Properties of Crystalline 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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2 This is shown for C the unit circle by an example of Lusin and Privalov in Priwalow, I. I., Randeigenschaften analytischer Funktionen (Berlin, 1956), pp. 229-230; and for general C by Bagemihl, F., and W. Seidel, "Regular functions with prescribed measurable boundary values almost everywhere," these PROCEEDINGS, 41, 740-743 (1955), Theorem 2. 8 See Golusin, G. M., Geometrische Funktionentheor...
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15 صفحه اولCrystal 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: Journal of Biological Chemistry
سال: 1965
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)97562-9