Production of a novel tryptophan analog, β-1-indazole-L-alanine with tryptophan synthase ofEscherichia coli
- 17 February 1986
- journal article
- Published by Wiley in FEBS Letters
- Vol. 196 (2) , 357-360
- https://doi.org/10.1016/0014-5793(86)80279-4
Abstract
The tryptophan synthase α2β2 complex from Escherichia coli has been found to catalyze the β-replacement reaction of L-serine with indazole, an indole analog which has a nitrogen atom at the 2-position (pyrazole ring). The reaction product was isolated and identified as β-indazolealanine by mass spectrometric, elemental and NMR analyses. Careful assignment of 1H- and 13C-signals with several NMR techniques revealed that the β-carbon of the product alanine moiety was bound to the 1-N-position of the indazole ring. This is the first example of the β-replacement reaction catalyzed by tryptophan synthase occurring at any other position than the 3-position of indole analogs.Keywords
This publication has 7 references indexed in Scilit:
- Enzymatic synthesis of Se-substituted L-selenocysteine with tryptophan synthaseFEBS Letters, 1983
- Enzymatic synthesis of S-substituted L-cysteines with tryptophan synthase of Escherichia coli.Agricultural and Biological Chemistry, 1983
- The interaction of Escherichia coli Tryptophanase with Various Amino Acids and Their AnalogsThe Journal of Biochemistry, 1977
- O-phthalaldehyde: fluorogenic detection of primary amines in the picomole range. Comparison with fluorescamine and ninhydrin.Proceedings of the National Academy of Sciences, 1975
- Crystalline α2β2 Complexes of Tryptophan Synthetase of Escherichia coliPublished by Elsevier ,1974
- The enzymatic synthesis of l-tryptophan analoguesAnalytical Biochemistry, 1974
- The Synthesis of an Indazole Analog of DL-TryptophanJournal of the American Chemical Society, 1952