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

Jaisson, Stéphane;Veiga da Cunha, Maria;Van Schaftingen, Emile
(2009) Biochimie : an international journal of biochemistry and molecular biology — Vol. 91, n° 9, p. 1066-1071 (2009)

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  • Jaisson, StéphaneUCLouvain
    Author
  • Veiga da Cunha, MariaUCLouvain
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  • Van Schaftingen, EmileUCLouvain
    Author
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.
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Jaisson, S., Veiga da Cunha, M., & Van Schaftingen, E. (2009). Molecular identification of omega-amidase, the enzyme that is functionally coupled with glutamine transaminases, as the putative tumor suppressor Nit2. Biochimie : an international journal of biochemistry and molecular biology, 91(9), 1066-1071. https://doi.org/10.1016/j.biochi.2009.07.002 (Original work published 2009)