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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/70966
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dc.contributor.authorThum, Caroline-
dc.contributor.authorSchneider, Cristopher Z.-
dc.contributor.authorPalma, Mario Sergio-
dc.contributor.authorSantos, Diógenes S.-
dc.contributor.authorBasso, Luiz A.-
dc.date.accessioned2014-05-27T11:23:53Z-
dc.date.accessioned2016-10-25T18:26:56Z-
dc.date.available2014-05-27T11:23:53Z-
dc.date.available2016-10-25T18:26:56Z-
dc.date.issued2009-04-01-
dc.identifierhttp://dx.doi.org/10.1128/JB.01337-08-
dc.identifier.citationJournal of Bacteriology, v. 191, n. 8, p. 2884-2887, 2009.-
dc.identifier.issn0021-9193-
dc.identifier.urihttp://hdl.handle.net/11449/70966-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/70966-
dc.description.abstractThe Mycobacterium tuberculosis cmk gene, predicted to encode a CMP kinase (CMK), was cloned and expressed, and its product was purified to homogeneity. Steady-state kinetics confirmed that M. tuberculosis CMK is a monomer that preferentially phosphorylates CMP and dCMP by a sequential mechanism. A plausible role for CMK is discussed. Copyright © 2009, American Society for Microbiology. All Rights Reserved.en
dc.format.extent2884-2887-
dc.language.isoeng-
dc.sourceScopus-
dc.subjectcytidine phosphate kinase-
dc.subjectdeoxycytidine phosphate-
dc.subjectmonomer-
dc.subjectphosphotransferase-
dc.subjectunclassified drug-
dc.subjectcytidylate kinase-
dc.subjectnucleoside monophosphate kinase-
dc.subjectrecombinant protein-
dc.subjectbacterial gene-
dc.subjectbacterial strain-
dc.subjectcontrolled study-
dc.subjectenzyme kinetics-
dc.subjectenzyme phosphorylation-
dc.subjectgene expression-
dc.subjectgene locus-
dc.subjectgenetic code-
dc.subjectmolecular cloning-
dc.subjectMycobacterium tuberculosis-
dc.subjectnonhuman-
dc.subjectpriority journal-
dc.subjectprotein function-
dc.subjectprotein purification-
dc.subjectsteady state-
dc.subjectamino acid sequence-
dc.subjectenzymology-
dc.subjectgenetics-
dc.subjectisolation and purification-
dc.subjectkinetics-
dc.subjectmetabolism-
dc.subjectmolecular genetics-
dc.subjectphosphorylation-
dc.subjectsequence alignment-
dc.subjectAmino Acid Sequence-
dc.subjectCloning, Molecular-
dc.subjectDeoxycytidine Monophosphate-
dc.subjectGene Expression-
dc.subjectKinetics-
dc.subjectMolecular Sequence Data-
dc.subjectNucleoside-Phosphate Kinase-
dc.subjectPhosphorylation-
dc.subjectRecombinant Proteins-
dc.subjectSequence Alignment-
dc.titleThe Rv1712 locus from Mycobacterium tuberculosis H37Rv codes for a functional CMP kinase that preferentially Phosphorylates dCMPen
dc.typeoutro-
dc.contributor.institutionPontifícia Universidade Católica do Rio Grande do Sul (PUCRS)-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.description.affiliationCentro de Pesquisas em Biologia Molecular e Funcional Instituto Nacional de Ciência e Tecnologia em Tuberculose Pontificia Universidade Católica do Rio Grande do Sul, Av. Ipiranga 6681, Porto Alegre, RS 90619-900-
dc.description.affiliationPrograma de Pós-Graduação em Biologia Celular e Molecular Pontificia Universidade Católica do Rio Grande do Sul, Av. Ipiranga 6681, Porto Alegre, RS 90619-900-
dc.description.affiliationLaboratório de Biologia Estrutural e Zooquímica Centro de Estudos de Insetos Sociais Universidade Estadual Paulista-Rio Claro, SP13506-900-
dc.description.affiliation, Av. Ipiranga 6681, Tecnopuc-Predio 92A, Porto Alegre, RS 90619-900-
dc.description.affiliationUnespLaboratório de Biologia Estrutural e Zooquímica Centro de Estudos de Insetos Sociais Universidade Estadual Paulista-Rio Claro, SP13506-900-
dc.identifier.doi10.1128/JB.01337-08-
dc.rights.accessRightsAcesso restrito-
dc.identifier.file2-s2.0-65249143233.pdf-
dc.relation.ispartofJournal of Bacteriology-
dc.identifier.scopus2-s2.0-65249143233-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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