Preparation of Cell-free Tryptophanase
نویسندگان
چکیده
منابع مشابه
Properties of Crystalline Tryptophanase.
In 1903 Hopkins and Cole (1) identified tryptophan as the source of indole produced by bacterial cultures. The tryptophan-inducible enzyme responsible for this conversion, which is found most commonly in Escherichia coli, was subsequently named tryptophanase by Happold and Hoyle (2). Wood, Gunsalus, and Umbreit (3) showed that tryptophanase catalyzed the stoichiometric conversion of tryptophan ...
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The biosynthesis of the acid mucopolysaccharide, hyaluronic acid, has been demonstrated in cell-free preparations derived from Group A streptococci (1, 2) and embryonic rat skin (3). In keeping with their function as glycosyl donors in many systems, the uridine nucleotides, uridine 5’-diphosphate-N-acetyln-glucosamine and UDP-n-glucuronic acid, have been shown to be the requisite intermediates ...
متن کاملCrystal structure of tryptophanase.
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...
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ژورنال
عنوان ژورنال: Nature
سال: 1947
ISSN: 0028-0836,1476-4687
DOI: 10.1038/159099a0