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http://purl.uniprot.org/citations/11208796http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11208796http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11208796http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/11208796http://www.w3.org/2000/01/rdf-schema#comment"The anaerobic metabolism of 3-hydroxybenzoate was studied in the denitrifying bacterium Thauera aromatica. Cells grown with this substrate were adapted to grow with benzoate but not with 4-hydroxybenzoate. Vice versa, 4-hydroxybenzoate-grown cells did not utilize 3-hydroxybenzoate. The first step in 3-hydroxybenzoate metabolism is a coenzyme A (CoA) thioester formation, which is catalyzed by an inducible 3-hydroxybenzoate-CoA ligase. The enzyme was purified and characterized. Further metabolism of 3-hydroxybenzoyl-CoA by cell extract required MgATP and was coupled to the oxidation of 2 mol of reduced viologen dyes per mol of substrate added. Purification of the 3-hydroxybenzoyl-CoA reducing enzyme revealed that this activity was due to benzoyl-CoA reductase, which reduced the 3-hydroxy analogue almost as efficiently as benzoyl-CoA. The further metabolism of the alicyclic dienoyl-CoA product containing the hydroxyl substitution obviously required additional specific enzymes. Comparison of the protein pattern of 3-hydroxybenzoate-grown cells with benzoate-grown cells revealed several 3-hydroxybenzoate-induced proteins; the N-terminal amino acid sequences of four induced proteins were determined and the corresponding genes were identified and sequenced. A cluster of six adjacent genes contained the genes for substrate-induced proteins 1 to 3; this cluster may not yet be complete. Protein 1 is a short-chain alcohol dehydrogenase. Protein 2 is a member of enoyl-CoA hydratase enzymes. Protein 3 was identified as 3-hydroxybenzoate-CoA ligase. Protein 4 is another member of the enoyl-CoA hydratases. In addition, three genes coding for enzymes of beta-oxidation were present. The anaerobic 3-hydroxybenzoate metabolism here obviously combines an enzyme (benzoyl-CoA reductase) and electron carrier (ferredoxin) of the general benzoyl-CoA pathway with enzymes specific for the 3-hydroxybenzoate pathway. This raises some questions concerning the regulation of both pathways."xsd:string
http://purl.uniprot.org/citations/11208796http://purl.org/dc/terms/identifier"doi:10.1128/jb.183.3.968-979.2001"xsd:string
http://purl.uniprot.org/citations/11208796http://purl.org/dc/terms/identifier"doi:10.1128/jb.183.3.968-979.2001"xsd:string
http://purl.uniprot.org/citations/11208796http://purl.org/dc/terms/identifier"doi:10.1128/JB.183.3.968-979.2001"xsd:string
http://purl.uniprot.org/citations/11208796http://purl.uniprot.org/core/author"Fuchs G."xsd:string
http://purl.uniprot.org/citations/11208796http://purl.uniprot.org/core/author"Fuchs G."xsd:string
http://purl.uniprot.org/citations/11208796http://purl.uniprot.org/core/author"Breese K."xsd:string
http://purl.uniprot.org/citations/11208796http://purl.uniprot.org/core/author"Breese K."xsd:string
http://purl.uniprot.org/citations/11208796http://purl.uniprot.org/core/author"Jahn M."xsd:string
http://purl.uniprot.org/citations/11208796http://purl.uniprot.org/core/author"Jahn M."xsd:string
http://purl.uniprot.org/citations/11208796http://purl.uniprot.org/core/author"Laempe D."xsd:string
http://purl.uniprot.org/citations/11208796http://purl.uniprot.org/core/author"Laempe D."xsd:string
http://purl.uniprot.org/citations/11208796http://purl.uniprot.org/core/author"Schaegger H."xsd:string
http://purl.uniprot.org/citations/11208796http://purl.uniprot.org/core/author"Schaegger H."xsd:string
http://purl.uniprot.org/citations/11208796http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11208796http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11208796http://purl.uniprot.org/core/name"J. Bacteriol."xsd:string
http://purl.uniprot.org/citations/11208796http://purl.uniprot.org/core/name"J. Bacteriol."xsd:string
http://purl.uniprot.org/citations/11208796http://purl.uniprot.org/core/pages"968-979"xsd:string
http://purl.uniprot.org/citations/11208796http://purl.uniprot.org/core/pages"968-979"xsd:string
http://purl.uniprot.org/citations/11208796http://purl.uniprot.org/core/title"Anaerobic metabolism of 3-hydroxybenzoate by the denitrifying bacterium Thauera aromatica."xsd:string
http://purl.uniprot.org/citations/11208796http://purl.uniprot.org/core/title"Anaerobic metabolism of 3-hydroxybenzoate by the denitrifying bacterium Thauera aromatica."xsd:string
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