Gene Review:
pde-3 - Protein PDE-3
Caenorhabditis elegans
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text.
Read more.
Welcome to WikiGenes!
If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text.Ideally this entry shall become one comprehensive and continuous article. Bulleted lists, for instance, were only used because it is impossible to automatically integrate independent facts into a continuous text.
Much of the current information on this page has been automatically compiled from Pubmed.
This precompiled information serves as a substrate and matrix to embed your contributions, but it is by no means the final word - Homo sapiens can do much better!
WikiGenes is a non-profit and open access community project - Read more.
Disease relevance of pde-3
- Two GAF (for cGMP binding and stimulated PDEs, Anabaena adenylyl cyclases, and Escherichia coli FhlA) domains, similar to those contained in many signaling molecules including mammalian PDE2, PDE5, PDE6, PDE10, and PDE11, were located N-terminal to a consensus PDE catalytic domain [1].
High impact information on pde-3
- The catalytic domain is homologous to the catalytic domain of all 11 mammalian PDEs, the Dictyostelium discoideum RegA, and a probable PDE from Caenorhabditis elegans [1].
- The nonselective PDE inhibitors 3-isobutyl-1-methylxanthine, papaverine and pentoxifyline are poor inhibitors of TbPDE2B [1].
- Using a bioinformatic approach, two different expressed sequence tag clones were identified and used to isolate the complete sequence of two identical PDE genes arranged in tandem [1].
- Similarly, PDE inhibitors selective for the mammalian PDE families 2, 3, 5, and 6 (erythro-9-[3-(2-hydroxynonyl)]-adenine, enoximone, zaprinast, and sildenafil) were also unable to inhibit this enzyme [1].
- TbPDE2B has substrate specificity for cAMP with a K(m) of 2.4 microM. cGMP is not hydrolyzed by TbPDE2B nor does this cyclic nucleotide modulate cAMP PDE activity [1].
References
- Cloning and characterization of a cAMP-specific phosphodiesterase (TbPDE2B) from Trypanosoma brucei. Rascón, A., Soderling, S.H., Schaefer, J.B., Beavo, J.A. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
Contributions to this collaborative article are from individual authors of WikiGenes or mined by the WikiGenes Data Mining Engine from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenesOpen Access LicencePrivacy PolicyTerms of Useapsburg