PROSITE documentation PDOC00530

cAMP phosphodiesterases class-II signature




Description

Cyclic AMP phosphodiesterase (EC 3.1.4.17) (cAMP-PDEase) catalyzes the hydrolysis of cAMP to the corresponding nucleoside 5' monophosphate. While most PDEases can be, on the basis of sequence similarities, grouped together [1], there are at least two enzymes which do not belong to the main family of PDEases and which represent a second class of these enzymes [2]:

  • Slime mold Dictyostelium discoideum extracellular cAMP PDEase. This enzyme plays an essential role in development by hydrolyzing the cAMP used as a chemoattractant by aggregating cells.
  • Budding yeast and Candida albicans low-affinity cAMP PDEase (gene PDE1).
  • Fission yeast probable cAMP PDEase (gene cgs2).
  • Vibrio fischeri periplasmic cAMP PDEase (gene cpdP) [3].

There is, in the central part of these enzymes, a highly conserved region which contains three histidines. We have used this region as a signature pattern.

Last update:

December 2001 / Text revised.

Technical section

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

PDEASE_II, PS00607; cAMP phosphodiesterases class-II signature  (PATTERN)


References

1AuthorsBeavo 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

2AuthorsNikawa J.-I., Sass P., Wigler M.
TitleCloning and characterization of the low-affinity cyclic AMP phosphodiesterase gene of Saccharomyces cerevisiae.
SourceMol. Cell. Biol. 7:3629-3636(1987).
PubMed ID2824992

3AuthorsDunlap P.V., Callahan S.M.
TitleCharacterization of a periplasmic 3':5'-cyclic nucleotide phosphodiesterase gene, cpdP, from the marine symbiotic bacterium Vibrio fischeri.
SourceJ. Bacteriol. 175:4615-4624(1993).
PubMed ID8393003



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