Literature summary for 2.4.2.31 extracted from

Ravulapalli, R.; Lugo, M.R.; Pfoh, R.; Visschedyk, D.; Poole, A.; Fieldhouse, R.J.; Pai, E.F.; Merrill, A.R.
Characterization of Vis Toxin, a novel ADP-ribosyltransferase from Vibrio splendidus (2015), Biochemistry, 54, 5920-5936.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
apoenzyme and in complex with NAD+ and inhibitors, vapor diffusion method	Vibrio splendidus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.272	-	Nomega-(ADP-D-ribosyl)-agmatine-L-arginine	pH and temperature not specified in the publication	Vibrio splendidus
0.276	-	NAD+	pH and temperature not specified in the publication	Vibrio splendidus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
NAD+ + agmatine	Vibrio splendidus	the enzyme labels L-arginine with ADP-ribose from the NAD(+) substrate at the amino nitrogen of the guanidinium side chain	nicotinamide + Nomega-(ADP-D-ribosyl)-agmatine	-	r
nicotinamide + Nomega-(ADP-D-ribosyl)-agmatine-L-arginine	Vibrio splendidus	-	NAD+ + agmatine L-arginine	-	r

Organism

Organism	UniProt	Comment	Textmining
Vibrio splendidus	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
NAD+ + agmatine	the enzyme labels L-arginine with ADP-ribose from the NAD(+) substrate at the amino nitrogen of the guanidinium side chain	Vibrio splendidus	nicotinamide + Nomega-(ADP-D-ribosyl)-agmatine	-	r
nicotinamide + Nomega-(ADP-D-ribosyl)-agmatine-L-arginine	-	Vibrio splendidus	NAD+ + agmatine L-arginine	-	r

Synonyms

Synonyms	Comment	Organism
ADP-ribosyltransferase	-	Vibrio splendidus
Vis toxin	-	Vibrio splendidus

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Release 2023.1 (January 2023)