Literature summary for 3.6.1.41 extracted from

Guranowski, A.; Starzynska, E.; Pietrowska-Borek, M.; Rejman, D.; Blackburn, G.M.
Novel diadenosine polyphosphate analogs with oxymethylene bridges replacing oxygen in the polyphosphate chain: potential substrates and/or inhibitors of Ap4A hydrolases (2009), FEBS J., 276, 1546-1553.

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Inhibitors

Inhibitors	Comment	Organism	Structure
A-5'-pCH2OpOCH2p-5'-A	no activity as inhibitor of Escherichia coli symmetrical Ap4A hydrolase	Escherichia coli
A-5'-pCH2OpOpOCH2p-5'-A	no activity as inhibitor of Escherichia coli symmetrical Ap4A hydrolase	Escherichia coli
A-5'-pOCH2pCH2Op-5'-A	no activity as inhibitor of Escherichia coli symmetrical Ap4A hydrolase	Escherichia coli
A-5'-pOCH2pOpCH2Op-5'-A	no activity as inhibitor of Escherichia coli symmetrical Ap4A hydrolase	Escherichia coli
A-5'-pOpCH2OpOp-5'-A	no activity as inhibitor of Escherichia coli symmetrical Ap4A hydrolase	Escherichia coli
A-5'-pOpOCH2pCH2OpOp-5'-A	no activity as inhibitor of Escherichia coli symmetrical Ap4A hydrolase	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Co2+	symmetrical Ap4A hydrolase is Co2+-dependent	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
symmetrical Ap4A hydrolase is partially purified	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	hydrolase from Escherichia coli shows almost no cleavage of dinucleoside polyphosphate molecules modified in their ADP moieties	Escherichia coli	?	-	?

Synonyms

Synonyms	Comment	Organism
bis(5'-nucleosyl)-tetraphosphatase (symmetrical)	-	Escherichia coli
symmetrical Ap4A hydrolase	-	Escherichia coli

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Release 2023.1 (January 2023)