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Structure of Escherichia coli tryptophanase purified from an alkaline-stressed bacterial culture.

Stephane Rety, Patrick Deschamps, and Nicolas Leulliot (2015)

Acta Crystallogr F Struct Biol Commun, 71(Pt 11):1378-83.

Tryptophanase is a bacterial enzyme involved in the degradation of tryptophan toindole, pyruvate and ammonia, which are compounds that are essential for bacterial survival. Tryptophanase is often overexpressed in stressed cultures. Large amounts of endogenous tryptophanase were purified from Escherichia coli BL21 strain overexpressing another recombinant protein. Tryptophanase was crystallized in space group P6522 in the apo form without pyridoxal 5'-phosphatebound in the active site.

 
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