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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
22
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pubmed:dateCreated |
1995-12-19
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pubmed:databankReference |
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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.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7592432-1351742,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7592432-1369492,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7592432-14071565,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7592432-14152852,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7592432-1476446,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7592432-1610191,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7592432-16349272,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7592432-1680850,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7592432-1885526,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7592432-1972535,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7592432-2115488,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/7592432-2271166,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/7592432-3031611,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7592432-3169018,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/7592432-6546423,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/7592432-8486283
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9193
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
177
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6545-51
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pubmed:dateRevised |
2010-9-13
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pubmed:meshHeading |
pubmed-meshheading:7592432-Acyl Coenzyme A,
pubmed-meshheading:7592432-Amino Acid Sequence,
pubmed-meshheading:7592432-Anaerobiosis,
pubmed-meshheading:7592432-Base Sequence,
pubmed-meshheading:7592432-Benzoates,
pubmed-meshheading:7592432-Benzoic Acid,
pubmed-meshheading:7592432-Cloning, Molecular,
pubmed-meshheading:7592432-Coenzyme A Ligases,
pubmed-meshheading:7592432-Cyclohexanecarboxylic Acids,
pubmed-meshheading:7592432-Genes, Bacterial,
pubmed-meshheading:7592432-Molecular Sequence Data,
pubmed-meshheading:7592432-Mutation,
pubmed-meshheading:7592432-Restriction Mapping,
pubmed-meshheading:7592432-Rhodopseudomonas,
pubmed-meshheading:7592432-Sequence Analysis, DNA,
pubmed-meshheading:7592432-Sequence Homology, Amino Acid
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pubmed:year |
1995
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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.
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pubmed:affiliation |
Department of Microbiology, University of Iowa, Iowa City 52242, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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