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| Subject | Predicate | Object |
|---|---|---|
| http://purl.uniprot.org/citations/7592432 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7592432 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7592432 | http://www.w3.org/2000/01/rdf-schema#comment | "The first step of anaerobic benzoate degradation is the formation of benzoyl-coenzyme A by benzoate-coenzyme A ligase. This enzyme, purified from Rhodopseudomonas palustris, is maximally active with 5 microM benzoate. To study the molecular basis for this reaction, the benzoate-coenzyme A ligase gene (badA) was cloned and sequenced. The deduced amino acid sequence of badA showed substantial similarity to other coenzyme A ligases, with the highest degree of similarity being that to 4-hydroxybenzoate-coenzyme A ligase (50% amino acid identity) from R. palustris. A badA mutant that was constructed had barely detectable levels of ligase activity when cell extracts were assayed at 10 microM benzoate. Despite this, the mutant grew at wild-type rates on benzoate under laboratory culture conditions (3 mM benzoate), and mutant cell extracts had high levels of ligase activity when assayed at a high concentration of benzoate (1 mM). This suggested that R. palustris expresses, in addition to BadA, a benzoate-activating enzyme(s) with a relatively low affinity for benzoate. A possible role of 4-hydroxybenzoate-coenzyme A ligase (encoded by hbaA) in this capacity was investigated by constructing a badA hbaA double mutant. Although the double mutant grew more slowly on benzoate than badA cells, growth rates were still significant, suggesting the involvement of a third enzyme in benzoate activation. Competition experiments involving the addition of a small amount of cyclohexanecarboxylate to ligase assay mixtures implicated cyclohexanecarboxylate-coenzyme A ligase as being this third enzyme. These results show that wild-type R. palustris cells synthesize at least three enzymes that can catalyze the initial step in anaerobic benzoate degradation during growth on benzoate. This observation supports previous suggestions that benzoyl-coenzyme A formation plays a central role in anaerobic aromatic compound biodegradation."xsd:string |
| http://purl.uniprot.org/citations/7592432 | http://purl.org/dc/terms/identifier | "doi:10.1128/jb.177.22.6545-6551.1995"xsd:string |
| http://purl.uniprot.org/citations/7592432 | http://purl.uniprot.org/core/author | "Gibson J."xsd:string |
| http://purl.uniprot.org/citations/7592432 | http://purl.uniprot.org/core/author | "Gibson J."xsd:string |
| http://purl.uniprot.org/citations/7592432 | http://purl.uniprot.org/core/author | "Harwood C.S."xsd:string |
| http://purl.uniprot.org/citations/7592432 | http://purl.uniprot.org/core/author | "Harwood C.S."xsd:string |
| http://purl.uniprot.org/citations/7592432 | http://purl.uniprot.org/core/author | "Egland P.G."xsd:string |
| http://purl.uniprot.org/citations/7592432 | http://purl.uniprot.org/core/author | "Egland P.G."xsd:string |
| http://purl.uniprot.org/citations/7592432 | http://purl.uniprot.org/core/date | "1995"xsd:gYear |
| http://purl.uniprot.org/citations/7592432 | http://purl.uniprot.org/core/date | "1995"xsd:gYear |
| http://purl.uniprot.org/citations/7592432 | http://purl.uniprot.org/core/name | "J. Bacteriol."xsd:string |
| http://purl.uniprot.org/citations/7592432 | http://purl.uniprot.org/core/name | "J Bacteriol"xsd:string |
| http://purl.uniprot.org/citations/7592432 | http://purl.uniprot.org/core/pages | "6545-6551"xsd:string |
| http://purl.uniprot.org/citations/7592432 | http://purl.uniprot.org/core/pages | "6545-6551"xsd:string |
| http://purl.uniprot.org/citations/7592432 | http://purl.uniprot.org/core/title | "Benzoate-coenzyme A ligase, encoded by badA, is one of three ligases able to catalyze benzoyl-coenzyme A formation during anaerobic growth of Rhodopseudomonas palustris on benzoate."xsd:string |
| http://purl.uniprot.org/citations/7592432 | http://purl.uniprot.org/core/title | "Benzoate-coenzyme A ligase, encoded by badA, is one of three ligases able to catalyze benzoyl-coenzyme A formation during anaerobic growth of Rhodopseudomonas palustris on benzoate."xsd:string |
| http://purl.uniprot.org/citations/7592432 | http://purl.uniprot.org/core/volume | "177"xsd:string |
| http://purl.uniprot.org/citations/7592432 | http://purl.uniprot.org/core/volume | "177"xsd:string |
| http://purl.uniprot.org/citations/7592432 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/7592432 |
| http://purl.uniprot.org/citations/7592432 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/7592432 |
| http://purl.uniprot.org/citations/7592432 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/7592432 |
| http://purl.uniprot.org/citations/7592432 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/7592432 |
| http://purl.uniprot.org/uniprot/Q59760 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/7592432 |