Acid Phosphatase in Dictyostelium discoideum

An acid phosphatase has been studied at various stages of development of Dictyostelium discoideum. This enzyme has a pH optimum of 3.6 and catalyses the hydrolysis of both hexose phosphates and mononucleotides as well as that of p-nitrophenyl phosphate. The enzyme specific activity increases 2–4 fold in vitro during differentiation, but the activity in vivo may be controlled through endproduct inhibition by orthophosphate, which accumulates in the cells during sorocarp formation. The predicted activity in vivo is highest in the middle of development, especially at the pre-culmination stage.