TAILIEUCHUNG - Báo cáo khoa học: UMP kinase from the Gram-positive bacterium Bacillus subtilis is strongly dependent on GTP for optimal activity

The gene encodingBacillus subtilisUMP kinase (pyrH/ smbA) is transcribed in vivo into a functional enzyme, which represents approximately of total soluble proteins. The specific activity of the purified enzyme under optimal conditions is 25 unitsÆmg )1 of protein. In the absenceofGTP,theactivityofB. subtilisenzyme is less than 10% of its maximum activity. Only dGTP and 3¢-anthraniloyl-2¢-deoxyguanosine-5¢-triphosphate (Ant-dGTP) can increase catalysis significantly. | Eur. J. Biochem. 270 _196 - _2 U 2003 FEBS 2003 doi UMP kinase from the Gram-positive bacterium Bacillussubtilis is strongly dependent on GTP for optimal activity Cristina Gaavi1. Nadia Bucurenci2 Ovidiu Sĩrbu1. Gilles Labesse3 Mihaela ionescu1. Auaustin Ofiteru2. BB B B M BM M wV V B w B B B B w w B B B VBB B F w B BB B w B F B B w w B B B B BB w B B B B B B BB BB B BB B Bf B B w B BBB BB w B B B B B F B B BB B w Liliane Assairi1. Stephanie Landais1. Antoine Danchin4 Octavian Barzu1 and Anne-Marie Gilles1 1 Laboratoire de Chimie Structurale des Macromolecules 4Unite de Genetique des Genomes Bacteriens Institut Pasteur Paris France 2Laboratory of Enzymology and Applied Microbiology Cantacuzino Institute Bucharest Romania 3Centre de Biochimie Structurale Faculte de Pharmacie Universite de Montpellier I Montpellier France The gene encoding Bacillus subtilis UMP kinase pyrH smbA is transcribed in vivo into a functional enzyme which represents approximately of total soluble proteins. The specific activity of the purified enzyme under optimal conditions is 25 units-mg-1 of protein. In the absence of GTP the activity of B. subtilis enzyme is less than 10 of its maximum activity. Only dGTP and 3 -anthraniloyl-2 -deoxyguanosine-5 -triphosphate Ant-dGTP can increase catalysis significantly. Binding of Ant-dGTP to B. subtilis UMP kinase increased the quantum yield of the fluorescent analogue by a factor of more than three. UTP and GTP completely displaced Ant-dGTP whereas GMP and UMP were ineffective. UTP inhibits UMP kinase of B. subtilis with a lower affinity than that shown towards the Escherichia coli enzyme. Among nucleoside monophosphates 5-fluoro-UMP 5F-UMP and 6-aza-UMP were actively phosphorylated by B. subtilis UMP kinase exi-Taining the ccootoxicity o t tile corresponding nucleosides towards this bacterium. A structural model of UMP kinase 01 1 on die coneer-vation of the fold of carbamate kinase and N-acetyl-glutamate kinase .

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