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Background  Arginase (RocF) hydrolyzes L-arginine to L-ornithine and urea. While previously characterized arginases have an alkaline pH optimum and require activation with manganese, arginase from  Helicobacter pylori  is optimally active with cobalt at pH 6. The arginase from  Bacillus anthracis  is not well characterized; therefore, this arginase was investigated by a variety of strategies and the enzyme was purified.    Results  The  rocF  gene from  B. anthracis  was cloned and expressed in  E. coli  and compared with  E. coli  expressing  H. pylori rocF . In the native organisms  B. anthracis  arginase was up to 1,000 times more active than  H. pylori  arginase and displayed remarkable activity in the absence of exogenous metals, although manganese, cobalt, and nickel all improved activity. Optimal  B. anthracis  arginase activity occurred with nickel at an alkaline pH. Either  B. anthracis  arginase expressed in  E. coli  or purified  B. anthracis  RocF showed similar findings. The  B. anthracis  arginase expressed in  E. coli  shifted its metal preference from Ni > Co > Mn when assayed at pH 6 to Ni > Mn > Co at pH 9. Using a viable cell arginase assay,  B. anthracis  arginase increased dramatically when the cells were grown with manganese, even at final concentrations of <1 μM, whereas  B. anthracis  grown with cobalt or nickel (≥500 μM) showed no such increase, suggesting existence of a high affinity and specificity manganese transporter.    Conclusion  Unlike other eubacterial arginases,  B. anthracis  arginase displays unusual metal promiscuity. The unique properties of  B. anthracis  arginase may allow utilization of a specific metal, depending on the  in vivo  niches occupied by this organism.

Characterization of Bacillus anthracis arginase: effects of pH, temperature, and cell viability on metal preference