cd09006

purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas vaginalis PNP

CDD entry
Member databaseCDD
CDD typedomain
Short namePNP_EcPNPI-like
SetNP-I

Description

Escherichia coli purine nucleoside phosphorylase (PNP)-I (or DeoD) accepts both 6-oxo and 6-amino purine nucleosides as substrates. Trichomonas vaginalis PNP has broad substrate specificity, having phosphorolytic catalytic activity with adenosine, inosine, and guanosine (with adenosine as the preferred substrate). This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.
[3, 2, 1]

References

1.Structural basis for substrate specificity of Escherichia coli purine nucleoside phosphorylase. Bennett EM, Li C, Allan PW, Parker WB, Ealick SE. J. Biol. Chem. 278, 47110-8, (2003). View articlePMID: 12937174

2.Structure of purine nucleoside phosphorylase (DeoD) from Bacillus anthracis. Grenha R, Levdikov VM, Fogg MJ, Blagova EV, Brannigan JA, Wilkinson AJ, Wilson KS. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 61, 459-62, (2005). View articlePMID: 16511068

3.Inhibition and structure of Trichomonas vaginalis purine nucleoside phosphorylase with picomolar transition state analogues. Rinaldo-Matthis A, Wing C, Ghanem M, Deng H, Wu P, Gupta A, Tyler PC, Evans GB, Furneaux RH, Almo SC, Wang CC, Schramm VL. Biochemistry 46, 659-68, (2007). View articlePMID: 17223688

This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice and Terms of Use.