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Literature summary extracted from

  • Trummal, K.; Aaspollu, A.; Tonismaegi, K.; Samel, M.; Subbi, J.; Siigur, J.; Siigur, E.
    Phosphodiesterase from Vipera lebetina venom - structure and characterization (2014), Biochimie, 106, 48-55.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.15.1 DNA and amino acid sequence determination and analysis, phylogenetic tree Macrovipera lebetina

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.15.1 extracellular
-
 Macrovipera lebetina
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.15.1 60000
-
 reduced enzyme Macrovipera lebetina
3.1.15.1 93860
-
 sequence calculation Macrovipera lebetina
3.1.15.1 120000
-
 non-reduced enzyme Macrovipera lebetina

Organism

EC Number Organism UniProt Comment Textmining
3.1.15.1 Macrovipera lebetina W8E7D1 i.e. Macrovipera lebetina
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.15.1 proteolytic modification the enzyme is synthesized as a 828-amino acid single-chain protein but subsequently cleaved to form a two-chain protein held together with disulfide bonds Macrovipera lebetina

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.15.1 native extracellular enzyme from venom 3.2fold by gel filtration, and two different steps of anion exchange chromatography Macrovipera lebetina

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.15.1 venom
-
 Macrovipera lebetina
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.15.1 4-nitrophenyl thymidine-5'-phosphate + H2O best substrate Macrovipera lebetina 4-nitrophenol + thymidine-5'-phosphate
-
 ?
3.1.15.1 ADP + H2O
-
 Macrovipera lebetina AMP + phosphate
-
 ?
3.1.15.1 bis(p-nitrophenyl)phosphate + H2O good substrate Macrovipera lebetina ?
-
 ?
3.1.15.1 additional information the enzyme hydrolyses ADP but not ATP and 5'-AMP, the enzyme inhibits aggregation of platelets induced by ADP or collagen Macrovipera lebetina ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.15.1 More the enzyme is synthesized as a 828-amino acid single-chain protein but subsequently cleaved to form a two-chain protein held together with disulfide bonds, nevertheless the enzyme behaves like a heterodimeric protein with 60000 kDa subunits, molecular modelling. The enzyme contains four domains including two somatomedin-B domains, a PDE/nucleotide pyrophosphatase domain, and a nonspecific endonuclease domain Macrovipera lebetina

Synonyms

EC Number Synonyms Comment Organism
3.1.15.1 VLPDE
-
 Macrovipera lebetina

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.15.1 60
-
-
 Macrovipera lebetina

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.15.1 8.5 9
-
 Macrovipera lebetina

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.1.15.1 Macrovipera lebetina sequence calculation
-
 6.87

General Information

EC Number General Information Comment Organism
3.1.15.1 additional information enzyme secondary structure molecular modelling Macrovipera lebetina