Ferredoxin-dependent glutamate synthase: involvement in ammonium assimilation in Haloferax mediterranei

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dc.contributorBiotecnología de Extremófilos (BIOTECEXTREM)es
dc.contributor.authorPire, Carmen-
dc.contributor.authorMartínez-Espinosa, Rosa María-
dc.contributor.authorPérez Pomares, Francisco-
dc.contributor.authorEsclapez, Julia-
dc.contributor.authorBonete, María-José-
dc.contributor.otherUniversidad de Alicante. Departamento de Agroquímica y Bioquímicaes
dc.date.accessioned2014-05-26T09:36:11Z-
dc.date.available2014-05-26T09:36:11Z-
dc.date.issued2014-01-
dc.identifier.citationExtremophiles. 2014, 18(1): 147-159. doi:10.1007/s00792-013-0606-9es
dc.identifier.issn1431-0651 (Print)-
dc.identifier.issn1433-4909 (Online)-
dc.identifier.urihttp://hdl.handle.net/10045/37355-
dc.description.abstractGlutamate synthase (GOGAT) is one of the two important enzymes involved in the ammonium assimilation pathway glutamine synthetase (GS)/GOGAT, which enables Hfx. mediterranei to thrive in media with low ammonium concentration or containing just nitrate as single nitrogen source. The gene coding for this enzyme, gltS, has been sequenced, analysed and compared with other GOGATs from different organisms from the three domains of life. According to its amino acid sequence, Hfx. mediterranei GOGAT displays high homology with those from other archaeal halophilic organisms and with the bacterial alpha-like subunit. Hfx. mediterranei GOGAT and GS expression was induced under conditions of ammonium restriction. The GOGAT protein was found to be a monomer with a molecular mass of 163.78 kDa, which is consistent with that estimated by gel filtration, 198 ± 30 kDa. The enzyme is highly ferredoxin dependent: activity was only observed with one of the two different 2Fe–2S ferredoxins chromatographically isolated from Hfx. mediterranei. The enzyme also displayed typical halophilic behaviour, being fully stable, and producing maximal activity, at salt concentrations from 3 to 4 M NaCl, pH 7.5 and a temperature of 50 °C.es
dc.description.sponsorshipThis work was supported by project BIO2008-00082 from the Spanish Ministry of Science and Innovation (MICINN), which includes funding from the European Union ("FEDER").es
dc.languageenges
dc.publisherSpringer Japanes
dc.rightsThe original publication is available at www.springerlink.comes
dc.subjectHaloferax mediterraneies
dc.subjectGS/GOGAT pathwayes
dc.subjectGlutamate synthase expressiones
dc.subjectEnrichment and characterizationes
dc.subject.otherBioquímica y Biología Moleculares
dc.titleFerredoxin-dependent glutamate synthase: involvement in ammonium assimilation in Haloferax mediterraneies
dc.typeinfo:eu-repo/semantics/articlees
dc.peerreviewedsies
dc.identifier.doi10.1007/s00792-013-0606-9-
dc.relation.publisherversionhttp://dx.doi.org/10.1007/s00792-013-0606-9es
dc.rights.accessRightsinfo:eu-repo/semantics/restrictedAccesses
dc.relation.projectIDinfo:eu-repo/grantAgreement/MICINN//BIO2008-00082-
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