| pubmed-article:11698383 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11698383 | lifeskim:mentions | umls-concept:C1042122 | lld:lifeskim |
| pubmed-article:11698383 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:11698383 | lifeskim:mentions | umls-concept:C0036075 | lld:lifeskim |
| pubmed-article:11698383 | lifeskim:mentions | umls-concept:C0439851 | lld:lifeskim |
| pubmed-article:11698383 | lifeskim:mentions | umls-concept:C1260969 | lld:lifeskim |
| pubmed-article:11698383 | lifeskim:mentions | umls-concept:C1552596 | lld:lifeskim |
| pubmed-article:11698383 | lifeskim:mentions | umls-concept:C1947931 | lld:lifeskim |
| pubmed-article:11698383 | pubmed:issue | 23 | lld:pubmed |
| pubmed-article:11698383 | pubmed:dateCreated | 2001-11-7 | lld:pubmed |
| pubmed-article:11698383 | pubmed:abstractText | In cell extracts of Pseudaminobacter salicylatoxidans strain BN12, an enzymatic activity was detected which converted salicylate in an oxygen-dependent but NAD(P)H-independent reaction to a product with an absorbance maximum at 283 nm. This metabolite was isolated, purified, and identified by mass spectrometry and (1)H and (13)C nuclear magnetic resonance spectroscopy as 2-oxohepta-3,5-dienedioic acid. This metabolite could be formed only by direct ring fission of salicylate by a 1,2-dioxygenase reaction. Cell extracts from P. salicylatoxidans also oxidized 5-aminosalicylate, 3-, 4-, and 5-chlorosalicylate, 3-, 4-, and 5-methylsalicylate, 3- and 5-hydroxysalicylate (gentisate), and 1-hydroxy-2-naphthoate. The dioxygenase was purified and shown to consist of four identical subunits with a molecular weight of about 45,000. The purified enzyme showed higher catalytic constants with gentisate or 1-hydroxy-2-naphthoate than with salicylate. It was therefore concluded that P. salicylatoxidans synthesized a gentisate 1,2-dioxygenase with an extraordinary substrate range, which also allowed the oxidation of salicylate. | lld:pubmed |
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| pubmed-article:11698383 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11698383 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11698383 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11698383 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11698383 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11698383 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:11698383 | pubmed:issn | 0021-9193 | lld:pubmed |
| pubmed-article:11698383 | pubmed:author | pubmed-author:StormTT | lld:pubmed |
| pubmed-article:11698383 | pubmed:author | pubmed-author:StollSS | lld:pubmed |
| pubmed-article:11698383 | pubmed:author | pubmed-author:LechnerCC | lld:pubmed |
| pubmed-article:11698383 | pubmed:author | pubmed-author:KEMPTT | lld:pubmed |
| pubmed-article:11698383 | pubmed:author | pubmed-author:RiegertUU | lld:pubmed |
| pubmed-article:11698383 | pubmed:author | pubmed-author:ReemtsmaTT | lld:pubmed |
| pubmed-article:11698383 | pubmed:author | pubmed-author:HintnerJ PJP | lld:pubmed |
| pubmed-article:11698383 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11698383 | pubmed:volume | 183 | lld:pubmed |
| pubmed-article:11698383 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11698383 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11698383 | pubmed:pagination | 6936-42 | lld:pubmed |
| pubmed-article:11698383 | pubmed:dateRevised | 2010-9-14 | lld:pubmed |
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| pubmed-article:11698383 | pubmed:meshHeading | pubmed-meshheading:11698383... | lld:pubmed |
| pubmed-article:11698383 | pubmed:meshHeading | pubmed-meshheading:11698383... | lld:pubmed |
| pubmed-article:11698383 | pubmed:meshHeading | pubmed-meshheading:11698383... | lld:pubmed |
| pubmed-article:11698383 | pubmed:meshHeading | pubmed-meshheading:11698383... | lld:pubmed |
| pubmed-article:11698383 | pubmed:meshHeading | pubmed-meshheading:11698383... | lld:pubmed |
| pubmed-article:11698383 | pubmed:meshHeading | pubmed-meshheading:11698383... | lld:pubmed |
| pubmed-article:11698383 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11698383 | pubmed:articleTitle | Direct ring fission of salicylate by a salicylate 1,2-dioxygenase activity from Pseudaminobacter salicylatoxidans. | lld:pubmed |
| pubmed-article:11698383 | pubmed:affiliation | Institut für Mikrobiologie, Universität Stuttgart, Allmandring 31, 70569 Stuttgart, Germany. | lld:pubmed |
| pubmed-article:11698383 | pubmed:publicationType | Journal Article | lld:pubmed |
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