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http://purl.uniprot.org/citations/10482517http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10482517http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10482517http://www.w3.org/2000/01/rdf-schema#comment"The methylotrophic proteobacterium Methylobacterium extorquens AM1 possesses tetrahydromethanopterin (H(4)MPT)-dependent enzymes, which are otherwise specific to methanogenic and sulfate-reducing archaea and which have been suggested to be involved in formaldehyde oxidation to CO(2) in M. extorquens AM1. The distribution of H(4)MPT-dependent enzyme activities in cell extracts of methylotrophic bacteria from 13 different genera are reported. H(4)MPT-dependent activities were detected in all of the methylotrophic and methanotrophic proteobacteria tested that assimilate formaldehyde by the serine or ribulose monophosphate pathway. H(4)MPT-dependent activities were also found in autotrophic Xanthobacter strains. However, no H(4)MPT-dependent enzyme activities could be detected in other autotrophic alpha-proteobacteria or in gram-positive methylotrophic bacteria. Genes encoding methenyl H(4)MPT cyclohydrolase (mch genes) were cloned and sequenced from several proteobacteria. Bacterial and archaeal Mch sequences have roughly 35% amino acid identity and form distinct groups in phylogenetic analysis."xsd:string
http://purl.uniprot.org/citations/10482517http://purl.org/dc/terms/identifier"doi:10.1128/jb.181.18.5750-5757.1999"xsd:string
http://purl.uniprot.org/citations/10482517http://purl.org/dc/terms/identifier"doi:10.1128/jb.181.18.5750-5757.1999"xsd:string
http://purl.uniprot.org/citations/10482517http://purl.uniprot.org/core/author"Thauer R.K."xsd:string
http://purl.uniprot.org/citations/10482517http://purl.uniprot.org/core/author"Thauer R.K."xsd:string
http://purl.uniprot.org/citations/10482517http://purl.uniprot.org/core/author"Vorholt J.A."xsd:string
http://purl.uniprot.org/citations/10482517http://purl.uniprot.org/core/author"Vorholt J.A."xsd:string
http://purl.uniprot.org/citations/10482517http://purl.uniprot.org/core/author"Chistoserdova L."xsd:string
http://purl.uniprot.org/citations/10482517http://purl.uniprot.org/core/author"Chistoserdova L.V."xsd:string
http://purl.uniprot.org/citations/10482517http://purl.uniprot.org/core/author"Chistoserdova L.V."xsd:string
http://purl.uniprot.org/citations/10482517http://purl.uniprot.org/core/author"Lidstrom M.E."xsd:string
http://purl.uniprot.org/citations/10482517http://purl.uniprot.org/core/author"Lidstrom M.E."xsd:string
http://purl.uniprot.org/citations/10482517http://purl.uniprot.org/core/author"Stolyar S.M."xsd:string
http://purl.uniprot.org/citations/10482517http://purl.uniprot.org/core/author"Stolyar S.M."xsd:string
http://purl.uniprot.org/citations/10482517http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10482517http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10482517http://purl.uniprot.org/core/name"J. Bacteriol."xsd:string
http://purl.uniprot.org/citations/10482517http://purl.uniprot.org/core/name"J. Bacteriol."xsd:string
http://purl.uniprot.org/citations/10482517http://purl.uniprot.org/core/pages"5750-5757"xsd:string
http://purl.uniprot.org/citations/10482517http://purl.uniprot.org/core/pages"5750-5757"xsd:string
http://purl.uniprot.org/citations/10482517http://purl.uniprot.org/core/title"Distribution of tetrahydromethanopterin-dependent enzymes in methylotrophic bacteria and phylogeny of methenyl tetrahydromethanopterin cyclohydrolases."xsd:string
http://purl.uniprot.org/citations/10482517http://purl.uniprot.org/core/title"Distribution of tetrahydromethanopterin-dependent enzymes in methylotrophic bacteria and phylogeny of methenyl tetrahydromethanopterin cyclohydrolases."xsd:string
http://purl.uniprot.org/citations/10482517http://purl.uniprot.org/core/volume"181"xsd:string