Enzymatic Synthesis ofs-Substitutedl-Cysteines with Tryptophan Synthase ofEscherichia coli
نویسندگان
چکیده
منابع مشابه
A Neurospora mutant deficient in the enzymatic synthesis of tryptophan.
Until recently there has been no demonstrated case in Neurospora in which the loss of activity of an essential enzyme could be attributed to gene mutation. It has been assumed from indirect evidence1 that gene mutations do cause such losses and thereby result in “blocks” of essential biochemical reactions. The products of the “blocked” reactions thus become essential growth substances for the m...
متن کاملEnzymatic studies with a series of tryptophan auxotrophs of Escherichia coli.
Direct support for the participation in tivo of the above reactions in tryptophan synthesis would be provided by the demonstration that the enzymes catalyzing these reactions are lacking in specific tryptophan auxotrophs. The purpose of the present study was to obtsin evidence of this type and, in addition, to attempt to correlate the nutritional, enzymatic, and metabolite accumulation behavior...
متن کاملProduction of a novel tryptophan analog, beta-1-indazole-L-alanine with tryptophan synthase of Escherichia coli.
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 ...
متن کاملSynthesis of β-Branched Tryptophan Analogues Using an Engineered Subunit of Tryptophan Synthase.
We report that l-threonine may substitute for l-serine in the β-substitution reaction of an engineered subunit of tryptophan synthase from Pyrococcus furiosus, yielding (2S,3S)-β-methyltryptophan (β-MeTrp) in a single step. The trace activity of the wild-type β-subunit on this substrate was enhanced more than 1000-fold by directed evolution. Structural and spectroscopic data indicate that this ...
متن کاملImmunochemical and enzymatic comparisons of the tryptophan synthase alpha subunits from five species of Enterobacteriaceae.
The reactive surface structures of alpha subunits of tryptophan synthase from Escherichia coli, Shigella dysenteriae, Salmonella typhimurium, Aerobacter aerogenes, and Serratia marcescens were compared by measuring (i) their reactivities in micro-complement-fixation assays with antibodies directed specifically to E. coli wild-type alpha subunit, (ii) their reactivities in enzyme neutralization ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1983
ISSN: 0002-1369
DOI: 10.1080/00021369.1983.10866047