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Literature summary for 3.2.2.5 extracted from

  • Wu, S.D.; Liu, Y.; Xu, X.; Zhu, Z.
    Purification of NAD glycohydrolase from Agkistrodon acutus venom (2002), Protein Expr. Purif., 25, 319-322.
    View publication on PubMed

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
2 * 50000, reducing SDS-PAGE Deinagkistrodon acutus
100000
-
gel filtration, non-reducing SDS-PAGE Deinagkistrodon acutus

Organism

Organism UniProt Comment Textmining
Deinagkistrodon acutus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
15.6fold to homogeneity, rapid 3-step chromatographic procedure Deinagkistrodon acutus

Source Tissue

Source Tissue Comment Organism Textmining
venom lyophilized, powder Deinagkistrodon acutus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
12.8
-
purified enzyme Deinagkistrodon acutus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-NAD+ + H2O
-
Deinagkistrodon acutus ADP-ribose + nicotinamide
-
?

Subunits

Subunits Comment Organism
dimer 2 * 50000, reducing SDS-PAGE Deinagkistrodon acutus

Synonyms

Synonyms Comment Organism
NAD glycohydrolase
-
Deinagkistrodon acutus
NADase
-
Deinagkistrodon acutus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Deinagkistrodon acutus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.3
-
assay at Deinagkistrodon acutus