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dc.contributor.author
Liffourrena, Andres Sebastian  
dc.contributor.author
Lucchesi, Gloria Ines  
dc.date.available
2018-01-19T18:07:54Z  
dc.date.issued
2014-04  
dc.identifier.citation
Liffourrena, Andres Sebastian; Lucchesi, Gloria Ines; Identification, Cloning and Biochemical Characterization of Pseudomonas putida A (ATCC 12633) Monooxygenase Enzyme necessary for the Metabolism of Tetradecyltrimethylammonium Bromide; Humana Press; Applied Biochemistry And Biotechnology; 173; 2; 4-2014; 552-561  
dc.identifier.issn
0273-2289  
dc.identifier.uri
http://hdl.handle.net/11336/33975  
dc.description.abstract
This study presents the first report of the purification and characterization of a monooxygenase enzyme from Pseudomonas putida A (ATCC 12633) that is responsible for the oxidation of physiologically relevant quaternary ammonium compounds, the tetradecyltrimethylammonium bromide. The degradation of tetradecyltrimethylammonium bromide by P. putida A (ATCC 12633) is initiated by N-dealkylation and catalysed by tetradecyltrimethylammonium monooxygenase (TTABMO), resulting in the formation of tetradecylalkanal and trimethylamine. Based on sequence analysis, the gene for TTABMO (ttbmo) corresponded to an ORF named PP2033 in the genome of P. putida KT2440. Mutation in ttabmo blocked the utilization of tetradecyltrimethylammonium bromide by Pseudomonas putida A (ATCC 12633) as carbon and nitrogen sources. The enzyme can be highly overexpressed in P. putida Δttabmo-T7 in active form and purified as a hexahistidine fusion protein. Like the native enzyme, the his-TTABMO was found to be a monomer with molecular mass of 40 kDa, the isoelectric point 7.3, that catalyses the breakdown of tetradecyltrimethylammonium bromide and utilized NADPH and FAD as cofactor. The biochemical properties and the analysis of the respective protein sequence revealed that TTABMO represents a typical flavoprotein monooxygenase, which is member of a flavoprotein family that is distinct from Baeyer–Villiger monooxygenases.  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
Humana Press  
dc.rights
info:eu-repo/semantics/openAccess  
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/  
dc.subject
Monooxygenase Enzyme  
dc.subject
Pseudomonas Putida  
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Quaternary Ammonium Compounds  
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Tetradecyltrimethylammonium  
dc.subject.classification
Otras Ciencias Biológicas  
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Ciencias Biológicas  
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CIENCIAS NATURALES Y EXACTAS  
dc.title
Identification, Cloning and Biochemical Characterization of Pseudomonas putida A (ATCC 12633) Monooxygenase Enzyme necessary for the Metabolism of Tetradecyltrimethylammonium Bromide  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2018-01-18T21:02:36Z  
dc.journal.volume
173  
dc.journal.number
2  
dc.journal.pagination
552-561  
dc.journal.pais
Estados Unidos  
dc.journal.ciudad
Oregon  
dc.description.fil
Fil: Liffourrena, Andres Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Biología Molecular; Argentina  
dc.description.fil
Fil: Lucchesi, Gloria Ines. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Biología Molecular; Argentina  
dc.journal.title
Applied Biochemistry And Biotechnology  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007%2Fs12010-014-0862-x  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1007/s12010-014-0862-x