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Article

Contribution of Lys276 to the conformational flexibility of the active site of glutamate decarboxylase from Escherichia coli.

European journal of biochemistry - 1 Oct 2002

Tramonti Angela, John Robert A, Bossa Francesco, De Biase Daniela

Abstract excerpt

Glutamate decarboxylase is a pyridoxal 5'-phosphate-dependent enzyme responsible for the irreversible alpha-decarboxylation of glutamate to yield 4-aminobutyrate. In Escherichia coli, as well as in other pathogenic and nonpathogenic enteric bacteria, this enzyme is a structural component of the glutamate-based acid resistance system responsible for cell survival in extremely acidic conditions (pH < 2.5). The...

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Identifiers

PMID: 12383249
DOI: 10.1046/j.1432-1033.2002.03149.x

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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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