PMID: 8948489Nov 14, 1996Paper

Vanadate is a potent competitive inhibitor of phospholipase C from Bacillus cereus

Biochimica Et Biophysica Acta
C A Tan, M F Roberts

Abstract

Monomeric vanadate is a potent competitive inhibitor of phospholipase C from Bacillus cereus, much better than other oxyanions (e.g., phosphate or iodate). The apparent efficiency of inhibition depends on the substrate aggregate structure. The measured inhibition constant with respect to monomeric phosphatidylcholine substrate is 0.21 mM under conditions where the K(m) is 0.12 mM; for micellar substrate the apparent Ki appears much lower and in fact tracks the apparent K(m) which decreases 10-fold. Vanadate inhibition is removed by addition of exogenous diacylglycerol, which by itself is an inhibitor. In contrast to its effect with monomeric or micellar substrate, vanadate does not strongly inhibit the PLC-catalyzed hydrolysis of small unilamellar vesicles of phosphatidylcholine. These results are interpreted in terms of the surface binding of the enzyme. Because of its ability to mimic the transition state of phosphate ester hydrolysis vanadate is also used to investigate the constraints on the occurrence of strained cyclic intermediates in phospholipid hydrolysis by PLC.

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Citations

Feb 26, 2013·Cell·Cornelia G SpruijtMichiel Vermeulen
Dec 4, 2012·Molecular Cell·Joshua C BlackJohnathan R Whetstine
Jul 10, 2012·Cell Metabolism·Chao Lu, Craig B Thompson
Jul 24, 2013·Journal of Genetics and Genomics = Yi Chuan Xue Bao·Feng LiShimin Zhao
Jun 6, 2015·Molecular Cell·Athanasios Ploumakis, Mathew L Coleman
Jun 10, 2006·The Biochemical Journal·Isabelle Bougie, Martin Bisaillon
Oct 8, 2003·The Journal of Immunology : Official Journal of the American Association of Immunologists·Jose ZamoranoAchsah D Keegan
Mar 30, 2004·Archives of Biochemistry and Biophysics·Shinobu FujiiKiyoshi Ikeda
Nov 13, 2010·Bioorganic & Medicinal Chemistry·Patricia González-BulnesAmadeu Llebaria

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