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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1993-5-21
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pubmed:abstractText |
The initial step of anaerobic 4-hydroxybenzoate and 3-hydroxybenzoate degradation was studied in a denitrifying Pseudomonas sp. 4'-Hydroxybenzoate and 3-hydroxybenzoate are converted into their coenzyme A (CoA) thioesters by two different specific coenzyme A ligases. 4-Hydroxybenzoate-CoA ligase (AMP-forming) was purified 350-fold. The ligase is active as a monomer of molecular mass 48 kDa, as determined by gel filtration and SDS/PAGE. At a pH optimum of 8.5, the apparent Km values for 4-hydroxybenzoate, ATP, and coenzyme A are 37 microM, 77 microM, and 125 microM, respectively. The enzyme reacts specifically with 4-hydroxybenzoate (100%) and 4-aminobenzoate (30%). Other analogues of benzoate, notably 3- or 2-hydroxybenzoate, are inactive, and 2,4-dihydroxybenzoate and 2-hydroxy-4-methylbenzoate act as competitive inhibitors (Ki = 1 microM). Polyclonal antibodies were raised and used in immunoblot assays to study the regulation of the expression of 4-hydroxybenzoate-CoA ligase. The ligase is synthesized when cells are grown anaerobically with 4-hydroxybenzoate, phenol, or p-cresol; phenol and p-cresol are degraded via 4-hydroxybenzoate. The enzyme is not present in cells grown aerobically with 4-hydroxybenzoate or anaerobically with benzoate or 4-hydroxyphenylacetate.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/4-hydroxybenzoate coenzyme A ligase,
http://linkedlifedata.com/resource/pubmed/chemical/4-hydroxybenzoic acid,
http://linkedlifedata.com/resource/pubmed/chemical/Coenzyme A Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/Oxygen,
http://linkedlifedata.com/resource/pubmed/chemical/Parabens,
http://linkedlifedata.com/resource/pubmed/chemical/Phenols
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
213
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
555-61
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:8477728-Amino Acid Sequence,
pubmed-meshheading:8477728-Catalysis,
pubmed-meshheading:8477728-Chromatography, Gel,
pubmed-meshheading:8477728-Coenzyme A Ligases,
pubmed-meshheading:8477728-Molecular Sequence Data,
pubmed-meshheading:8477728-Molecular Weight,
pubmed-meshheading:8477728-Oxygen,
pubmed-meshheading:8477728-Parabens,
pubmed-meshheading:8477728-Phenols,
pubmed-meshheading:8477728-Pseudomonas,
pubmed-meshheading:8477728-Substrate Specificity
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pubmed:year |
1993
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pubmed:articleTitle |
Enzymes of anaerobic metabolism of phenolic compounds. 4-Hydroxybenzoate-CoA ligase from a denitrifying Pseudomonas species.
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pubmed:affiliation |
Abteilung Angewandte Mikrobiologie, Universität Ulm, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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