Literature summary for 3.2.2.5 extracted from

Xu, X.; Zhang, L.; Luo, Z.; Shen, D.; Wu, H.; Peng, L.; Song, J.; Zhang, Y.
Metal ions binding to NAD-glycohydrolase from the venom of Agkistrodon acutus: Regulation of multicatalytic activity (2010), Metallomics, 2, 480-489.

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Inhibitors

Inhibitors	Comment	Organism	Structure
Cu2+	the enzyme has two classes of Cu2+ binding sites, one activator site with high affinity and approximately six inhibitor sites with low affinity	Deinagkistrodon acutus
EDTA	irreversible inhibition	Deinagkistrodon acutus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	kinetics and thermodynamics in presence of different metal ions, overview	Deinagkistrodon acutus

Localization

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

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Co2+	AA-NADase has one strong and two weak Co2+ binding sites	Deinagkistrodon acutus
Co2+	the enzyme has one strong and two weak Co2+ binding sites	Deinagkistrodon acutus
Cu2+	although Cu2+ ions are important for catalyzing the hydrolysis of NAD, they are also able to inhibit its NADase activity in a concentration-dependent manner, Cu2+ ions in low-affinity binding sites inhibit its NADase activity. AA-NADase has two classes of Cu2+ binding sites, one activator site with high affinity and approximately six inhibitor sites with low affinity. Cu2+ ions function as a switch for its NADase activity.	Deinagkistrodon acutus
Cu2+	the enzyme contains Cu2+ ions that are essential for its multicatalytic activity. The enzyme has two classes of Cu2+ binding sites, one activator site with high affinity and approximately six inhibitor sites with low affinity. Both NADase and ADPase activities of the enzyme do not have an absolute requirement for Cu2+ and may be replaced by Zn2+ > Mn2+ > Cu2+/Co2+ > Ni2+	Deinagkistrodon acutus
Mn2+	AA-NADase has one Mn2+ binding site	Deinagkistrodon acutus
Mn2+	the enzyme has one Mn2+ binding site	Deinagkistrodon acutus
additional information	no absolute requirement for metal ions, metal ion binding affinities in descending order: Cu2+ , Ni2+, Mn2+, Co2+, and Zn2+. Enzyme-metal ion interaction analysis by equilibrium dialysis, isothermal titration calorimetry, fluorescence, circular dichroism, dynamic light scattering and HPLC, overview	Deinagkistrodon acutus
Ni2+	AA-NADase has two strong and six weak Ni2+ binding sites	Deinagkistrodon acutus
Ni2+	the enzyme has two strong and six weak Ni2+ binding sites	Deinagkistrodon acutus
Zn2+	AA-NADase has one Zn2+ binding site	Deinagkistrodon acutus
Zn2+	the enzyme has one Zn2+ binding site	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
-	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	-	?
NAD+ + H2O	-	Deinagkistrodon acutus	ADP-ribose + nicotinamide + H+	-	?

Synonyms

Synonyms	Comment	Organism
AA-NADase	-	Deinagkistrodon acutus
NAD-glycohydrolase	-	Deinagkistrodon acutus
NADase	multicatalytic enzyme with both NADase and AT(D)Pase activities	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

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Release 2023.1 (January 2023)