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Literature summary extracted from

  • Nirmal, N.; Praba, G.O.; Velmurugan, D.
    Modeling studies on phospholipase A2-inhibitor complexes (2008), Indian J. Biochem. Biophys., 45, 256-262.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.1.1.4 drug development herbal compounds (acalyphin, chlorogenic acid, stigmasterol, curcumin and tectoridin) and marine compounds (gracilin A and aplysulphurin A) show favorable interactions with the amino acid residues at the active site of PLA2, thereby substantiating their proven efficacy as anti-inflammatory compounds and antidotes Bos taurus
3.1.1.4 drug development herbal compounds (acalyphin, chlorogenic acid, stigmasterol, curcumin and tectoridin) and marine compounds (gracilin A and aplysulphurin A) show favorable interactions with the amino acid residues at the active site of PLA2, thereby substantiating their proven efficacy as anti-inflammatory compounds and antidotes Daboia russelii

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.4 acalyphin from Acalypha indica, shows interaction with the amino acids at the active site of PLA2, interacts also with the Ca2+ ion in the active site of PLA2 Bos taurus
3.1.1.4 acalyphin from Acalypha indica, shows interaction with the amino acids (Asp-49, Lys-69 and Gly-30) at the active site of PLA2 Daboia russelii
3.1.1.4 aplysulphurin A from Aplysilla sp., shows interaction with the amino acids at the active site of PLA2, interacts also with the Ca2+ ion in the active site of PLA2 Bos taurus
3.1.1.4 aplysulphurin A from Aplysilla sp., shows interaction with the amino acids at the active site of PLA2 Daboia russelii
3.1.1.4 chlorogenic acid from Achillea millefolium, shows interaction with the amino acids at the active site of PLA2 Bos taurus
3.1.1.4 chlorogenic acid from Achillea millefolium, shows interaction with the amino acids (Asp-49, Lys-69, Trp-31 and Trp-A31) at the active site of PLA2 Daboia russelii
3.1.1.4 curcumin from Curcuma longa, shows interaction with the amino acids at the active site of PLA2 Bos taurus
3.1.1.4 curcumin from Curcuma longa, shows interaction with the amino acids (Asp-49 and Gly-30) at the active site of PLA2 Daboia russelii
3.1.1.4 gracilin A from Aplysilla sp., shows interaction with the amino acids at the active site of PLA2, interacts also with the Ca2+ ion in the active site of PLA2 Bos taurus
3.1.1.4 gracilin A from Aplysilla sp., shows interaction with the amino acids (Asp-49, His-48, Trp-31 and Gly-30) at the active site of PLA2 Daboia russelii
3.1.1.4 stigmasterol from Achillea millefolium, shows interaction with the amino acids at the active site of PLA2 Bos taurus
3.1.1.4 stigmasterol from Achillea millefolium, shows interaction with the amino acids (His-48) at the active site of PLA2 Daboia russelii
3.1.1.4 tectoridin from Belamcanda chinensis, shows interaction with the amino acids at the active site of PLA2 Bos taurus
3.1.1.4 tectoridin from Belamcanda chinensis, shows interaction with the amino acids (Asp-49 and Lys-69) at the active site of PLA2 Daboia russelii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.1.4 Ca2+ essential for catalysis and substrate binding Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.4 Bos taurus P00593
-
-
3.1.1.4 Daboia russelii P59071 Russell's viper
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.1.4 pancreas
-
 Bos taurus
-

Synonyms

EC Number Synonyms Comment Organism
3.1.1.4 phospholipase A2
-
 Bos taurus
3.1.1.4 phospholipase A2
-
 Daboia russelii
3.1.1.4 PLA2
-
 Bos taurus
3.1.1.4 PLA2
-
 Daboia russelii