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PDE7A1 hydrolyzes cCMP.
Monzel, Maike; Kuhn, Maike; Bähre, Heike; Seifert, Roland; Schneider, Erich H.
Afiliación
  • Monzel M; Institute of Pharmacology, Hannover Medical School, Carl-Neuberg-Str. 1, 30625 Hannover, Germany.
  • Kuhn M; Institute of Pharmacology, Hannover Medical School, Carl-Neuberg-Str. 1, 30625 Hannover, Germany.
  • Bähre H; Institute of Pharmacology, Hannover Medical School, Carl-Neuberg-Str. 1, 30625 Hannover, Germany; Core Facility Mass Spectrometry and Metabolomics, Institute of Pharmacology, Hannover Medical School, Carl-Neuberg-Str. 1, 30625 Hannover, Germany.
  • Seifert R; Institute of Pharmacology, Hannover Medical School, Carl-Neuberg-Str. 1, 30625 Hannover, Germany.
  • Schneider EH; Institute of Pharmacology, Hannover Medical School, Carl-Neuberg-Str. 1, 30625 Hannover, Germany.
FEBS Lett ; 588(18): 3469-74, 2014 Sep 17.
Article en En | MEDLINE | ID: mdl-25128584
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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Texto completo: 1 Banco de datos: MEDLINE Asunto principal: CMP Cíclico / Fosfodiesterasas de Nucleótidos Cíclicos Tipo 7 Límite: Animals / Humans Idioma: En Revista: FEBS Lett Año: 2014 Tipo del documento: Article País de afiliación: Alemania

Texto completo: 1 Banco de datos: MEDLINE Asunto principal: CMP Cíclico / Fosfodiesterasas de Nucleótidos Cíclicos Tipo 7 Límite: Animals / Humans Idioma: En Revista: FEBS Lett Año: 2014 Tipo del documento: Article País de afiliación: Alemania