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The pH\u2010dependent spectroscopic properties and activity profile, combined with<jats:italic>in silico<\/jats:italic> sequence comparison with<jats:italic>E. coli<\/jats:italic> GadB (<jats:italic>Ec<\/jats:italic>GadB), suggest that<jats:italic>Bm<\/jats:italic>GadB has the necessary structural requirements for the binding of activating chloride ions at acidic pH and for the closure of its active site at neutral pH. On the contrary, cellular localization analysis, corroborated by sequence inspection, suggests that<jats:italic>Bm<\/jats:italic>GadB does not undergo membrane recruitment at acidic pH, which was observed in<jats:italic>Ec<\/jats:italic>GadB. The comparison of GadB from evolutionary distant microorganisms suggests that for this enzyme to be functional in GDAR some structural features must be preserved.<\/jats:p>","DOI":"10.1016\/j.fob.2015.03.006","type":"journal-article","created":{"date-parts":[[2015,3,23]],"date-time":"2015-03-23T09:59:25Z","timestamp":1427104765000},"page":"209-218","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":14,"title":["Biochemical and spectroscopic properties of<i>Brucella microti<\/i> glutamate decarboxylase, a key component of the glutamate\u2010dependent acid resistance system"],"prefix":"10.1002","volume":"5","author":[{"given":"Gaia","family":"Grassini","sequence":"first","affiliation":[{"name":"Istituto Pasteur-Fondazione Cenci Bolognetti, Department of Medico-Surgical Sciences and Biotechnologies, Sapienza University of Rome, 04100 Latina, 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