Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2011-3-25
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1769-7123
pubmed:author
pubmed:copyrightInfo
Copyright © 2011 Institut Pasteur. Published by Elsevier SAS. All rights reserved.
pubmed:issnType
Electronic
pubmed:volume
162
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
285-91
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Homologous gene clusters of nicotine catabolism, including a new ?-amidase for ?-ketoglutaramate, in species of three genera of Gram-positive bacteria.
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
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't