Source:http://linkedlifedata.com/resource/pubmed/id/21288482
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2011-3-25
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pubmed:abstractText |
Gram-positive soil bacteria Arthrobacter nicotinovorans, Nocardioides sp. JS614 and Rhodococcus opacus were shown to contain similarly organized clusters of homologous genes for nicotine catabolism. An uncharacterized gene of a predicted nitrilase within these gene clusters was cloned from A. nicotinovorans and biochemical data unexpectedly showed that the protein exhibited ?-amidase activity toward ?-ketoglutaramate. Structural modelling of the protein suggested the presence of the catalytic triad Cys-Glu-Lys, characteristic of this class of enzymes, and supported ?-ketoglutaramate as substrate. A-ketoglutaramate could be generated by hydrolytic cleavage of the C-N bond of the trihydroxypyridine ring produced by nicotine catabolism in these bacteria. This ?-amidase, together with glutamate dehydrogenase, may form a physiologically relevant enzyme couple, leading to transformation of metabolically inert ?-ketoglutaramate derived from trihydroxypyridine into glutamate, a central compound of nitrogen metabolism.
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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/Amidohydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Ketoglutaric Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Nicotine,
http://linkedlifedata.com/resource/pubmed/chemical/alpha-ketoglutaramate,
http://linkedlifedata.com/resource/pubmed/chemical/amidase
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1769-7123
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pubmed:author | |
pubmed:copyrightInfo |
Copyright © 2011 Institut Pasteur. Published by Elsevier SAS. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:volume |
162
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
285-91
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pubmed:meshHeading |
pubmed-meshheading:21288482-Actinomycetales,
pubmed-meshheading:21288482-Amidohydrolases,
pubmed-meshheading:21288482-Arthrobacter,
pubmed-meshheading:21288482-Catalytic Domain,
pubmed-meshheading:21288482-Gene Order,
pubmed-meshheading:21288482-Ketoglutaric Acids,
pubmed-meshheading:21288482-Metabolic Networks and Pathways,
pubmed-meshheading:21288482-Models, Molecular,
pubmed-meshheading:21288482-Multigene Family,
pubmed-meshheading:21288482-Nicotine,
pubmed-meshheading:21288482-Protein Structure, Tertiary,
pubmed-meshheading:21288482-Rhodococcus
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pubmed:year |
2011
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pubmed:articleTitle |
Homologous gene clusters of nicotine catabolism, including a new ?-amidase for ?-ketoglutaramate, in species of three genera of Gram-positive bacteria.
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pubmed:affiliation |
Institute of Biochemistry and Molecular Biology, Centre for Biochemistry and Molecular Cell Research, Albert-Ludwigs University, Freiburg, Germany. cristina.cobzaru@biochemie.uni-freiburg.de
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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