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Mutant enzyme unstability

All three laboratories [187,188,215] reported evidence that the trpS mutant strains were defective in tryptophanyl-tRNA synthetase activity by in vitro tests. Doolittle and Yanofsky [187] found little or no enzyme activity in extracts of various mutant strains, and some displayed distinct temperature sensitivities. Substrate protected some of the defective enzymes from inactivation. Two of the mutant enzyme extracts were examined for K , values which were found to be ten times as high as that of wild type [187]. Ito et al. [188] studied one trpS mutant in detail and determined that the tryptophanyl-tRNA synthetase was very unstable but could be stabilized by tryptophan in the presence of ATP. [Pg.432]

For further investigation, the triple mutant R33E/E60R/T81P was constructed. Surprisingly, the triple mutation was found to produce a fairly thermally unstable enzyme. The half-life (U/2) value of the triple mutant was determined as 58°C. [Pg.211]

See other pages where Mutant enzyme unstability is mentioned: [Pg.151]    [Pg.602]    [Pg.607]    [Pg.250]    [Pg.173]    [Pg.13]    [Pg.27]    [Pg.121]    [Pg.324]    [Pg.40]    [Pg.110]    [Pg.116]    [Pg.117]    [Pg.121]    [Pg.237]    [Pg.210]    [Pg.55]    [Pg.421]    [Pg.433]    [Pg.145]    [Pg.172]    [Pg.184]    [Pg.258]    [Pg.1757]    [Pg.626]    [Pg.132]    [Pg.223]    [Pg.742]    [Pg.242]    [Pg.55]    [Pg.55]    [Pg.156]    [Pg.9]    [Pg.61]    [Pg.118]    [Pg.432]    [Pg.55]    [Pg.223]    [Pg.115]    [Pg.29]    [Pg.15]    [Pg.316]    [Pg.434]    [Pg.388]    [Pg.699]    [Pg.71]    [Pg.81]    [Pg.361]    [Pg.21]   
See also in sourсe #XX -- [ Pg.195 , Pg.196 , Pg.197 , Pg.198 , Pg.199 , Pg.200 , Pg.201 ]



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Unstability

Unstable

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