نتایج جستجو برای: tryptophanase
تعداد نتایج: 360 فیلتر نتایج به سال:
In pure form indole, when subjected to pyrolysis mass spectrometry @MS), gave a pattern of peaks at m/z 117, 90,89 and a murmur at 63. Significant differences in the magnitudes of these peaks were observed between strains of Escherichia coli which were grown on nutrient agar and which differed solely in whether a transposon had been inserted into the tryptophanase gene or elsewhere within the g...
The X-ray structure of tryptophanase (Tnase) reveals the interactions responsible for binding of the pyridoxal 5'-phosphate (PLP) and atomic details of the K+ binding site essential for catalysis. The structure of holo Tnase from Proteus vulgaris (space group P2(1)2(1)2(1) with a = 115.0 A, b = 118.2 A, c = 153.7 A) has been determined at 2.1 A resolution by molecular replacement using tyrosine...
The tutB gene, which lies just downstream of tpl, has been cloned from Erwinia herbicola, and its product was analyzed. Despite its high sequence similarity to tryptophan transporters, TutB was found to be a tyrosine-specific transporter. Tryptophan acted as a competitive inhibitor of tyrosine transport. Unlike the tryptophanase operon, the tpl and tutB genes do not constitute an operon.
نمودار تعداد نتایج جستجو در هر سال
با کلیک روی نمودار نتایج را به سال انتشار فیلتر کنید