Molecular identification of omega-amidase, the enzyme that is functionally coupled with glutamine transaminases, as the putative tumor suppressor Nit2.

Abstract

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.

• Authors: Stéphane Jaisson, Maria Veiga-da-Cunha, Emile Van Schaftingen
• Journal: Biochimie (Biochimie) Vol. 91 Issue 9 Pg. 1066-71 (Sep 2009) ISSN: 1638-6183 [Electronic] France
• PMID: 19596042 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Bacterial Proteins
• Ketoglutaric Acids
• alpha-ketoglutaramate
• Transaminases
• glutamine-pyruvate aminotransferase
• Amidohydrolases
• omega-amidase
• Aminohydrolases

Topics

• Amidohydrolases (chemistry, genetics, metabolism)
• Amino Acid Sequence
• Aminohydrolases (chemistry, genetics, metabolism)
• Animals
• Bacillus subtilis (enzymology, genetics)
• Bacterial Proteins (chemistry, genetics, metabolism)
• Blotting, Western
• Cell Line
• Computational Biology
• Databases, Genetic
• Escherichia coli (genetics, metabolism)
• Genome, Bacterial (genetics)
• Humans
• Ketoglutaric Acids (metabolism)
• Mice
• Models, Genetic
• Molecular Sequence Data
• Sequence Homology, Amino Acid
• Transaminases (chemistry, genetics, metabolism)