Purification and characterization of phosphodiesterase (exonuclease) from Cerastes cerastes (Egyptian sand viper) venom
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Cited by (15)
State-of-the-art review of snake venom phosphodiesterases (svPDEs)
2022, ToxiconCitation Excerpt :As described above, svPDE-inhibitors can be inhibited by molecules as EDTA, since they are metalloenzymes (Dolapchiev et al., 1980; Mitra and Bhattacharyya, 2014; Oliveira et al., 2021; Peng et al., 2011). Other examples of inhibitors are some reducing agents, such as β-mercaptoethanol that can block svPDEs in a dose-dependent matter, DTT, and cysteine (Halim et al., 1987; Ibrahim et al., 2016; Oliveira et al., 2021; Valério et al., 2002). Snake venom toxins possibly evolved from proteins presenting physiological activity, being selected for composing the venom proteome (Calvete et al., 2009).
Unraveling the structure and function of CdcPDE: A novel phosphodiesterase from Crotalus durissus collilineatus snake venom
2021, International Journal of Biological MacromoleculesCitation Excerpt :In addition, glycosylation may have an effect on inflammatory reactions and cellular signaling [67,68], as well as it may contribute to snake venom diversity through changing toxin conformation and, consequently, its function [69–72]. CdcPDE molecular masses are quite similar to other monomeric PDEs, such as those reported from Cerastes cerastes (110 kDa) [66] and B. alternatus (105 kDa) venoms [21]. However, in these two cases, PDE molecular masses were estimated by SDS-PAGE while the methodology used in our study is more accurate.
NPP-BJ, a nucleotide pyrophosphatase/phosphodiesterase from Bothrops jararaca snake venom, inhibits platelet aggregation
2009, ToxiconCitation Excerpt :NPP-BJ – as other snake venom phosphodiesterases and NPP3 from bovine intestine (Kelly et al., 1975) – is much more effective to hydrolyze thymidine 5′-monophosphate p-nitrophenyl ester than bis(p-nitrophenyl) phosphate, likely due to the fact that the structure of the former is more similar to nucleotides than that of the latter. Interestingly, NPP-BJ is remarkably more active on thymidine 5′-monophosphate p-nitrophenyl ester than other snake venom phosphodiesterases (Sugihara et al., 1986; Mori et al., 1987), but it is less active on bis(p-nitrophenyl) phosphate compared to other phosphodiesterases (Halim et al., 1987; Valério et al., 2002). Changes in the primary structure of the catalytic site may account for such differences.
Proteomic characterization of Naja mandalayensis venom
2021, Journal of Venomous Animals and Toxins Including Tropical DiseasesPhosphodiesterases (PDEs) from snake venoms: Therapeutic applications
2018, Protein and Peptide Letters