1.
FEBS Lett
; 196(2): 357-60, 1986 Feb 17.
Article
in English
| MEDLINE
| ID: mdl-3512296
ABSTRACT
The tryptophan synthase alpha 2 beta 2 complex from Escherichia coli has been found to catalyze the beta-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 beta-indazolealanine by mass spectrometric, elemental and NMR analyses. Careful assignment of 1H- and 13C-signals with several NMR techniques revealed that the beta-carbon of the product alanine moiety was bound to the 1-N-position of the indazole ring. This is the first example of the beta-replacement reaction catalyzed by tryptophan synthase occurring at any other position than the 3-position of indole analogs.
Subject(s)
Escherichia coli/enzymology , Indazoles/biosynthesis , Pyrazoles/biosynthesis , Tryptophan Synthase/metabolism , Tryptophan/analogs & derivatives , Chemical Phenomena , Chemistry , Magnetic Resonance Spectroscopy , Tryptophan/biosynthesis
2.
Arch Int Pharmacodyn Ther
; 187(1): 155-62, 1970 Sep.
Article
in English
| MEDLINE
| ID: mdl-5480135