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Literature summary for 3.2.2.5 extracted from

  • Zhang, L.Y.; Xu, X.L.; Luo, Z.F.; Wu, H.; Shen, D.K.; Peng, L.L.; Liu, Y.Z.
    Small-molecule reductants inhibit multicatalytic activity of AA-NADase from Agkistrodon acutus venom by reducing the disulfide-bonds and Cu(II) of enzyme (2010), Biopolymers, 93, 141-149.
    View publication on PubMed
Search for more literature for 3.2.2.5

Inhibitors

Inhibitors Comment Organism Structure
dithiothreitol inhibits both NADase and ADPase activities through the reduction of Cu(II) to Cu(I) and the cleavage of disulfide-bonds in AA-NADase Deinagkistrodon acutus
DTT
-
 Deinagkistrodon acutus
glutathione inhibits both NADase and ADPase activities through the reduction of Cu(II) to Cu(I) and the cleavage of disulfide-bonds in AA-NADase Deinagkistrodon acutus
L-ascorbate inhibits AA-NADase on both NADase and ADPase activities through the reduction of Cu(II) in AA-NADase to Cu(I) Deinagkistrodon acutus
tris(2-carboxyethyl)phosphine TCEP, inhibits both NADase and ADPase activities through the reduction of Cu(II) to Cu(I) and the cleavage of disulfide-bonds in AA-NADase Deinagkistrodon acutus

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular venom Deinagkistrodon acutus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ among all identified NADases, only AA-NADase contains Cu2+ and has six disulfide-bond linkages between two peptide chains Deinagkistrodon acutus
Zn2+ apo-AA-NADase can recover its NADase and ADPase activities in the presence of 1 mM Zn2+, which is inhibited by tris(2-carboxyethyl)phosphine Deinagkistrodon acutus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
NAD+ + H2O Deinagkistrodon acutus
-
 ADP-ribose + nicotinamide
-
 ?

Organism

Organism UniProt Comment Textmining
Deinagkistrodon acutus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme Deinagkistrodon acutus

Source Tissue

Source Tissue Comment Organism Textmining
venom
-
 Deinagkistrodon acutus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the multifunctional AA-NADase also shows ADPase activity Deinagkistrodon acutus ?
-
 ?
NAD+ + H2O
-
 Deinagkistrodon acutus ADP-ribose + nicotinamide
-
 ?

Subunits

Subunits Comment Organism
More among all identified NADases, only AA-NADase contains Cu2+ and has six disulfide-bond linkages between two peptide chains, and it has 15 free cysteine residues Deinagkistrodon acutus

Synonyms

Synonyms Comment Organism
AA-NADase
-
 Deinagkistrodon acutus
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
7.4
-
 assay at Deinagkistrodon acutus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
 additional information inhibition kinetics, overview Deinagkistrodon acutus

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.42
-
 pH 7.4, 37°C, inhibition of the NADase activity Deinagkistrodon acutus tris(2-carboxyethyl)phosphine
1.79
-
 pH 7.4, 37°C, inhibition of the NADase activity Deinagkistrodon acutus L-ascorbate
2.48
-
 pH 7.4, 37°C, inhibition of the NADase activity Deinagkistrodon acutus DTT
6.11
-
 pH 7.4, 37°C, inhibition of the NADase activity Deinagkistrodon acutus glutathione