期刊
BIOCHIMIE
卷 91, 期 9, 页码 1066-1071出版社
ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
DOI: 10.1016/j.biochi.2009.07.002
关键词
omega-Amidase; Nitrilase 2; alpha-Ketoglutaramate; Glutamine transaminases
资金
- Belgian 'Fonds National de la Recherche Scientifique' (FNRS)
- Interuniversity Attraction Pole Programme - Belgian Science Policy [P6/05]
- 'Association de Langue Francaise pour l'etude du Diabete et des Maladies Metaboliques' (ALFEDIAM)
- 'Region Champagne-Ardenne' (France)
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. (C) 2009 Elsevier Masson SAS. All rights reserved.
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