminotransferases (L-TAT-1 and L-TAT-2) and one D-tryptophan aminotransferase (D-TAT) were separated from maize coleoptiles by using L- and D-tryptophan as amino group donors. The enzymes were partially purlfied by hydrophobic and gel filtration column chromatographies. L-TAT-1 and L-TAT-2 had similar properties, showing optimum pH at 8–9 and a high optimum temperature of 50–60 C for catalytic activity. As the amino group acceptor for these two enzymes, α-keto glutaric acid was more effective than pyruvic, oxaloacetic and glyoxylic acids. The molecular masses of L-TAT-1 and L-TAT-2 estimated by gel filtration were approximately 80 kDa and 45 kDa, respectively. D-TAT had an optimum pH similar to those of L-TATs, but the optimum temperature was conslderably lower (30 C). Pyruvic acid was an effective amino group acceptor for D-TAT, whereas oxaloacetic and α-keto glutaric acids were not. D-Cycloserine completely inhibited the activity. The molecular mass of D-TAT was approximately 55 kDa. These three TATs required pyridoxal-5-phosphate for their catalytic activities.
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Abbreviations
- AT:
-
aminotransferase
- HPLG:
-
high performance liquid chromatography
- α:
-
KG
- α:
-
keto glutaric acid
- PLP:
-
pyridoxal-5-phosphate
- TAT:
-
tryptophan aminotransferase
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Koshiba, T., Mito, N. & Miyakado, M. L- and D-tryptophan aminotransferases from maize coleoptiles. J. Plant Res. 106, 25–29 (1993). https://doi.org/10.1007/BF02344369
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DOI: https://doi.org/10.1007/BF02344369