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Structure of Escherichia coli tryptophanase 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 from Escherichia coli BL21 strain overexpressing another recombinant protein. Tryptophanase was crystallized in space group P6522 in the apo form without pyridoxal 5'-phosphate bound in the active site.

SUBMITTER: Rety S

PROVIDER: S-EPMC4631586 | biostudies-literature | 2015 Nov

REPOSITORIES: biostudies-literature

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

Rety Stephane S Deschamps Patrick P Leulliot Nicolas N

Acta crystallographica. Section F, Structural biology communications 20151023 Pt 11

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 from Escherichia coli BL21 strain overexpressing another recombinant protein. Tryptophanase was crystallized in space group P6522 in the apo form without pyridoxal 5'-phosphate bound in the active site. ...[more]

PMID: 26527264

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