Alkaline phosphatase possessing alkaline phosphodiesterase activity and other phosphodiesterases in Bacillus subtilis.

摘要: In Bacillus subtilis Marburg strain, single-point mutations in the phoP locus brought about simultaneous losses of major activities alkaline phosphatase (APase) and phosphodiesterase (APDase). Revertants recovered two activities. APases with APDase activity were purified from membrane fraction B. 6160-BC6 culture fluid an APase-secreting mutant RAN 1. addition to these activity, at least kinds (PDase) without found cytoplasmic supernatants 1 APase-less SP25. Another minor APase a molecular weight 80,000, which had almost no PDase was isolated strain 6160-BC6. Enzyme distribution subcellular fractions various strains cultured high- low-phosphate media analyzed. The PDases did not cross-react rabbit antiserum against activity. main component 80,000 most active pH 8.0. These results suggest that is different detected structural gene for phosphate-repressible