Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Valentin, E.; Lambeau, G.
    What can venom phospholipases A2 tell us about the functional diversity of mammalian secreted phospholipases A2? (2000), Biochimie, 82, 815-831.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.4
-
 Pandinus imperator
3.1.1.4
-
 Pseudonaja textilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.1.4 Ca2+ dependent Apis mellifera
3.1.1.4 Ca2+ dependent Crotalus atrox
3.1.1.4 Ca2+ dependent Exaiptasia diaphana
3.1.1.4 Ca2+ dependent Mammalia
3.1.1.4 Ca2+ dependent Pandinus imperator
3.1.1.4 Ca2+ dependent Pseudonaja textilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.1.4 43000
-
 44000 Da and 43000 Da Exaiptasia diaphana
3.1.1.4 44000
-
 44000 Da and 43000 Da Exaiptasia diaphana

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.1.4 additional information Mammalia role in the digestion of prey, neurotoxic, myotoxic, cardiotoxic and cytotoxic activities, can have convulsant, hypotensive and proinflammatory effects, can affect blood coagulation and platelet aggregation, some forms can induce cell proliferation, cell migration and antibacterial activity. Mechanism of action can involve: the intrinsic catalytic activity of vPLA2, i.e. its ability to release potent biologically active fatty acids and lysophospholipids from membrane lipids, the interfacial binding to the membrane lipid bilayer which, without any phospholipid hydrolysis, may affect cellular functions by perturbing cellular membranes, and the binding to specific proteins located at the cell surface ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.4 Apis mellifera P00630 bee
-
3.1.1.4 Crotalus atrox
-
-
-
3.1.1.4 Exaiptasia diaphana
-
 sea anemone
-
3.1.1.4 Mammalia
-
-
-
3.1.1.4 Pandinus imperator
-
 scorpion
-
3.1.1.4 Pseudonaja textilis
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.1.4 proteolytic modification enzyme has an uncleaved propeptide sequence with is catalytically inactive Pseudonaja textilis

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.4
-
 Exaiptasia diaphana

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.1.4 venom
-
 Mammalia
-
3.1.1.4 venom
-
 Apis mellifera
-
3.1.1.4 venom
-
 Pandinus imperator
-
3.1.1.4 venom
-
 Pseudonaja textilis
-
3.1.1.4 venom
-
 Crotalus atrox
-
3.1.1.4 venom
-
 Exaiptasia diaphana
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.4 additional information role in the digestion of prey, neurotoxic, myotoxic, cardiotoxic and cytotoxic activities, can have convulsant, hypotensive and proinflammatory effects, can affect blood coagulation and platelet aggregation, some forms can induce cell proliferation, cell migration and antibacterial activity. Mechanism of action can involve: the intrinsic catalytic activity of vPLA2, i.e. its ability to release potent biologically active fatty acids and lysophospholipids from membrane lipids, the interfacial binding to the membrane lipid bilayer which, without any phospholipid hydrolysis, may affect cellular functions by perturbing cellular membranes, and the binding to specific proteins located at the cell surface Mammalia ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.1.4 dimer homodimer Crotalus atrox

Synonyms

EC Number Synonyms Comment Organism
3.1.1.4 imperatoxin
-
 Pandinus imperator
3.1.1.4 notexinII-1
-
 Mammalia
3.1.1.4 phospholipin
-
 Pandinus imperator
3.1.1.4 taipoxin
-
 Mammalia
3.1.1.4 textilotoxin
-
 Pseudonaja textilis