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Literature summary for 3.1.15.1 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
Search for more literature for 3.1.15.1

Cloned(Commentary)

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

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Macrovipera lebetina
-
-

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Macrovipera lebetina W8E7D1 i.e. Macrovipera lebetina
-

Posttranslational Modification

Posttranslational Modification Comment Organism
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)

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

Source Tissue

Source Tissue Comment Organism Textmining
venom
-
 Macrovipera lebetina
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl thymidine-5'-phosphate + H2O best substrate Macrovipera lebetina 4-nitrophenol + thymidine-5'-phosphate
-
 ?
ADP + H2O
-
 Macrovipera lebetina AMP + phosphate
-
 ?
bis(p-nitrophenyl)phosphate + H2O good substrate Macrovipera lebetina ?
-
 ?
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

Subunits Comment Organism
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

Synonyms Comment Organism
VLPDE
-
 Macrovipera lebetina

Temperature Optimum [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5 9
-
 Macrovipera lebetina

pI Value

Organism Comment pI Value Maximum pI Value
Macrovipera lebetina sequence calculation
-
 6.87

General Information

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