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We attribute the lack of hydrolysis of these phosphopeptides to their highly acidic nature, which might interfere with binding to these enzymes.
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Previous studies on in vitro pyrophosphorylated peptide and protein substrates by Snyder and co-workers[8b] accessed the effect of PP1 and PP2B, both of which are members of the PPP family and did not hydrolyze the pyrophosphate moiety. To our knowledge, the effect of PP2C, a PPM family member, on pyrophosphopeptide or protein hydrolysis had not previously been evaluated.
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The enzymatic activity of hDIPP1 was confirmed by treating P1P5-di(adenosine-5′)pentaphosphate(Ap5A), a known hDIPP1 substrate,[7d] with the enzyme, which resulted in 48% hydrolysis of Ap5A to adenosine monophosphate by HPLC after 30 min of incubation.
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51
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84922501386
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Phosphopeptides 2, 6, 19 and pyrophosphopeptides 11, 15, 19 were treated with another small molecule pyrophosphatase, inorganic pyrophosphatase (iPPase), resulting in no hydrolysis of any of the peptide substrates, which is in agreement with previously published results.[8b]The activity of iPPase was confirmed by full hydrolysis of inorganic pyrophosphate to inorganic phosphate, as determined by 31P NMR under standard reaction conditions.
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No phosphopeptide intermediates were observed when the pyrophosphopeptides were treated with the AP enzymes under standard reaction conditions.
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As a small amount of the phosphopeptide intermediate was observed by HPLC (Figure S3), we believe that the hydrolysis in a S. cerevisiae lysate proceeds, at least in part, through a sequential dephosphorylation mechanism.
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These results were corroborated through treatment of 14P and 15P with the pho8Δ lysates, where a more prominent reduction in hydrolysis was observed (Figure S5C, S6C).
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62
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84922501382
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note
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We also tested the yeast enzyme most similar to Pho8 and Pho13[38] by treating pyrophosphopeptides 14P, 15P, and 19 and phosphopeptides 5P, 6P, and 10 with a pho13Δ lysate. In this case, the levels of hydrolysis did not decrease for either the pyrophospho- or phosphopeptide (Figure S7 A-C).
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66
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Although this level of hydrolysis appears lower than for the yeast system, it is important to note that our standard assay conditions used a lower concentration of HeLa cell lysate (0.8 mg mL-1) than S. cerevisiae cell lysate (1.7 mg mL-1).
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84922501380
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We did not pursue genetic perturbations of APs in HeLa cells because HeLa cells express three related AP enzymes, complicating interpretation of knockdown studies.
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