3.6.1.41	654523	Adenosine-5'-O-phosphorylated and adenosine-5'-O-phosphorothioylated polyols as strong inhibitors of (symmetrical) and (asymmetrical) dinucleoside tetraphosphatases	Biochem. J.	373	635-640	2003	Escherichia coli	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=12697025&form=6&db=m	
3.6.1.41	654523	Adenosine-5'-O-phosphorylated and adenosine-5'-O-phosphorothioylated polyols as strong inhibitors of (symmetrical) and (asymmetrical) dinucleoside tetraphosphatases	Biochem. J.	373	635-640	2003	Salmonella enterica subsp. enterica serovar Typhimurium	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=12697025&form=6&db=m	
3.6.1.41	246770	Catabolism of bis(5-nucleosidyl) oligophosphates in Escherichia coli: metal requirements and substrate specificity of homogeneous diadenosine-5,5-P1,P4-tetraphosphate pyrophosphohydrolase	Biochemistry	24	914-922	1985	Escherichia coli	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=2986688&form=6&db=m	
3.6.1.41	246770	Catabolism of bis(5-nucleosidyl) oligophosphates in Escherichia coli: metal requirements and substrate specificity of homogeneous diadenosine-5,5-P1,P4-tetraphosphate pyrophosphohydrolase	Biochemistry	24	914-922	1985	Escherichia coli EM20031	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=2986688&form=6&db=m	
3.6.1.41	246765	Catabolism of diadenosine 5,5-P1,P4-tetraphosphate in procaryotes. Purification and properties of diadenosine 5,5-P1,P4-tetraphosphate (symmetrical) pyrophosphohydrolase from Escherichia coli K12	J. Biol. Chem.	258	14784-14789	1983	Acidaminococcus fermentans	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=6317672&form=6&db=m	
3.6.1.41	246765	Catabolism of diadenosine 5,5-P1,P4-tetraphosphate in procaryotes. Purification and properties of diadenosine 5,5-P1,P4-tetraphosphate (symmetrical) pyrophosphohydrolase from Escherichia coli K12	J. Biol. Chem.	258	14784-14789	1983	Escherichia coli	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=6317672&form=6&db=m	
3.6.1.41	246765	Catabolism of diadenosine 5,5-P1,P4-tetraphosphate in procaryotes. Purification and properties of diadenosine 5,5-P1,P4-tetraphosphate (symmetrical) pyrophosphohydrolase from Escherichia coli K12	J. Biol. Chem.	258	14784-14789	1983	Pyrodictium occultum	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=6317672&form=6&db=m	
3.6.1.41	246764	Diadenosine 5,5-P1,P4-tetraphosphate pyrophosphohydrolase from Physarum polycephalum. Substrate specificity	Biochemistry	21	6129-6133	1982	Physarum polycephalum	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=6295457&form=6&db=m	
3.6.1.41	733872	Enzymatic characteristics of an ApaH-like phosphatase, PrpA, and a diadenosine tetraphosphate hydrolase, ApaH, from Myxococcus xanthus	FEBS Lett.	588	3395-3402	2014	Myxococcus xanthus	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=25107648&form=6&db=m	
3.6.1.41	733872	Enzymatic characteristics of an ApaH-like phosphatase, PrpA, and a diadenosine tetraphosphate hydrolase, ApaH, from Myxococcus xanthus	FEBS Lett.	588	3395-3402	2014	Myxococcus xanthus DK 1622	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=25107648&form=6&db=m