- PDE7A1 hydrolyzes cCMP.
PDE7A1 hydrolyzes cCMP.
FEBS letters (2014-08-17)
Maike Monzel, Maike Kuhn, Heike Bähre, Roland Seifert, Erich H Schneider
PMID25128584
RÉSUMÉ
The degradation and biological role of the cyclic pyrimidine nucleotide cCMP is largely elusive. We investigated nucleoside 3',5'-cyclic monophosphate (cNMP) specificity of six different recombinant phosphodiesterases (PDEs) by using a highly-sensitive HPLC-MS/MS detection method. PDE7A1 was the only enzyme that hydrolyzed significant amounts of cCMP. Enzyme kinetic studies using purified GST-tagged truncated PDE7A1 revealed a cCMP KM value of 135 ± 19 μM. The Vmax for cCMP hydrolysis reached 745 ± 27 nmol/(minmg), which is about 6-fold higher than the corresponding velocity for adenosine 3',5'-cyclic monophosphate (cAMP) degradation. In summary, PDE7A is a high-speed and low-affinity PDE for cCMP.
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Adenosine, European Pharmacopoeia (EP) Reference Standard