| pubmed-article:7592432 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7592432 | lifeskim:mentions | umls-concept:C0995501 | lld:lifeskim |
| pubmed-article:7592432 | lifeskim:mentions | umls-concept:C0023689 | lld:lifeskim |
| pubmed-article:7592432 | lifeskim:mentions | umls-concept:C0018270 | lld:lifeskim |
| pubmed-article:7592432 | lifeskim:mentions | umls-concept:C0220795 | lld:lifeskim |
| pubmed-article:7592432 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
| pubmed-article:7592432 | lifeskim:mentions | umls-concept:C2700640 | lld:lifeskim |
| pubmed-article:7592432 | lifeskim:mentions | umls-concept:C0053264 | lld:lifeskim |
| pubmed-article:7592432 | pubmed:issue | 22 | lld:pubmed |
| pubmed-article:7592432 | pubmed:dateCreated | 1995-12-19 | lld:pubmed |
| pubmed-article:7592432 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7592432 | pubmed:abstractText | 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. | lld:pubmed |
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| pubmed-article:7592432 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7592432 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7592432 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7592432 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7592432 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:7592432 | pubmed:issn | 0021-9193 | lld:pubmed |
| pubmed-article:7592432 | pubmed:author | pubmed-author:GibsonJJ | lld:pubmed |
| pubmed-article:7592432 | pubmed:author | pubmed-author:HarwoodC SCS | lld:pubmed |
| pubmed-article:7592432 | pubmed:author | pubmed-author:EglandP GPG | lld:pubmed |
| pubmed-article:7592432 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7592432 | pubmed:volume | 177 | lld:pubmed |
| pubmed-article:7592432 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7592432 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7592432 | pubmed:pagination | 6545-51 | lld:pubmed |
| pubmed-article:7592432 | pubmed:dateRevised | 2010-9-13 | lld:pubmed |
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| pubmed-article:7592432 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7592432 | pubmed:articleTitle | 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. | lld:pubmed |
| pubmed-article:7592432 | pubmed:affiliation | Department of Microbiology, University of Iowa, Iowa City 52242, USA. | lld:pubmed |
| pubmed-article:7592432 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7592432 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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