The tryptophan synthases from three human pathogens show remarkable structural conservation, but at the same time display local differences in both their catalytic and allosteric sites that may be responsible… Click to show full abstract
The tryptophan synthases from three human pathogens show remarkable structural conservation, but at the same time display local differences in both their catalytic and allosteric sites that may be responsible for the observed differences in catalysis and inhibitor binding. This functional dissimilarity may be exploited in the design of species-specific enzyme inhibitors.
               
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