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Literature summary for 3.1.1.4 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

Application Comment Organism
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
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

Inhibitors Comment Organism Structure
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
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
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
aplysulphurin A from Aplysilla sp., shows interaction with the amino acids at the active site of PLA2 Daboia russelii
chlorogenic acid from Achillea millefolium, shows interaction with the amino acids at the active site of PLA2 Bos taurus
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
curcumin from Curcuma longa, shows interaction with the amino acids at the active site of PLA2 Bos taurus
curcumin from Curcuma longa, shows interaction with the amino acids (Asp-49 and Gly-30) at the active site of PLA2 Daboia russelii
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
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
stigmasterol from Achillea millefolium, shows interaction with the amino acids at the active site of PLA2 Bos taurus
stigmasterol from Achillea millefolium, shows interaction with the amino acids (His-48) at the active site of PLA2 Daboia russelii
tectoridin from Belamcanda chinensis, shows interaction with the amino acids at the active site of PLA2 Bos taurus
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

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

Organism

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

Source Tissue

Source Tissue Comment Organism Textmining
pancreas
-
Bos taurus
-

Synonyms

Synonyms Comment Organism
phospholipase A2
-
Bos taurus
phospholipase A2
-
Daboia russelii
PLA2
-
Bos taurus
PLA2
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Daboia russelii