A novel glycerophosphodiesterase from Bacillus pumilus. 
A novel glycerophosphodiesterase activity was detected in extracts from phosphate-starved Bacillus pumilus DSM27 cells.  The enzyme had a substrate specificity for glycerophosphodiester bonds and the reaction product formed with partially purified enzyme was (sn)-glycero-3-phosphate.  Purified cell wall teichoic acid of the polyglycerophosphate type, as well as deacylated, unsubstituted lipoteichoic acid of the polyglycerophosphate type, di(glycerophospho)glycerol (deacylated cardiolipin) and mono(glycerophospho)glycerol (deacylated phosphatidylglycerol) served as substrates for the enzyme.  Their native counterparts, however, cell wall-bound polyglycerophosphate, lipoteichoic acid (D-alanine substituted and dealanylated), cardiolipin and phosphatidylglycerol were poor or no substrates, respectively.  Enzyme activity was inhibited by purified cell walls and by heparin.  The enzyme was partially purified using a column of Heparin-Sepharose.