| pubmed-article:19943898 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19943898 | lifeskim:mentions | umls-concept:C0042153 | lld:lifeskim |
| pubmed-article:19943898 | lifeskim:mentions | umls-concept:C1930621 | lld:lifeskim |
| pubmed-article:19943898 | lifeskim:mentions | umls-concept:C0017398 | lld:lifeskim |
| pubmed-article:19943898 | lifeskim:mentions | umls-concept:C1704259 | lld:lifeskim |
| pubmed-article:19943898 | lifeskim:mentions | umls-concept:C1705987 | lld:lifeskim |
| pubmed-article:19943898 | lifeskim:mentions | umls-concept:C0066318 | lld:lifeskim |
| pubmed-article:19943898 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:19943898 | pubmed:dateCreated | 2010-1-18 | lld:pubmed |
| pubmed-article:19943898 | 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. | lld:pubmed |
| pubmed-article:19943898 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19943898 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19943898 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19943898 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19943898 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19943898 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19943898 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19943898 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19943898 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19943898 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19943898 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19943898 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19943898 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:19943898 | pubmed:issn | 1365-2958 | lld:pubmed |
| pubmed-article:19943898 | pubmed:author | pubmed-author:HackettMurray... | lld:pubmed |
| pubmed-article:19943898 | pubmed:author | pubmed-author:SongYangY | lld:pubmed |
| pubmed-article:19943898 | pubmed:author | pubmed-author:WangTiansongT | lld:pubmed |
| pubmed-article:19943898 | pubmed:author | pubmed-author:KalyuzhnayaMa... | lld:pubmed |
| pubmed-article:19943898 | pubmed:author | pubmed-author:LatypovaEkate... | lld:pubmed |
| pubmed-article:19943898 | pubmed:author | pubmed-author:SchäferHendri... | lld:pubmed |
| pubmed-article:19943898 | pubmed:author | pubmed-author:ChavkinTheodo... | lld:pubmed |
| pubmed-article:19943898 | pubmed:author | pubmed-author:WangYi-ShunYS | lld:pubmed |
| pubmed-article:19943898 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19943898 | pubmed:volume | 75 | lld:pubmed |
| pubmed-article:19943898 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19943898 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19943898 | pubmed:pagination | 426-39 | lld:pubmed |
| pubmed-article:19943898 | pubmed:meshHeading | pubmed-meshheading:19943898... | lld:pubmed |
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| pubmed-article:19943898 | pubmed:meshHeading | pubmed-meshheading:19943898... | lld:pubmed |
| pubmed-article:19943898 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:19943898 | pubmed:articleTitle | Genetics of the glutamate-mediated methylamine utilization pathway in the facultative methylotrophic beta-proteobacterium Methyloversatilis universalis FAM5. | lld:pubmed |
| pubmed-article:19943898 | pubmed:affiliation | Department of Chemical Engineering, University of Washington, Seattle, WA 98195, USA. | lld:pubmed |
| pubmed-article:19943898 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19943898 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:19943898 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:19943898 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:19943898 | lld:pubmed |
