2012
DOI: 10.1248/bpb.b12-00165
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Molecular Characterization and Mutational Analysis of Recombinant Diadenosine 5′,5″-P<sup>1</sup>,P<sup>4</sup>-Tetraphosphate Hydrolase from <i>Plasmodium falciparum</i>

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Cited by 6 publications
(11 citation statements)
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References 18 publications
(16 reference statements)
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“…We performed Pf Ap4AH enzyme assays to access activity of recombinant enzyme ( Fig. 3C ), which displayed kinetic parameters similar to the earlier reports (data not shown) 11 . Enzyme assays in the presence of suramin suggested inhibition with an IC 50 value of ~11.8 μM ( Fig.…”
Section: Resultssupporting
confidence: 67%
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“…We performed Pf Ap4AH enzyme assays to access activity of recombinant enzyme ( Fig. 3C ), which displayed kinetic parameters similar to the earlier reports (data not shown) 11 . Enzyme assays in the presence of suramin suggested inhibition with an IC 50 value of ~11.8 μM ( Fig.…”
Section: Resultssupporting
confidence: 67%
“…Based on sequence analysis the P. falciparum Ap4AH ( Pf Ap4AH, EC 3.6.1.17 ) was predicted to be an animal-archeal type which cleaves polyphosphate chain at the fourth phosphate from the tightly bound adenosine resulting in asymmetrical cleavage of Ap4A. This is distinct from some plant-bacterial type hydrolases 8 9 11 . Eukaryotic Ap4AHs are predominantly cytoplasmic or nuclear, while the bacterial Ap4AHs appear to be ribosome associated 12 13 14 .…”
mentioning
confidence: 99%
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“…[6] In order to verify ac onservede nzymatic activity for PfA-p3Aase as an A3pA hydrolase and to establisha ne xperimental system for validation of cyclomarin Aa sa ni nhibitor of the enzymatica ctivity of PfAp3Aase in vitro, we expressed three diadenosine polyphosphate hydrolases in E. coli and established enzymatic assays with use of al uminescence readout.I na ddition to the plasmodial and human A3pA hydrolases, we included PFE1035c (PfAp4Aase), which converts Ap4A into ATPa nd AMP.P fAp4Aase has recently been proposed as ap otential antimalaria targeta nd was included in this study as ac ontrol. [8] Indeed, we observed A3pA hydrolase activity for recombinant PfAp3Aase in vitro:t he Michaelis-Menten constant (K m )w as determined for the enzyme PfAp3Aase with the preferred substrate Ap3A. The observed K m value of 10.2 mm Ap3A is similar to the values described for the yeast (5.3 mm)a nd the human (1.2 mm)h omologues.…”
supporting
confidence: 70%
“…Hence, signaling mediated by these molecules within red blood cells is of special interest in malaria. [7] Purinergic signaling has been shown to play role in parasite invasion. [8] The malaria parasite enzyme Ap4A hydrolase regulates levels of signaling molecules like Ap4A by hydrolyzing them to adenosine triphosphate and adenosine monophosphate.…”
Section: Introductionmentioning
confidence: 99%