| pubmed-article:9878353 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9878353 | lifeskim:mentions | umls-concept:C1002597 | lld:lifeskim |
| pubmed-article:9878353 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:9878353 | lifeskim:mentions | umls-concept:C1517495 | lld:lifeskim |
| pubmed-article:9878353 | lifeskim:mentions | umls-concept:C1157853 | lld:lifeskim |
| pubmed-article:9878353 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:9878353 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:9878353 | pubmed:dateCreated | 1999-3-12 | lld:pubmed |
| pubmed-article:9878353 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9878353 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9878353 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9878353 | pubmed:abstractText | Arthrobacter nicotinovorans is a Gram-positive aerobic soil bacterium able to grow on nicotine as its sole source of carbon and nitrogen. The initial steps of nicotine catabolism are catalyzed by nicotine dehydrogenase, the l- and d-specific 6-hydroxynicotine oxidases, and ketone dehydrogenase. The genes encoding these enzymes reside on a 160 kb plasmid, pAO1. The cccDNA of this plasmid was isolated in high purity and reasonable yield. It served as template material for the construction of a lambda-phage DNA library of the plasmid. The genes coding for 6-hydroxy-l-nicotine oxidase and for the subunits of the heterotrimeric ketone dehydrogenase were identified, subcloned and sequenced. The 6-hlno gene was identified as a 1278 bp open reading frame; its regulatory elements were also recognized. The derived primary structure of the monomer of apo-6-hydroxy-l-nicotine oxidase (46,264.5 Da) agrees with the data obtained by partial amino acid sequencing. 6-Hydroxy-l-nicotine oxidase and 6-hydroxy-d-nicotine oxidase were expressed in Escherichia coli and obtained in a state of high purity and crystallized. Ketone dehydrogenase (KDH) was found to be a heterotrimer with subunits of molecular mass 89,021.71, 26,778.65 and 17,638.88. The genes of KDH-A and KDH-B are juxtaposed; the A of the stop codon of KDH-A is used in the start codon of KDH-B, eliciting a frame shift. KDH-C is separated from KDH-A by 281 bp. | lld:pubmed |
| pubmed-article:9878353 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9878353 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9878353 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9878353 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9878353 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9878353 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9878353 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9878353 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9878353 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9878353 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:9878353 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:9878353 | pubmed:author | pubmed-author:KraussBB | lld:pubmed |
| pubmed-article:9878353 | pubmed:author | pubmed-author:SchenkSS | lld:pubmed |
| pubmed-article:9878353 | pubmed:author | pubmed-author:DeckerKK | lld:pubmed |
| pubmed-article:9878353 | pubmed:author | pubmed-author:HoelzAA | lld:pubmed |
| pubmed-article:9878353 | pubmed:copyrightInfo | Copyright 1998 Academic Press | lld:pubmed |
| pubmed-article:9878353 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9878353 | pubmed:day | 18 | lld:pubmed |
| pubmed-article:9878353 | pubmed:volume | 284 | lld:pubmed |
| pubmed-article:9878353 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9878353 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9878353 | pubmed:pagination | 1323-39 | lld:pubmed |
| pubmed-article:9878353 | pubmed:dateRevised | 2009-11-3 | lld:pubmed |
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| pubmed-article:9878353 | pubmed:meshHeading | pubmed-meshheading:9878353-... | lld:pubmed |
| pubmed-article:9878353 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9878353 | pubmed:articleTitle | Gene structures and properties of enzymes of the plasmid-encoded nicotine catabolism of Arthrobacter nicotinovorans. | lld:pubmed |
| pubmed-article:9878353 | pubmed:affiliation | Institute of Biochemistry and Molecular Biology, Albert-Ludwig University, Freiburg i.Br., Germany. | lld:pubmed |
| pubmed-article:9878353 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9878353 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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