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Structure of Escherichia coli tryptophanase purified from an alkaline‐stressed bacterial culture
Author(s) -
Rety Stephane,
Deschamps Patrick,
Leulliot Nicolas
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15017549
Subject(s) - tryptophanase , escherichia coli , biochemistry , pyridoxal phosphate , indole test , tryptophan , enzyme , pyridoxal , chemistry , tryptophan synthase , biology , cofactor , amino acid , gene
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 P 6 5 22 in the apo form without pyridoxal 5′‐phosphate bound in the active site.