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Literature summary for 3.1.15.1 extracted from

  • Peng, L.; Xu, X.; Guo, M.; Yan, X.; Wang, S.; Gao, S.; Zhu, S.
    Effects of metal ions and disulfide bonds on the activity of phosphodiesterase from Trimeresurus stejnegeri venom (2013), Metallomics, 5, 920-927.
    View publication on PubMed
Search for more literature for 3.1.15.1

Inhibitors

Inhibitors Comment Organism Structure
Cu2+ required for activity, but inhibitory at 1 mM, two Cu2+ binding sites. Cu2+ ions function as a switch for its phosphodiesterase activity Trimeresurus stejnegeri
dithiothreitol inhibits the phosphodiesterase activity of the enzyme by reducing both the Cu2+ and disulfide bonds Trimeresurus stejnegeri
glutathione endogenous inhibitor, inhibits the phosphodiesterase activity of the enzyme by reducing both the Cu2+ and disulfide bonds Trimeresurus stejnegeri
L-ascorbate endogenous inhibitor, inhibits the phosphodiesterase activity of the enzyme through reduction of Cu2+ Trimeresurus stejnegeri
tris(2-carboxyethyl)phosphine inhibits the phosphodiesterase activity of the enzyme by reducing both the Cu2+ and disulfide bonds Trimeresurus stejnegeri

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Trimeresurus stejnegeri
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activates Trimeresurus stejnegeri
Co2+ activates Trimeresurus stejnegeri
Cu2+ required for activity, but inhibitory at 1 mM, two Cu2+ binding sites. Cu2+ ions function as a switch for its phosphodiesterase activity Trimeresurus stejnegeri
Mg2+ activates Trimeresurus stejnegeri
Mn2+ activates Trimeresurus stejnegeri
additional information analysis of the effects of metal ions and small-molecule reductants on the enzyme's structure and activity, overview. Mg2+, Mn2+, Ni2+, Co2+ and Ca2+ can partiallyy substitute for Cu2+ and Zn2+ Trimeresurus stejnegeri
Ni2+ activates Trimeresurus stejnegeri
Zn2+ required for activity, one Zn2+ binding site Trimeresurus stejnegeri

Organism

Organism UniProt Comment Textmining
Trimeresurus stejnegeri
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
 Trimeresurus stejnegeri
-
venom
-
 Trimeresurus stejnegeri
-

Synonyms

Synonyms Comment Organism
PDE
-
 Trimeresurus stejnegeri
TS-PDE
-
 Trimeresurus stejnegeri

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Trimeresurus stejnegeri

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Trimeresurus stejnegeri

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
1.48
-
 holo-enzyme containing Cu2+ and Zn2+, pH 7.4, 37°C Trimeresurus stejnegeri tris(2-carboxyethyl)phosphine
1.84
-
 enzyme containing only Zn2+, pH 7.4, 37°C Trimeresurus stejnegeri tris(2-carboxyethyl)phosphine
2.56
-
 holo-enzyme containing Cu2+ and Zn2+, pH 7.4, 37°C Trimeresurus stejnegeri glutathione
2.87
-
 holo-enzyme containing Cu2+ and Zn2+, pH 7.4, 37°C Trimeresurus stejnegeri L-ascorbate
3.45
-
 enzyme containing only Zn2+, pH 7.4, 37°C Trimeresurus stejnegeri glutathione
6.9
-
 holo-enzyme containing Cu2+ and Zn2+, pH 7.4, 37°C Trimeresurus stejnegeri dithiothreitol
8.62
-
 enzyme containing only Zn2+, pH 7.4, 37°C Trimeresurus stejnegeri dithiothreitol

General Information

General Information Comment Organism
additional information the catalytic activity of the enzyme relies on its disulfide bonds and bimetallic cluster Trimeresurus stejnegeri