Structural highlights
Function
3PASE_NITEU Involved in the hydrolysis of the beta-gamma-phosphoanhydride linkage of triphosphate-containing substrates (inorganic or nucleoside-linked). Catalyzes the hydrolysis of inorganic triphosphate (PPPi). The enzyme has a strong preference for linear PPPi compared with cyclic PPPi (cyclic trimetaphosphate) and to the linear P4. The longer chains polyphosphate are not hydrolyzed. It has only a slight thiamine triphosphatase (ThTPase) activity. Nucleoside triphosphatase activity is negligible in the presence of magnesium, but a small activity is observed in the presence of manganese, in particular with GTP.[1]
References
- ↑ Delvaux D, Murty MR, Gabelica V, Lakaye B, Lunin VV, Skarina T, Onopriyenko O, Kohn G, Wins P, De Pauw E, Bettendorff L. A specific inorganic triphosphatase from Nitrosomonas europaea: structure and catalytic mechanism. J Biol Chem. 2011 Sep 30;286(39):34023-35. Epub 2011 Aug 12. PMID:21840996 doi:10.1074/jbc.M111.233585
