Literature summary extracted from

Gabelli, S.B.; Bianchet, M.A.; Ohnishi, Y.; Ichikawa, Y.; Bessman, M.J.; Amzel, L.M.
Mechanism of the Escherichia coli ADP-ribose pyrophosphatase, a Nudix hydrolase (2002), Biochemistry, 41, 9279-9285.

Metals/Ions

EC Number	Metals/Ions	Comment	Organism	Structure
3.6.1.13	Mg2+	dependent on	Escherichia coli

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.6.1.13	Escherichia coli	Q93K97	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
3.6.1.13	ADPribose + H2O	nucleophilic attack at the adenosyl phosphate. The enzyme cycles between an open free enzyme and a closed substrate-metal complex conformation. This cycling may be important in preventing nonspecific hydrolysis of other nucleotides	Escherichia coli	AMP + D-ribose 5-phosphate	-	?

Synonyms

EC Number	Synonyms	Comment	Organism
3.6.1.13	ADP-ribose pyrophosphatase	-	Escherichia coli
3.6.1.13	ADPRase	-	Escherichia coli

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Release 2023.1 (January 2023)