Acid and alkaline phosphatases of Capnocytophaga species. I. Production and cytological localization of the enzymes.
The two hydrolytic enzymes, acid (AcP; EC 3.1.3.2) and alkaline (AlP; EC 3.1.3.1) phosphatase, of the three types species of Capnocytophaga were examined. Both enzymes were produced constitutively, with their activity highest in C. ochracea strain 25. These two degradative enzymes (approximately 10% of the total activity) were released into the growth medium during the latter stages of growth, both as soluble and membrane-bound enzymes. When grown in the presence of high concentrations of organic phosphates, the synthesis and expression of AcP and AlP was unaltered. Cyto- and immuno-chemical localization situated the phosphatases in the periplasmic space, at the cell surface, and in membranous vesicles.
D000135:Acid Phosphatase / Q000096:biosynthesis / Q000378:metabolism*; D000469:Alkaline Phosphatase / Q000096:biosynthesis / Q000378:metabolism*; D002206:Capnocytophaga / Q000201:enzymology*; D002451:Cell Compartmentation; D003470:Culture Media; D041964:Cytophagaceae / Q000201:enzymology*; D004790:Enzyme Induction; D007700:Kinetics; D010710:Phosphates / Q000378:metabolism
D003470:Culture Media; D010710:Phosphates; D000469:Alkaline Phosphatase; D000135:Acid Phosphatase