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Article

A structural view of the dissociation of Escherichia coli tryptophanase.

Acta crystallographica. Section D, Biological crystallography - 1 Dec 2015

Green Keren, Qasim Nasrin, Gdaelvsky Garik, Kogan Anna, Goldgur Yehuda, Parola Abraham H, Lotan Ofra, Almog Orna

Abstract excerpt

Tryptophanase (Trpase) is a pyridoxal 5'-phosphate (PLP)-dependent homotetrameric enzyme which catalyzes the degradation of L-tryptophan. Trpase is also known for its cold lability, which is a reversible loss of activity at low temperature (2°C) that is associated with the dissociation of the tetramer. Escherichia coli Trpase dissociates into dimers, while Proteus vulgaris Trpase dissociates into monomers. As...

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Identifiers

PMID: 26627645
DOI: 10.1107/S139900471501799X

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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