The Enzyme Database

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EC 3.6.1.15     
Accepted name: nucleoside-triphosphate phosphatase
Reaction: a nucleoside triphosphate + H2O = a nucleoside diphosphate + phosphate
Other name(s): nucleoside-triphosphatase; nucleoside triphosphate phosphohydrolase; nucleoside-5-triphosphate phosphohydrolase; nucleoside 5-triphosphatase; unspecific diphosphate phosphohydrolase
Systematic name: nucleoside-triphosphate phosphohydrolase
Comments: The enzyme is found in eukaryotes and thermophilic bacteria, but appears to be absent from mesophilic bacteria. Also hydrolyses nucleoside diphosphates, thiamine diphosphate and FAD. The enzyme from the plant Pisum sativum (garden pea) is regulated by calmodulin [5].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9075-51-8
References:
1.  Brightwell, R. and Tappel, A.L. Lysosomal acid pyrophosphatase and acid phosphatase. Arch. Biochem. Biophys. 124 (1968) 333–343. [DOI] [PMID: 5661608]
2.  Lewis, M. and Weissman, S. Properties of a soluble nucleoside triphosphatase activity in mammalian liver. Arch. Biochem. Biophys. 109 (1965) 490–498. [DOI] [PMID: 14320490]
3.  Matsushita, S. and Raacke, I.D. Purification of nucleoside triphosphatases from pea seedling ribosomes. Biochim. Biophys. Acta 166 (1968) 707–710. [DOI] [PMID: 4301913]
4.  Tong, C.G., Dauwalder, M., Clawson, G.A., Hatem, C.L. and Roux, S.J. The major nucleoside triphosphatase in pea (Pisum sativum L.) nuclei and in rat liver nuclei share common epitopes also present in nuclear lamins. Plant Physiol. 101 (1993) 1005–1011. [PMID: 7508630]
5.  Hsieh, H.L., Tong, C.G., Thomas, C. and Roux, S.J. Light-modulated abundance of an mRNA encoding a calmodulin-regulated, chromatin-associated NTPase in pea. Plant Mol. Biol. 30 (1996) 135–147. [PMID: 8616230]
6.  Klinger, C., Rossbach, M., Howe, R. and Kaufmann, M. Thermophile-specific proteins: the gene product of aq_1292 from Aquifex aeolicus is an NTPase. BMC Biochem. 4:12 (2003). [DOI] [PMID: 14503925]
7.  Placzek, W.J., Almeida, M.S. and Wuthrich, K. NMR structure and functional characterization of a human cancer-related nucleoside triphosphatase. J. Mol. Biol. 367 (2007) 788–801. [DOI] [PMID: 17291528]
[EC 3.6.1.15 created 1972]
 
 


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