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Reference on EC 3.6.1.61 - diadenosine hexaphosphate hydrolase (ATP-forming)

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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zheng, Q.C.; Li, Z.S.; Sun, M.; Zhang, Y.; Sun, C.C.
Homology modeling and substrate binding study of Nudix hydrolase Ndx1 from Thermos thermophilus HB8
Biochem. Biophys. Res. Commun.
333
881-887
2005
Thermus thermophilus
Manually annotated by BRENDA team
Bessman, M.J.; Walsh, J.D.; Dunn, C.A.; Swaminathan, J.; Weldon, J.E.; Shen, J.
The gene ygdP, associated with the invasiveness of Escherichia coli K1, designates a Nudix hydrolase, Orf176, active on adenosine (5')-pentaphospho-(5')-adenosine (Ap5A)
J. Biol. Chem.
276
37834-37838
2001
Escherichia coli (P0A776)
Manually annotated by BRENDA team
Iwai, T.; Kuramitsu, S.; Masui, R.
The Nudix hydrolase Ndx1 from Thermus thermophilus HB8 is a diadenosine hexaphosphate hydrolase with a novel activity
J. Biol. Chem.
279
21732-21739
2004
Thermus thermophilus (Q75UV1)
Manually annotated by BRENDA team