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Literature summary for 3.1.4.11 extracted from

  • Baumann, M.K.; Swann, M.J.; Textor, M.; Reimhult, E.
    Pleckstrin homology-phospholipase C-delta1 interaction with phosphatidylinositol 4,5-bisphosphate containing supported lipid bilayers monitored in situ with dual polarization interferometry (2011), Anal. Chem., 83, 6267-6274.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
enzyme expression in Escherichia coli strain BL21 (DE3) Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
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PH-PLCdelta1 residues 11-140
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O interaction analysis, modeling and binding kinetics of substrate and enzyme PH-PLCdelta1, overview. PH-PLCdelta1 binds specifically to 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate, breaking up clusters and expelling nonspecifically associated peptide from the surface Rattus norvegicus 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
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Synonyms

Synonyms Comment Organism
PH-PLCdelta1
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Rattus norvegicus
pleckstrin homology-phospholipase C-delta1
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Rattus norvegicus