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Literature summary for 3.1.1.4 extracted from

  • Huancahuire-Vega, S.; Ponce-Soto, L.A.; Martins-de-Souza, D.; Marangoni, S.
    Biochemical and pharmacological characterization of PhTX-I a new myotoxic phospholipase A2 isolated from Porthidium hyoprora snake venom (2011), Comp. Biochem. Physiol. C, 154, 108-119.
    View publication on PubMed
Search for more literature for 3.1.1.4

Inhibitors

Inhibitors Comment Organism Structure
Cd2+
-
 Bothrocophias hyoprora
Mg2+
-
 Bothrocophias hyoprora
Mn2+
-
 Bothrocophias hyoprora
Zn2+
-
 Bothrocophias hyoprora

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.96
-
 4-nitro-3-(octanoyloxy) benzoic acid at pH 8.0, 37°C Bothrocophias hyoprora

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ dependent on Ca2+, full activity at 10 mM Bothrocophias hyoprora

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
14249
-
 x * 14249, MALDI-TOF mass spectrometry Bothrocophias hyoprora

Organism

Organism UniProt Comment Textmining
Bothrocophias hyoprora
-
-
-

Purification (Commentary)

Purification (Comment) Organism
gamma-Bondapack C18 column chromatography Bothrocophias hyoprora

Source Tissue

Source Tissue Comment Organism Textmining

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.3
-
 crude enzyme, in 10 mM Tris-HCl, 10 mM CaCl2 and 100 mM NaCl, pH 8.0, at 37°C Bothrocophias hyoprora
408.3
-
 after 1361.7fold purification, in 10 mM Tris-HCl, 10 mM CaCl2 and 100 mM NaCl, pH 8.0, at 37°C Bothrocophias hyoprora

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitro-3-(octanoyloxy) benzoic acid + H2O
-
 Bothrocophias hyoprora 3-hydroxy-4-nitrobenzoate + octanoate
-
 ?

Subunits

Subunits Comment Organism
? x * 14249, MALDI-TOF mass spectrometry Bothrocophias hyoprora

Synonyms

Synonyms Comment Organism
myotoxic phospholipase A2
-
 Bothrocophias hyoprora
PLA2
-
 Bothrocophias hyoprora
TX-I
-
 Bothrocophias hyoprora

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35 45
-
 Bothrocophias hyoprora

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
 Bothrocophias hyoprora

General Information

General Information Comment Organism
physiological function ex vivo, whole venom and TX-I phospholipases A2 cause blockade of the neuromuscular transmission in young chick biventer cervicis preparations similar to other isolated snake venom toxins from the Bothrops genus. In vivo, both induce local myotoxicity and systemic interleukin-6 response upon intramuscular injection, additionally, induce moderate footpad edema. In vitro, both induce low cytotoxicity in skeletal muscle myoblasts, however TX-I phospholipases A2 is able to lyse myotubes Bothrocophias hyoprora