Structural highlights
Function
C3SLI7_ECOLX
Publication Abstract from PubMed
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.
Structure of Escherichia coli tryptophanase purified from an alkaline-stressed bacterial culture.,Rety S, Deschamps P, Leulliot N Acta Crystallogr F Struct Biol Commun. 2015 Nov 1;71(Pt 11):1378-83. doi:, 10.1107/S2053230X15017549. Epub 2015 Oct 23. PMID:26527264[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rety S, Deschamps P, Leulliot N. Structure of Escherichia coli tryptophanase purified from an alkaline-stressed bacterial culture. Acta Crystallogr F Struct Biol Commun. 2015 Nov 1;71(Pt 11):1378-83. doi:, 10.1107/S2053230X15017549. Epub 2015 Oct 23. PMID:26527264 doi:http://dx.doi.org/10.1107/S2053230X15017549