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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/64662
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dc.contributor.authorOliva, Glaucius-
dc.contributor.authorFontes, Marcos R.M.-
dc.contributor.authorGarratt, Richard C.-
dc.contributor.authorAltamirano, Myriam M.-
dc.contributor.authorCalcagno, Mario L.-
dc.contributor.authorHorjales, Eduardo-
dc.date.accessioned2014-05-27T11:18:02Z-
dc.date.accessioned2016-10-25T18:13:37Z-
dc.date.available2014-05-27T11:18:02Z-
dc.date.available2016-10-25T18:13:37Z-
dc.date.issued1995-12-01-
dc.identifierhttp://dx.doi.org/10.1016/S0969-2126(01)00270-2-
dc.identifier.citationStructure, v. 3, n. 12, p. 1323-1332, 1995.-
dc.identifier.issn0969-2126-
dc.identifier.urihttp://hdl.handle.net/11449/64662-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/64662-
dc.description.abstractBackground: Glucosamine 6-phosphate deaminase from Escherichia coli is an allosteric hexameric enzyme which catalyzes the reversible conversion of D-glucosamine 6-phosphate into D-fructose 6-phosphate and ammonium ion and is activated by N-acetyl-D-glucosamine 6-phosphate. Mechanistically, it belongs to the group of aldose-ketose isomerases, but its reaction also accomplishes a simultaneous amination/deamination. The determination of the structure of this protein provides fundamental knowledge for understanding its mode of action and the nature of allosteric conformational changes that regulate its function. Results: The crystal structure of glucosamine 6-phosphate deaminase with bound phosphate ions is presented at 2.1 Å resolution together with the refined structures of the enzyme in complexes with its allosteric activator and with a competitive inhibitor. The protein fold can be described as a modified NAD-binding domain. Conclusions: From the similarities between the three presented structures, it is concluded that these represent the enzymatically active R state conformer. A mechanism for the deaminase reaction is proposed. It comprises steps to open the pyranose ring of the substrate and a sequence of general base-catalyzed reactions to bring about isomerization and deamination, with Asp72 playing a key role as a proton exchanger.en
dc.format.extent1323-1332-
dc.language.isoeng-
dc.sourceScopus-
dc.subjectα/β open structure-
dc.subjectAldose-ketose isomerase-
dc.subjectAllosteric enzyme-
dc.subjectNAD-binding domain-
dc.subject2 deoxy 2 aminoglucitol 6 phosphate-
dc.subject2-deoxy-2-aminoglucitol-6-phosphate-
dc.subjectbacterial protein-
dc.subjectdrug derivative-
dc.subjectenzyme inhibitor-
dc.subjectepimerase-
dc.subjectfructose 6 phosphate-
dc.subjectfructose phosphate-
dc.subjectfructose-6-phosphate-
dc.subjectglucosamine-
dc.subjectglucosamine 6 phosphate-
dc.subjectglucosamine 6 phosphate isomerase-
dc.subjectglucosamine 6-phosphate-
dc.subjectglucosamine-6-phosphate isomerase-
dc.subjectglucose 6 phosphate-
dc.subjectglucose phosphate-
dc.subjectisomerase-
dc.subjectnicotinamide adenine dinucleotide-
dc.subjectphosphate-
dc.subjectsorbitol-
dc.subjectsugar phosphate-
dc.subjectallosterism-
dc.subjectbinding site-
dc.subjectbiosynthesis-
dc.subjectcatalysis-
dc.subjectchemical structure-
dc.subjectchemistry-
dc.subjectdrug antagonism-
dc.subjectenzymology-
dc.subjectEscherichia coli-
dc.subjectmacromolecule-
dc.subjectmetabolism-
dc.subjectprotein conformation-
dc.subjectX ray crystallography-
dc.subjectAldose-Ketose Isomerases-
dc.subjectAllosteric Regulation-
dc.subjectBacterial Proteins-
dc.subjectBinding Sites-
dc.subjectCarbohydrate Epimerases-
dc.subjectCatalysis-
dc.subjectCrystallography, X-Ray-
dc.subjectEnzyme Inhibitors-
dc.subjectFructosephosphates-
dc.subjectGlucosamine-
dc.subjectGlucose-6-Phosphate-
dc.subjectGlucosephosphates-
dc.subjectMacromolecular Substances-
dc.subjectModels, Molecular-
dc.subjectNAD-
dc.subjectPhosphates-
dc.subjectProtein Conformation-
dc.subjectSorbitol-
dc.subjectSugar Phosphates-
dc.subjectBacteria (microorganisms)-
dc.titleStructure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 Å resolutionen
dc.typeoutro-
dc.contributor.institutionUniversidade de São Paulo (USP)-
dc.contributor.institutionUniv. Nac. Auton. de México-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.description.affiliationInst. de Fisica de São Carlos Universidade de São Paulo, São Carlos, SP, 13560-970-
dc.description.affiliationDepartamento de Bioquímica Facultad de Medicina Univ. Nac. Auton. de México, 04510, México, D.F.-
dc.description.affiliationDepto. de Fis. e Biofísica IB-UNESP, CP 510, Botucatu, 18618-000-
dc.description.affiliationDepto. Reconocimiento Molec. y B. Instituto de Biotecnología Univ. Nac. Auton. de México, PO Box 510-3, Cuernavaca, MOR, 62250-
dc.description.affiliationUnespDepto. de Fis. e Biofísica IB-UNESP, CP 510, Botucatu, 18618-000-
dc.identifier.doi10.1016/S0969-2126(01)00270-2-
dc.rights.accessRightsAcesso aberto-
dc.identifier.file2-s2.0-0029646095.pdf-
dc.relation.ispartofStructure-
dc.identifier.scopus2-s2.0-0029646095-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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