Journal
PLANT SCIENCE
Volume 177, Issue 6, Pages 636-642Publisher
ELSEVIER IRELAND LTD
DOI: 10.1016/j.plantsci.2009.09.005
Keywords
Calcium ions; Euphorbia characias; Magnesium ions; Metallo-proteins; Nucleotide pyrophosphatase/phosphodiesterase
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Funding
- Fondazione Banco di Sardegna, Sassari (Italy)
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An authentic soluble metallo-protein nucleotide pyrophosphatase/phosphodiesterase (ELNPP) was purified to homogeneity from Euphorbia characias latex. The native protein had a molecular mass of 80 +/- 5 kDa and was shown to be formed by two apparently identical subunits, each containing 1 Ca2+ and I Mg2+ ion. Whereas Mg2+ was shown to be strongly bound to the enzyme, Ca2+ was easily removed by treatment with EDTA. Ca2+-demetalated enzyme was shown to be almost totally inactive and the activity was fully restored incubating the demetalated ELNPP with Ca2+ ions. ELNPP exhibited hydrolytic activities toward pyrophosphate/phosphodiester bonds of a broad range of substrates and very efficiently hydrolyzed the artificial substrate thymidine T-monophosphate 4-nitrophenyl ester generating 4-nitrophenolate as a final product, and it has been used for enzyme kinetic experiments. ELNPP represents the first example of a nucleotide pyrophosphatase/phosphodiesterase enzyme purified from the latex of a plant belonging to the large genus Euphorbia. (C) 2009 Elsevier Ireland Ltd. All rights reserved.
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