PMID: 6319195Jan 30, 1984Paper

A novel glycerophosphodiesterase from Bacillus pumilus

FEBS Letters
W Kusser, F Fiedler


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.


Oct 1, 1978·Infection and Immunity·L J SilvestriA S Bleiweis
Aug 1, 1973·Analytical Biochemistry·N Blumenkrantz, G Asboe-Hansen
Jan 1, 1972·Proceedings of the National Academy of Sciences of the United States of America·E M WiseE Teimer
Nov 15, 1973·European Journal of Biochemistry·J C Le Hégarat, C Anagnostopoulos
Jul 1, 1983·European Journal of Biochemistry·W FischerR Haas
Jul 1, 1983·Journal of Bacteriology·W Kusser, F Fiedler
Feb 15, 1982·The Biochemical Journal·K JohnstoneD J Ellar
Apr 1, 1983·Journal of Bacteriology·G L Card, D J Finn


Jan 1, 2014·The FEBS Journal·Daniela CordaStefania Mariggiò
Jun 9, 2016·The Journal of Biological Chemistry·Anneleen CornelissenDouwe van Sinderen

Related Concepts

Glycerophosphodiester phosphodiesterase 2
Natto Bacteria
Cell Wall
Phosphoric diester hydrolase
Staphylococcus aureus
Substrate Specificity

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