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PROSITE documentation PDOC00116

3'5'-cyclic nucleotide phosphodiesterases signature





Description

3'5'-cyclic nucleotide phosphodiesterases (EC 3.1.4.17) (PDEases) catalyze the hydrolysis of cAMP or cGMP to the corresponding nucleoside 5' monophosphates [1]. There are at least seven different subfamilies of PDEases [2,E1]:

  • Type 1, calmodulin/calcium-dependent PDEases.
  • Type 2, cGMP-stimulated PDEases.
  • Type 3, cGMP-inhibited PDEases.
  • Type 4, cAMP-specific PDEases.
  • Type 5, cGMP-specific PDEases.
  • Type 6, rhodopsin-sensitive cGMP-specific PDEases.
  • Type 7, High affinity cAMP-specific PDEases.

All of these forms seem to share a conserved domain of about 270 residues. We have derived a signature pattern from a stretch of 12 residues that contains two conserved histidines.

Note:

Slime mold extracellular PDEase and yeast low-affinity PDEase (gene PDE1) do not show any similarity with the above enzymes and belong to another class of PDEases (see <PDOC00530>).

Last update:

July 1998 / Pattern and text revised.

Technical section

PROSITE method (with tools and information) covered by this documentation:

PDEASE_I, PS00126; 3'5'-cyclic nucleotide phosphodiesterases signature  (PATTERN)


References

1AuthorsCharbonneau H., Beier N., Walsh K.A., Beavo J.A.
TitleIdentification of a conserved domain among cyclic nucleotide phosphodiesterases from diverse species.
SourceProc. Natl. Acad. Sci. U.S.A. 83:9308-9312(1986).
PubMed ID3025833

2AuthorsBeavo J.A., Reifsnyder D.H.
TitlePrimary sequence of cyclic nucleotide phosphodiesterase isozymes and the design of selective inhibitors.
SourceTrends Pharmacol. Sci. 11:150-155(1990).
PubMed ID2159198

E1Sourcehttp://depts.washington.edu/pde/



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