A novel glycerophosphodiesterase from Bacillus pumilus

FEBS Letters

Fiedler, Franz¹  Kusser, Wolfgang¹ 

[1] Institut für Genetik und Mikrobiologie der Universität, Maria-Ward-Straβe 1a, D-800 München 19, FRG

关键词: Teichoic acid;    Teichoicase;    Lipoteichoic acid;    Phospholipid;    Phosphate starvation;   

DOI  :  10.1016/0014-5793(84)80100-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 substitued and dealanylated), cardiolipin and phosphatiylglycerol 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.

【 授权许可】

Unknown