TAILIEUCHUNG - Báo cáo khoa học: Purification and characterization of Helicobacter pylori arginase, RocF: unique features among the arginase superfamily

The urea cycle enzyme arginase (EC ) hydrolyzes L-arginine to L-ornithine and urea. Mammalian arginases require manganese, have a highly alkaline pH optimum and are resistant to reducing agents. The gastric human pathogen,Helicobacter pylori, also has a complete urea cycle and contains therocFgene encoding arginase (RocF), which is involved in the pathogenesis ofH. pyloriinfection. Its arginase is specifically involved in acid resistance and inhibits host nitric oxide production. | Eur. J. Biochem. 271 1952-1962 2004 FEBS 2004 doi Purification and characterization of Helicobacter pylori arginase RocF unique features among the arginase superfamily David J. McGee1 Jovanny Zabaleta2 Ryan J. Viator3 Traci L. Testerman1 Augusto C. Ochoa2 4 and George L. Mendz5 1 Department of Microbiology Immunology University of South Alabama College of Medicine Mobile AL USA 2Department of Pathology and Tumor Immunology Program Stanley S. Scott Cancer Center Louisiana State University Health Sciences Center New Orleans LA USA 3Department of Biological Sciences University of South Alabama College of Arts Sciences Mobile AL USA 4Tumor Immunology Program Stanley S. Scott Cancer Center and Department of Pediatrics Louisiana State University Health Sciences Center New Orleans LA USA 5School of Biotechnology and Biomolecular Sciences University of New South Wales Sydney NSW Australia The urea cycle enzyme arginase EC hydrolyzes L-arginine to L-ornithine and urea. Mammalian arginases require manganese have a highly alkaline pH optimum and are resistant to reducing agents. The gastric human pathogen Helicobacter pylori also has a complete urea cycle and contains the rocF gene encoding arginase RocF which is involved in the pathogenesis of H. pylori infection. Its arginase is specifically involved in acid resistance and inhibits host nitric oxide production. The rocF gene was found to confer arginase activity to Escherichia coli disruption of plasmid-borne rocF abolished arginase activity. A translationally fused His6-RocF was purified from E. coli under nondenaturing conditions and had catalytic activity. Remarkably the purified enzyme had an acidic pH optimum of . Both purified arginase and arginasecontaining H. pylori extracts exhibited optimal catalytic activity with cobalt as a metal cofactor manganese and nickel were significantly less efficient in catalyzing the hydrolysis of arginine. Viable H. pylori or E. coli .

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