pubmed-article:207665 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:207665 | lifeskim:mentions | umls-concept:C0001930 | lld:lifeskim |
pubmed-article:207665 | lifeskim:mentions | umls-concept:C0080194 | lld:lifeskim |
pubmed-article:207665 | lifeskim:mentions | umls-concept:C0025519 | lld:lifeskim |
pubmed-article:207665 | lifeskim:mentions | umls-concept:C0007066 | lld:lifeskim |
pubmed-article:207665 | lifeskim:mentions | umls-concept:C0010566 | lld:lifeskim |
pubmed-article:207665 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:207665 | pubmed:dateCreated | 1978-8-14 | lld:pubmed |
pubmed-article:207665 | pubmed:abstractText | Thirty-three microorganisms capable of growth with cyclohexane carboxylate as the sole source of carbon were isolated from mud, water, and soil samples from the Aberystwyth area. Preliminary screening and whole-cell oxidation studies suggested that, with one exception, all of the strains metabolized the growth substrate by beta-oxidation of the coenzyme A ester. This single distinctive strain, able to oxidize rapidly trans-4-hydroxycyclohexane carboxylate, 4-ketocyclohexane carboxylate, p-hydroxybenzoate, and protocatechuate when grown with cyclohexane carboxylate, was classified as a strain of Alcaligenes and given the number W1. Enzymes capable of converting cyclohexane carboxylate to p-hydroxybenzoate were induced by growth with the alicyclic acid and included the first unambiguous specimen of a cyclohexane carboxylate hydroxylase. Because it is a very fragile protein, attempts to stabilize the cyclohexane carboxylate hydroxylase so that a purification procedure could be developed have consistently failed. In limited studies with crude cell extracts, we found that hydroxylation occurred at the 4 position, probably yielding the trans isomer of 4-hydroxycyclohexane carboxylate. Simultaneous measurement of oxygen consumption and reduced nicotinamide adenine dinucleotide oxidation, coupled with an assessment of reactant stoichiometry, showed the enzyme to be a mixed-function oxygenase. Mass spectral analysis enabled the conversion of cyclohexane carboxylate to p-hydroxybenzoate by cell extracts to be established unequivocally, and all of our data were consistent with the pathway: cyclohexane carboxylate --> trans-4-hydroxycyclohexane carboxylate --> 4-ketocyclohexane carboxylate --> p-hydroxybenzoate. The further metabolism of p-hydroxybenzoate proceeded by meta fission and by the oxidative branch of the 2-hydroxy-4-carboxymuconic semialde-hyde-cleaving pathway. | lld:pubmed |
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pubmed-article:207665 | pubmed:language | eng | lld:pubmed |
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pubmed-article:207665 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:207665 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:207665 | pubmed:month | May | lld:pubmed |
pubmed-article:207665 | pubmed:issn | 0021-9193 | lld:pubmed |
pubmed-article:207665 | pubmed:author | pubmed-author:TrudgillP WPW | lld:pubmed |
pubmed-article:207665 | pubmed:author | pubmed-author:TaylorD GDG | lld:pubmed |
pubmed-article:207665 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:207665 | pubmed:volume | 134 | lld:pubmed |
pubmed-article:207665 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:207665 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:207665 | pubmed:pagination | 401-11 | lld:pubmed |
pubmed-article:207665 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:207665 | pubmed:year | 1978 | lld:pubmed |
pubmed-article:207665 | pubmed:articleTitle | Metabolism of cyclohexane carboxylic acid by Alcaligenes strain W1. | lld:pubmed |
pubmed-article:207665 | pubmed:publicationType | Journal Article | lld:pubmed |
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