Jaisson, Stéphane
[UCL]
Veiga da Cunha, Maria
[UCL]
Van Schaftingen, Emile
[UCL]
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.
Bibliographic reference |
Jaisson, Stéphane ; Veiga da Cunha, Maria ; Van Schaftingen, Emile. Molecular identification of omega-amidase, the enzyme that is functionally coupled with glutamine transaminases, as the putative tumor suppressor Nit2.. In: Biochimie : an international journal of biochemistry and molecular biology, Vol. 91, no. 9, p. 1066-1071 (2009) |
Permanent URL |
http://hdl.handle.net/2078.1/22821 |