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

Glutamate decarboxylase is a pyridoxal 5′‐phosphate‐dependent enzyme responsible for the irreversible α‐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 glutamat...

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Veröffentlicht in:	European journal of biochemistry 2002-10, Vol.269 (20), p.4913-4920
Hauptverfasser:	Tramonti, Angela, John, Robert A., Bossa, Francesco, De Biase, Daniela
Format:	Artikel
Sprache:	eng
Schlagworte:	active‐site lysine Binding Sites Circular Dichroism Escherichia coli Escherichia coli Proteins - chemistry Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism glutamate decarboxylase Glutamate Decarboxylase - chemistry Glutamate Decarboxylase - genetics Glutamate Decarboxylase - metabolism Glutamic Acid - chemistry Glutamic Acid - metabolism Lysine Mutation Protein Conformation pyridoxal 5′‐phosphate Pyridoxal Phosphate - metabolism site‐directed mutagenesis Spectrometry, Fluorescence Spectrophotometry
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Beschreibung
Zusammenfassung:	Glutamate decarboxylase is a pyridoxal 5′‐phosphate‐dependent enzyme responsible for the irreversible α‐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
ISSN:	0014-2956 1432-1033
DOI:	10.1046/j.1432-1033.2002.03149.x