MULTISPECIES: glutamate decarboxylase [Enterobacteriaceae]

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On the effect of alkaline pH and cofactor availability in the conformational and oligomeric state of Escherichia coli glutamate decarboxylase. [Protein Eng Des Sel. 2017]
On the effect of alkaline pH and cofactor availability in the conformational and oligomeric state of Escherichia coli glutamate decarboxylase.
Giovannercole F, Mérigoux C, Zamparelli C, Verzili D, Grassini G, Buckle M, Vachette P, De Biase D. Protein Eng Des Sel. 2017 Mar 1; 30(3):235-244.
Mutation of His465 alters the pH-dependent spectroscopic properties of Escherichia coli glutamate decarboxylase and broadens the range of its activity toward more alkaline pH. [J Biol Chem. 2009]
Mutation of His465 alters the pH-dependent spectroscopic properties of Escherichia coli glutamate decarboxylase and broadens the range of its activity toward more alkaline pH.
Pennacchietti E, Lammens TM, Capitani G, Franssen MC, John RA, Bossa F, De Biase D. J Biol Chem. 2009 Nov 13; 284(46):31587-96. Epub 2009 Sep 21.
Escherichia coli acid resistance: pH-sensing, activation by chloride and autoinhibition in GadB. [EMBO J. 2006]
Escherichia coli acid resistance: pH-sensing, activation by chloride and autoinhibition in GadB.
Gut H, Pennacchietti E, John RA, Bossa F, Capitani G, De Biase D, Grütter MG. EMBO J. 2006 Jun 7; 25(11):2643-51. Epub 2006 May 4.

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