Source:http://linkedlifedata.com/resource/pubmed/id/19943898
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2010-1-18
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pubmed:abstractText |
The ability of some microbial species to oxidize monomethylamine via glutamate-mediated pathways was proposed in the 1960s; however, genetic determinants of the pathways have never been described. In the present study we describe a gene cluster essential for operation of the N-methylglutamate pathway in the methylotrophic beta-proteobacterium Methyloversatilis universalis FAM5. Four major polypeptides from protein fractions displaying high activities of N-methylglutamate synthetase, N-methylglutamate dehydrogenase and gamma-glutamylmethylamide synthetase were selected for mass spectrometry-based identification. The activities of enzymes were associated with the presence of peptides identified as ferredoxin-dependent glutamate synthase (GltB2), large subunit of putative heterotetrameric sarcosine oxidase (SoxA) and glutamine synthetase type III (GSIII) respectively. A gene cluster (8.3 kb) harbouring gltB2, soxA and gsIII-like genes was amplified from M. universalis FAM5, sequenced and assembled. Two partial and six complete open reading frames arranged in the order soxBDAG-gsIII-gltB132 were identified and subjected to mutational analysis, functional and metabolic profiling. We demonstrated that gltB-like and sox-like genes play a key role in methylamine utilization and encode N-methylglutamate synthetase and N-methylglutamate dehydrogenase respectively. Metabolic, enzymatic and mutational analyses showed that the gsIII-like gene encodes gamma-glutamylmethylamide synthetase; however, this enzyme is not essential for oxidation of methylamine.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Alanine,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamate Synthase,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamine,
http://linkedlifedata.com/resource/pubmed/chemical/Methylamines,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/methylamine
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1365-2958
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
75
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
426-39
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pubmed:meshHeading |
pubmed-meshheading:19943898-Alanine,
pubmed-meshheading:19943898-Bacterial Proteins,
pubmed-meshheading:19943898-Betaproteobacteria,
pubmed-meshheading:19943898-DNA Mutational Analysis,
pubmed-meshheading:19943898-Gene Expression Profiling,
pubmed-meshheading:19943898-Glutamate Synthase,
pubmed-meshheading:19943898-Glutamic Acid,
pubmed-meshheading:19943898-Glutamine,
pubmed-meshheading:19943898-Kinetics,
pubmed-meshheading:19943898-Methylamines,
pubmed-meshheading:19943898-Multigene Family,
pubmed-meshheading:19943898-Open Reading Frames,
pubmed-meshheading:19943898-Oxidation-Reduction,
pubmed-meshheading:19943898-Peptide Fragments
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pubmed:year |
2010
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pubmed:articleTitle |
Genetics of the glutamate-mediated methylamine utilization pathway in the facultative methylotrophic beta-proteobacterium Methyloversatilis universalis FAM5.
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pubmed:affiliation |
Department of Chemical Engineering, University of Washington, Seattle, WA 98195, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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