Premium
PDE7A1 hydrolyzes cCMP
Author(s) -
Monzel Maike,
Kuhn Maike,
Bähre Heike,
Seifert Roland,
Schneider Erich H.
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.08.005
Subject(s) - chemistry , phosphodiesterase , enzyme , nucleoside , hydrolysis , biochemistry , enzyme kinetics , recombinant dna , adenosine , nucleotide , chromatography , active site , gene
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 K M value of 135 ± 19 μM. The V max for cCMP hydrolysis reached 745 ± 27 nmol/(min mg), 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.