Structure ofEscherichia colitryptophanase purified from an alkaline-stressed bacterial culture

Abstract

Tryptophanase is a bacterial enzyme involved in the degradation of tryptophan to indole, 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 fromEscherichia coliBL21 strain overexpressing another recombinant protein. Tryptophanase was crystallized in space groupP6522 in the apo form without pyridoxal 5′-phosphate bound in the active site.