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dc.contributor.author
Liffourrena, Andres Sebastian
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dc.contributor.author
Salvano, Mario Armando
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dc.contributor.author
Lucchesi, Gloria Ines
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dc.date.available
2021-04-20T18:45:33Z
dc.date.issued
2010-05-01
dc.identifier.citation
Liffourrena, Andres Sebastian; Salvano, Mario Armando; Lucchesi, Gloria Ines; Pseudomonas putida A ATCC 12633 oxidizes trimethylamine aerobically via two different pathways; Springer; Archives of Microbiology; 192; 6; 1-5-2010; 471-476
dc.identifier.issn
0302-8933
dc.identifier.uri
http://hdl.handle.net/11336/130544
dc.description.abstract
The present study examined the aerobic metabolism of trimethylamine in Pseudomonas putida A ATCC 12633 grown on tetradecyltrimethylammonium bromide or trimethylamine. In both conditions, the trimethylamine was used as a nitrogen source and also accumulated in the cell, slowing the bacterial growth. Decreased bacterial growth was counteracted by the addition of AlCl3. Cell-free extracts prepared from cells grown aerobically on tetradecyltrimethylammonium bromide exhibited trimethylamine monooxygenase activity that produced trimethylamine N-oxide and trimethylamine N-oxide demethylase activity that produced dimethylamine. Cell-free extracts from cells grown on trimethylamine exhibited trimethylamine dehydrogenase activity that produced dimethylamine, which was oxidized to methanal and methylamine by dimethylamine dehydrogenase. These results show that this bacterial strain uses two enzymes to initiate the oxidation of trimethylamine in aerobic conditions. The apparent Km for trimethylamine was 0.7 mM for trimethylamine monooxygenase and 4.0 mM for trimethylamine dehydrogenase, but both enzymes maintain similar catalytic efficiency (0.5 and 0.4, respectively). Trimethylamine dehydrogenase was inhibited by trimethylamine from 1 mM. Therefore, the accumulation of trimethylamine inside Pseudomonas putida A ATCC 12633 grown on tetradecyltri- methylammonium bromide or trimethylamine may be due to the low catalytic efficiency of trimethylamine monooxygenase and trimethylamine dehydrogenase.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Springer
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
PSEUDOMONAS PUTIDA
dc.subject
TETRADECYLTRIMETHYLAMMONIUM
dc.subject
TRIMETHYLAMINE
dc.subject
TRIMETHYLAMINE DEHYDROGENASE
dc.subject
TRIMETHYLAMINE MONOOXYGENASE
dc.subject.classification
Bioquímica y Biología Molecular
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
Pseudomonas putida A ATCC 12633 oxidizes trimethylamine aerobically via two different pathways
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2021-04-09T16:17:30Z
dc.journal.volume
192
dc.journal.number
6
dc.journal.pagination
471-476
dc.journal.pais
Alemania
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dc.description.fil
Fil: Liffourrena, Andres Sebastian. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Biología Molecular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina
dc.description.fil
Fil: Salvano, Mario Armando. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Biología Molecular; Argentina
dc.description.fil
Fil: Lucchesi, Gloria Ines. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Biología Molecular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina
dc.journal.title
Archives of Microbiology
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007/s00203-010-0577-5
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://doi.org/10.1007/s00203-010-0577-5
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