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Isolation and characterization of a dual-substrate phosphodiesterase gene family: PDE10A

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Soderling, Scott H., Bayuga, Sharon J., Beavo, Joseph A.·1999·Proceedings of the National Academy of Sciences

Abstract

We report here the cloning, expression, and characterization of a dual-substrate, cAMP and cGMP, cyclic nucleotide phosphodiesterase (PDE) from mouse. This PDE contains the consensus sequence for a PDE catalytic domain, but shares <50% sequence identity with the catalytic domains of all other known PDEs and, therefore, represents a new PDE gene family, designated PDE10A. The cDNA for PDE10A is 3,370 nt in length. It includes a full ORF, contains three in-frame stop codons upstream of the first methionine, and is predicted to encode a 779-aa enzyme. At the N terminus PDE10A has two GAF domains homologous to many signaling molecules, including PDE2, PDE5, and PDE6, which likely constitute a low-affinity binding site for cGMP. PDE10A hydrolyzes cAMP with a K m of 0.05 μM and cGMP with a K m of 3 μM. Although PDE10A has a lower K m for cAMP, the V max ratio (cGMP/cAMP) is 4.7. RNA distribution studies indicate that PDE10A is expressed at highest levels in testis and brain.

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Metadata

Authors
Soderling, S. H., Bayuga, S. J., & Beavo, J. A.
Venue
Proceedings of the National Academy of Sciences
Published
1999-06-08
Volume
96
Issue
12
Pages
7071-7076
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W1975769625
Cited by
374
References
1
FWCI
7.72
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Isolation and characterization of a dual-substrate phosphodiesterase gene family: PDE10A. https://app.cochat.ai/papers/10.1073/pnas.96.12.7071
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Soderling, S. H., Bayuga, S. J., & Beavo, J. A. (1999). Isolation and characterization of a dual-substrate phosphodiesterase gene family: PDE10A. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.96.12.7071

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