Title : RhoA activates purified phospholipase C-epsilon by a guanine nucleotide-dependent mechanism.

Pub. Date : 2004 Nov 12

PMID : 15322077






1 Functional Relationships(s)
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1 Similar to the enzymatic profiles of previously purified PLC-beta isozymes, the purified fragment of PLC-epsilon maximally hydrolyzed phosphatidylinositol 4-phosphate at a rate of approximately 10 mumol/mg of protein/min, exhibited phospholipase activity dependent on the concentration of free calcium, and favored phosphatidylinositol 4,5-bisphosphate as substrate relative to other phosphoinositides. Calcium phospholipase C like 1 (inactive) Homo sapiens