PDE7A1 hydrolyzes cCMP
Copyright © 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved..
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.
Medienart: |
E-Artikel |
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Erscheinungsjahr: |
2014 |
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Erschienen: |
2014 |
Enthalten in: |
Zur Gesamtaufnahme - volume:588 |
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Enthalten in: |
FEBS letters - 588(2014), 18 vom: 17. Sept., Seite 3469-74 |
Sprache: |
Englisch |
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Beteiligte Personen: |
Monzel, Maike [VerfasserIn] |
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Anmerkungen: |
Date Completed 11.11.2014 Date Revised 11.09.2014 published: Print-Electronic Citation Status MEDLINE |
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doi: |
10.1016/j.febslet.2014.08.005 |
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funding: |
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PPN (Katalog-ID): |
NLM241028027 |
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520 | |a 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 | ||
650 | 4 | |a Journal Article | |
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700 | 1 | |a Schneider, Erich H |e verfasserin |4 aut | |
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