Biochemical and spectroscopic properties ofBrucella microti glutamate decarboxylase, a key component of the glutamate‐dependent acid resistance system
Herein, biochemical and spectroscopic properties of GadB fromBrucella microti (BmGadB), aBrucella species which possesses GDAR, are described.B. microti belongs to a group of lately described and atypical brucellae that possess functionalgadB andgadC genes, unlike the most well‐known “classical”Bruc...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Wiley
2015-01-01
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| Series: | FEBS Open Bio |
| Subjects: | |
| Online Access: | https://doi.org/10.1016/j.fob.2015.03.006 |
| _version_ | 1811185075697483776 |
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| author | Gaia Grassini Eugenia Pennacchietti Francesca Cappadocio Alessandra Occhialini Daniela De Biase |
| author_facet | Gaia Grassini Eugenia Pennacchietti Francesca Cappadocio Alessandra Occhialini Daniela De Biase |
| author_sort | Gaia Grassini |
| collection | DOAJ |
| description | Herein, biochemical and spectroscopic properties of GadB fromBrucella microti (BmGadB), aBrucella species which possesses GDAR, are described.B. microti belongs to a group of lately described and atypical brucellae that possess functionalgadB andgadC genes, unlike the most well‐known “classical”Brucella species, which include important human pathogens.BmGadB is hexameric at acidic pH. The pH‐dependent spectroscopic properties and activity profile, combined within silico sequence comparison withE. coli GadB (EcGadB), suggest thatBmGadB 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 thatBmGadB does not undergo membrane recruitment at acidic pH, which was observed inEcGadB. The comparison of GadB from evolutionary distant microorganisms suggests that for this enzyme to be functional in GDAR some structural features must be preserved. |
| first_indexed | 2024-04-11T13:24:34Z |
| format | Article |
| id | doaj.art-516e0ad000ce4070b681f9e6ec567e2d |
| institution | Directory Open Access Journal |
| issn | 2211-5463 |
| language | English |
| last_indexed | 2024-04-11T13:24:34Z |
| publishDate | 2015-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | FEBS Open Bio |
| spelling | doaj.art-516e0ad000ce4070b681f9e6ec567e2d2022-12-22T04:22:07ZengWileyFEBS Open Bio2211-54632015-01-015120921810.1016/j.fob.2015.03.006Biochemical and spectroscopic properties ofBrucella microti glutamate decarboxylase, a key component of the glutamate‐dependent acid resistance systemGaia Grassini0Eugenia Pennacchietti1Francesca Cappadocio2Alessandra Occhialini3Daniela De Biase4Istituto Pasteur-Fondazione Cenci Bolognetti, Department of Medico-Surgical Sciences and Biotechnologies, Sapienza University of Rome, 04100 Latina, ItalyIstituto Pasteur-Fondazione Cenci Bolognetti, Department of Medico-Surgical Sciences and Biotechnologies, Sapienza University of Rome, 04100 Latina, ItalyIstituto Pasteur-Fondazione Cenci Bolognetti, Department of Medico-Surgical Sciences and Biotechnologies, Sapienza University of Rome, 04100 Latina, ItalyUniversité de Montpellier, Centre d’études d'agents Pathogènes et Biotechnologie pour la Santé (CPBS), F-34293 Montpellier, FranceIstituto Pasteur-Fondazione Cenci Bolognetti, Department of Medico-Surgical Sciences and Biotechnologies, Sapienza University of Rome, 04100 Latina, ItalyHerein, biochemical and spectroscopic properties of GadB fromBrucella microti (BmGadB), aBrucella species which possesses GDAR, are described.B. microti belongs to a group of lately described and atypical brucellae that possess functionalgadB andgadC genes, unlike the most well‐known “classical”Brucella species, which include important human pathogens.BmGadB is hexameric at acidic pH. The pH‐dependent spectroscopic properties and activity profile, combined within silico sequence comparison withE. coli GadB (EcGadB), suggest thatBmGadB 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 thatBmGadB does not undergo membrane recruitment at acidic pH, which was observed inEcGadB. The comparison of GadB from evolutionary distant microorganisms suggests that for this enzyme to be functional in GDAR some structural features must be preserved.https://doi.org/10.1016/j.fob.2015.03.006Brucella microtiGlutamate decarboxylaseCooperativitypH-dependent activityChloride activationSubstituted aldamine |
| spellingShingle | Gaia Grassini Eugenia Pennacchietti Francesca Cappadocio Alessandra Occhialini Daniela De Biase Biochemical and spectroscopic properties ofBrucella microti glutamate decarboxylase, a key component of the glutamate‐dependent acid resistance system FEBS Open Bio Brucella microti Glutamate decarboxylase Cooperativity pH-dependent activity Chloride activation Substituted aldamine |
| title | Biochemical and spectroscopic properties ofBrucella microti glutamate decarboxylase, a key component of the glutamate‐dependent acid resistance system |
| title_full | Biochemical and spectroscopic properties ofBrucella microti glutamate decarboxylase, a key component of the glutamate‐dependent acid resistance system |
| title_fullStr | Biochemical and spectroscopic properties ofBrucella microti glutamate decarboxylase, a key component of the glutamate‐dependent acid resistance system |
| title_full_unstemmed | Biochemical and spectroscopic properties ofBrucella microti glutamate decarboxylase, a key component of the glutamate‐dependent acid resistance system |
| title_short | Biochemical and spectroscopic properties ofBrucella microti glutamate decarboxylase, a key component of the glutamate‐dependent acid resistance system |
| title_sort | biochemical and spectroscopic properties ofbrucella microti glutamate decarboxylase a key component of the glutamate dependent acid resistance system |
| topic | Brucella microti Glutamate decarboxylase Cooperativity pH-dependent activity Chloride activation Substituted aldamine |
| url | https://doi.org/10.1016/j.fob.2015.03.006 |
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