Substrate-protein interaction in tryptophanase from Bacillus alvei. Kinetic and spectral evaluations.
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چکیده
منابع مشابه
Catalytic studies on tryptophanase from Bacillus alvei.
Tryptophanase from Bacillus alvei exhibited the expected spectrum of pyridoxal-5'-phosphate-dependent reactions. It exhibited l-serine dehydratase, S-alkyl-cysteine lyase, and cysteine desulfhydrase activities, as well as the classic tryptophanase reactions (all beta elimination reactions). It also acted as a tryptophan synthetase (beta replacement reactions) using indole plus l-serine or l-cys...
متن کاملPhysiological role of tryptophanase in control of tryptophan biosynthesis in Bacillus alvei.
Hoch, J. A. (University of Illinois, Urbana), and R. D. DeMoss. Physiological role of tryptophanase in control of tryptophan biosynthesis in Bacillus alvei. J. Bacteriol. 91:667-672. 1966.-Indole excretion occurred early in the exponential growth phase, and derived mainly from biosynthetic intermediates of tryptophan. Tryptophan cleavage by tryptophanase contributed about 1.5% of the indole exc...
متن کاملNonmotile Variants of Bacillus alvei.
The ability of Bacillus alvei to form migrating colonies upon the surfaces of solid media free from excessive moisture was reported previously by Smith and Clark (1938).2 A similar property has been noted by Roberts (1935) for Bacillus rotans. Recently Shinn (1938), in a cinematographic study of colony motility of B. alvei, remarked that it was surprising that such motility had been so long ove...
متن کاملGeneration of leukotrienes from human granulocytes by alveolysin from Bacillus alvei.
We investigated the effect of alveolysin on human granulocytes. Alveolysin is an exoprotein produced by Bacillus alvei and belongs to the group of sulfhydryl-activated cytolysins. Other members of this group are streptolysin O and theta-toxin from Clostridium perfringens. It is demonstrated that alveolysin leads to leukotriene generation from human granulocytes, which exert chemotactic (leukotr...
متن کاملInteraction of structural modules in substrate binding by the ribozyme from Bacillus subtilis RNase P.
The ribozyme from bacterial ribonuclease P recognizes two structural modules in a tRNA substrate: the T stem-loop and the acceptor stem. These two modules are connected through a helical linker. The T stem-loop binds at a surface confined in a folding domain away from the active site. Substrates for the Bacillus subtilis RNase P RNA were previously selected in vitro that are shown to bind compa...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1975
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)40854-5