A phosphoinositide phospholipase C subtype that is primarily regulated by PROTEIN-TYROSINE KINASES. It is structurally related to PHOSPHOLIPASE C DELTA with the addition of SRC HOMOLOGY DOMAINS and pleckstrin homology domains located between two halves of the CATALYTIC DOMAIN
Phospholipases A -- physiology : Phospholipase A2 : basic and clinical aspects in inflammatory diseases / volume editors, W. Uhl, T.J. Nevalainen, M.W. Büchler
A subclass of phospholipases that hydrolyze the phosphoester bond found in the third position of GLYCEROPHOSPHOLIPIDS. Although the singular term phospholipase C specifically refers to an enzyme that catalyzes the hydrolysis of PHOSPHATIDYLCHOLINE (EC 3.1.4.3), it is commonly used in the literature to refer to broad variety of enzymes that specifically catalyze the hydrolysis of PHOSPHATIDYLINOSITOLS
A subclass of phospholipases that hydrolyze the phosphoester bond found in the third position of GLYCEROPHOSPHOLIPIDS. Although the singular term phospholipase C specifically refers to an enzyme that catalyzes the hydrolysis of PHOSPHATIDYLCHOLINE (EC 3.1.4.3), it is commonly used in the literature to refer to broad variety of enzymes that specifically catalyze the hydrolysis of PHOSPHATIDYLINOSITOLS
Phospholipid antibodies -- Congresses : Antiphospholipid syndrome : insights and highlights from the 13th International Congress on Antiphospholipid Antibodies / Doruk Erkan, Silvia S. Pierangeli, editors
Phospholipids -- Analysis : Micro/nanoencapsulation of active food ingredients / Qingrong Huang, editor, Peter Given, editor, Michael Qian, editor ; sponsored by the ACS Division of Agricultural and Food Chemistry, Inc
Phospholipids -- chemistry : Micro/nanoencapsulation of active food ingredients / Qingrong Huang, editor, Peter Given, editor, Michael Qian, editor ; sponsored by the ACS Division of Agricultural and Food Chemistry, Inc
2009
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Phospholipids -- Congresses. : Phospholipids : characterization, metabolism, and novel biological applications : proceedings of the 6th International Colloquium / editors, Gregor Cevc, Fritz Paltauf
Derivatives of phosphatidic acids in which the phosphoric acid is bound in ester linkage to the hexahydroxy alcohol, myo-inositol. Complete hydrolysis yields 1 mole of glycerol, phosphoric acid, myo-inositol, and 2 moles of fatty acids
Derivatives of phosphatidic acids in which the phosphoric acid is bound in ester linkage to the hexahydroxy alcohol, myo-inositol. Complete hydrolysis yields 1 mole of glycerol, phosphoric acid, myo-inositol, and 2 moles of fatty acids
A group of enzymes removing the SERINE- or THREONINE-bound phosphate groups from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase. (Enzyme Nomenclature, 1992)
A group of enzymes removing the SERINE- or THREONINE-bound phosphate groups from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase. (Enzyme Nomenclature, 1992)
An enzyme group that specifically dephosphorylates phosphotyrosyl residues in selected proteins. Together with PROTEIN-TYROSINE KINASE, it regulates tyrosine phosphorylation and dephosphorylation in cellular signal transduction and may play a role in cell growth control and carcinogenesis