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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1999-3-12
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pubmed:databankReference | |
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.
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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/6-hydroxy-D-nicotine oxidase,
http://linkedlifedata.com/resource/pubmed/chemical/6-hydroxy-L-nicotine oxidase,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Enzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Ketone Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Nicotine,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases Acting on CH-NH...,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0022-2836
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 1998 Academic Press
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pubmed:issnType |
Print
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pubmed:day |
18
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pubmed:volume |
284
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1323-39
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pubmed:dateRevised |
2009-11-3
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pubmed:meshHeading |
pubmed-meshheading:9878353-Arthrobacter,
pubmed-meshheading:9878353-Bacterial Proteins,
pubmed-meshheading:9878353-Bacteriophage lambda,
pubmed-meshheading:9878353-Electrophoresis, Gel, Pulsed-Field,
pubmed-meshheading:9878353-Enzymes,
pubmed-meshheading:9878353-Escherichia coli,
pubmed-meshheading:9878353-Gene Library,
pubmed-meshheading:9878353-Ketone Oxidoreductases,
pubmed-meshheading:9878353-Molecular Sequence Data,
pubmed-meshheading:9878353-Nicotine,
pubmed-meshheading:9878353-Oxidoreductases,
pubmed-meshheading:9878353-Oxidoreductases Acting on CH-NH Group Donors,
pubmed-meshheading:9878353-Plasmids,
pubmed-meshheading:9878353-Recombinant Proteins,
pubmed-meshheading:9878353-Sequence Homology, Amino Acid
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pubmed:year |
1998
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pubmed:articleTitle |
Gene structures and properties of enzymes of the plasmid-encoded nicotine catabolism of Arthrobacter nicotinovorans.
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pubmed:affiliation |
Institute of Biochemistry and Molecular Biology, Albert-Ludwig University, Freiburg i.Br., Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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