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Article

Modulation of Bacillus thuringiensis phosphatidylinositol-specific phospholipase C activity by mutations in the putative dimerization interface.

The Journal of biological chemistry - 5 Jun 2009

Shi Xiaomeng, Shao Chenghua, Zhang Xin, Zambonelli Carlo, Redfield Alfred G, Head James F, Seaton Barbara A, Roberts Mary F

Abstract excerpt

Cleavage of phosphatidylinositol (PI) to inositol 1,2-(cyclic)-phosphate (cIP) and cIP hydrolysis to inositol 1-phosphate by Bacillus thuringiensis phosphatidylinositol-specific phospholipase C are activated by the enzyme binding to phosphatidylcholine (PC) surfaces. Part of this reflects improved binding of the protein to interfaces. However, crystallographic analysis of an interfacially impaired...

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Identifiers

PMID: 19369255
DOI: 10.1074/jbc.M901601200
PMCID: PMC2708857

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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