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Literature summary for 3.1.1.4 extracted from

  • Damico, D.C.; Lilla, S.; de Nucci, G.; Ponce-Soto, L.A.; Winck, F.V.; Novello, J.C.; Marangoni, S.
    Biochemical and enzymatic characterization of two basic Asp49 phospholipase A2 isoforms from Lachesis muta muta (Surucucu) venom (2005), Biochim. Biophys. Acta, 1726, 75-86.
    View publication on PubMed
Search for more literature for 3.1.1.4

Inhibitors

Inhibitors Comment Organism Structure
crotapotin inhibitory to isoform LmTX-I Lachesis muta muta
Cu2+
-
 Lachesis muta muta
Zn2+
-
 Lachesis muta muta

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required Lachesis muta muta

Organism

Organism UniProt Comment Textmining
Lachesis muta muta
-
 isoforms LmTX-1, LmTX-II
-

Source Tissue

Source Tissue Comment Organism Textmining
venom
-
 Lachesis muta muta
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
? x * 14254.4, isoform LmTX-I, x * 14186.2, isoform LmTX-II, ESI/MS Lachesis muta muta

Synonyms

Synonyms Comment Organism
LmTX-I
-
 Lachesis muta muta
LmTX-II
-
 Lachesis muta muta

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35 45
-
 Lachesis muta muta

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
 Lachesis muta muta

pI Value

Organism Comment pI Value Maximum pI Value
Lachesis muta muta isoform LmTX-II, isoelectric focusing
-
 8.6
Lachesis muta muta isoform LmTX-I, isoelectric focusing
-
 8.7