Enzymes
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Reaction participants Show >> << Hide
- Name help_outline a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) Identifier CHEBI:57880 Charge -1 Formula C11H16O13PR2 SMILEShelp_outline [C@@H]1([C@@H]([C@@H]([C@@H]([C@H]([C@@H]1O)O)O)O)OP(OC[C@@H](COC(=O)*)OC(=O)*)(=O)[O-])O 2D coordinates Mol file for the small molecule Search links Involved in 74 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,204 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a 1-acyl-sn-glycero-3-phospho-(1D-myo-inositol) Identifier CHEBI:64771 Charge -1 Formula C10H17O12PR SMILEShelp_outline O[C@H](COC([*])=O)COP([O-])(=O)O[C@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 22 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a fatty acid Identifier CHEBI:28868 Charge -1 Formula CO2R SMILEShelp_outline [O-]C([*])=O 2D coordinates Mol file for the small molecule Search links Involved in 1,526 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:18001 | RHEA:18002 | RHEA:18003 | RHEA:18004 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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More general form(s) of this reaction
Publications
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On the specificity of a phospholipase A2 purified from the 106,000 X g pellet of bovine brain.
Gray N.C., Strickland K.P.
Assessment has been made of the specificity of a purified phospholipase A2 from the 106,000 X g pellet (microsomal fraction) of bovine grey matter which shows strong activity toward phosphatidylinositol (PI). In the first series of experiments involving the utilization as substrates of PI with dif ... >> More
Assessment has been made of the specificity of a purified phospholipase A2 from the 106,000 X g pellet (microsomal fraction) of bovine grey matter which shows strong activity toward phosphatidylinositol (PI). In the first series of experiments involving the utilization as substrates of PI with different 14C- or 3H-labeled fatty acids in the 2-position, the purified phospholipase A2 most readily removed 16:0 palmitic acid, followed by 18:0 stearic acid, 18:1 oleic acid and 20:4 arachidonic acid. In the second series of experiments, the purified phospholipase A2 showed preferential action toward PI (100%) compared to phosphatidylcholine (PC, 62.5%), phosphatidic acid (PA, 32.6%), phosphatidylethanolamine (PE, 25.1%) and phosphatidylserine (PS, 21.5%), where each phosphoglyceride was labeled in the 2-position with [1-14C] oleic acid. In the third series of experiments, fatty acids were shown to cause inhibition of action of the purified phospholipase A2 on 1-acyl, 2-[1-14C] oleoyl PI in the order 20:4 greater than 18:1 greater than 18:0 greater than 16:0 which is the reverse order to that just noted. In the final series of experiments, the addition of the phosphoglycerides PC, PE, PS and PA in amounts of 5 or 10 microM caused either no inhibition (PE, 2%), slight inhibition (PC, 15%) or reasonably significant inhibition (PA, 20% and PS, 40%) of action of the purified phospholipase A2 on 1-acyl, 2-[1-14C]-oleoyl PI. The pattern of specificity observed for the purified phospholipase A2 combined with its microsomal location are the expected properties of a phospholipase A2 that might function in a deacylation-reacylation cycle for modifying the fatty acid distribution in PI. << Less
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The purification and characterization of a phospholipase A2 activity from the 106,000 X g pellet (microsomal fraction) of bovine brain acting on phosphatidylinositol.
Gray N.C., Strickland K.P.
Can J Biochem 60:108-117(1982) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.