Nucleotide pyrophosphatase/phosphodiesterase from Euphorbia characias latex

ABSTRACT: The low-resolution structure of a nucleotide pyrophosphatase/phosphodiesterase from Euphorbia characias latex (ELNPP) has been determined in solution by means of Small Angle X-ray Scattering (SAXS). To improve the structural resolution of ELNPP a partial sequencing after proteolytic cleavage of the protein was performed. Protein digestion followed by high-resolution HPLC-ESI-MS/MS analysis allowed us to identify two different peptides of 82 and 41 amino acids, respectively. These sequences exhibit a high degree of identity with other NPPs predicted sequences from several higher plants including Malus domestica, Morus notabilis, Ricinus communis, and Triticum aestivum. In particular, Triticum aestivum NPP is the protein with the highest identity level (98 identical positions) towards the obtained fragments of ELNPP. From the alignment with the entire sequence of TaNPP, the two obtained fragments contain some known conserved residues belonging to the catalytic domain of the mammalian NPP family enzymes.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Euphorbia Characias

TISSUE(S): Latex

SUBMITTER: Tiziana Cabras  

LAB HEAD: Tiziana Cabras

PROVIDER: PXD009976 | Pride | 2022-03-02

REPOSITORIES: Pride