نتایج جستجو برای: tryptophan synthase

تعداد نتایج: 99594  

Journal: :Genetics 1968
C Gunsalus C F Gunsalus A M Chakrabarty S Sikes I P Crawford

ave used the tryptophan pathway to develop a gene transfer system via wta:sducing bacteriophage in Pseudomonas putida ( CHAKRAEARTY, GUNSALUS and GUNSALUS 1967). The tryptophan pathway itself has proved interesting in the number and nature of its enzymes, their mode of regulation, and the organization of the genes in the bacterial chromosome. Enzymatic analysis of extracts of prototrophic and a...

Journal: :Journal of bacteriology 1974
W Steinberg

A tryptophanyl-transfer ribonucleic acid (tRNA) synthetase (l-tryptophan: tRNA ligase adenosine monophosphate, EC 6.1.1.2) mutant (trpS1) of Bacillus subtilis is derepressed for enzymes of the tryptophan biosynthetic pathway at temperatures which reduce the growth rate but still allow exponential growth. Derepression of anthranilate synthase in a tryptophan-supplemented medium (50 mug/ml) is ma...

Journal: :Annual review of biochemistry 2001
X Huang H M Holden F M Raushel

The three-dimensional structures of tryptophan synthase, carbamoyl phosphate synthetase, glutamine phosphoribosylpyrophosphate amidotransferase, and asparagine synthetase have revealed the relative locations of multiple active sites within these proteins. In all of these polyfunctional enzymes, a product formed from the catalytic reaction at one active site is a substrate for an enzymatic react...

Journal: :Biochemistry 2005
Annaleise R Howard-Jones Christopher T Walsh

During the biosynthesis of the fused six-ring indolocarbazole scaffolds of rebeccamycin and staurosporine, two molecules of L-tryptophan are processed to a pyrrole-containing five-ring intermediate known as chromopyrrolic acid. We report here the heterologous expression of RebO and RebD from the rebeccamycin biosynthetic pathway in Escherichia coli, and tandem action of these two enzymes to con...

Journal: :FEBS letters 1986
H Tanaka K Tanizawa T Arai K Saito K Soda

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 ...

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