Literature summary for 3.1.4.11 extracted from

Kim, S.K.; Wee, S.M.; Chang, J.S.; Kwon, T.K.; Min do, S.; Lee, Y.H.; Suh, P.G.
Point mutations in the split PLC-gamma1 PH domain modulate phosphoinositide binding (2004), J. Biochem. Mol. Biol., 37, 720-725.

Search for more literature for 3.1.4.11

Cloned(Commentary)

Cloned (Comment)	Organism
expression in COS-7 cells	Rattus norvegicus

Protein Variants

Protein Variants	Comment	Organism
H503A	mutant enzyme shows reduced affinity for phosphoinositide binding and reduced hydrolysis of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate	Rattus norvegicus
P500A	mutant enzyme shows reduced affinity for phosphoinositide binding and reduced hydrolysis of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate	Rattus norvegicus

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	expression in COS-7 cells	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O	amino acids Pro500 and His503 are critical for binding of PLC-gamma1 to one of its substrates, 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate in the membrane	Rattus norvegicus	1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol	-	?

Synonyms

Synonyms	Comment	Organism
phospholipase C	-	Rattus norvegicus
PLC-gamma1	-	Rattus norvegicus

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Release 2023.1 (January 2023)