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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
9
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pubmed:dateCreated |
2009-8-3
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pubmed:abstractText |
Our purpose was to identify the sequence of omega-amidase, which hydrolyses the amide group of alpha-ketoglutaramate, a product formed by glutamine transaminases. In the Bacillus subtilis genome, the gene encoding a glutamine transaminase (mtnV) is flanked by a gene encoding a putative 'carbon-nitrogen hydrolase'. The closest mammalian homolog of this putative bacterial omega-amidase is 'nitrilase 2', whose size and amino acid composition were in good agreement with those reported for purified rat liver omega-amidase. Mouse nitrilase 2 was expressed in Escherichia coli, purified and shown to catalyse the hydrolysis of alpha-ketoglutaramate and other known substrates of omega-amidase. No such activity was observed with mouse nitrilase 1. We conclude that mammalian nitrilase 2 is omega-amidase.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1638-6183
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
91
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1066-71
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pubmed:meshHeading |
pubmed-meshheading:19596042-Amidohydrolases,
pubmed-meshheading:19596042-Amino Acid Sequence,
pubmed-meshheading:19596042-Aminohydrolases,
pubmed-meshheading:19596042-Animals,
pubmed-meshheading:19596042-Bacillus subtilis,
pubmed-meshheading:19596042-Bacterial Proteins,
pubmed-meshheading:19596042-Blotting, Western,
pubmed-meshheading:19596042-Cell Line,
pubmed-meshheading:19596042-Computational Biology,
pubmed-meshheading:19596042-Databases, Genetic,
pubmed-meshheading:19596042-Escherichia coli,
pubmed-meshheading:19596042-Genome, Bacterial,
pubmed-meshheading:19596042-Humans,
pubmed-meshheading:19596042-Ketoglutaric Acids,
pubmed-meshheading:19596042-Mice,
pubmed-meshheading:19596042-Models, Genetic,
pubmed-meshheading:19596042-Molecular Sequence Data,
pubmed-meshheading:19596042-Sequence Homology, Amino Acid,
pubmed-meshheading:19596042-Transaminases
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pubmed:year |
2009
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pubmed:articleTitle |
Molecular identification of omega-amidase, the enzyme that is functionally coupled with glutamine transaminases, as the putative tumor suppressor Nit2.
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pubmed:affiliation |
Laboratory of Physiological Chemistry, De Duve Institute, Université Catholique de Louvain, B-1200 Brussels, Belgium.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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