|PROSITE documentation PDOC00116
3'5'-cyclic nucleotide phosphodiesterases signature
3'5'-cyclic nucleotide phosphodiesterases (EC 220.127.116.11) (PDEases) catalyze the
hydrolysis of cAMP or cGMP to the corresponding nucleoside 5' monophosphates
. 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.
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>).
July 1998 / Pattern and text revised.
PROSITE method (with tools and information) covered by this documentation:
|PDEASE_I, PS00126; 3'5'-cyclic nucleotide phosphodiesterases signature (PATTERN)
|Sequences known to belong to this class detected by the pattern:
|Other sequence(s) detected in Swiss-Prot:
|Matching PDB structures:
1F0J 1JP1 1JP2 1LHQ ... [ALL]
||Charbonneau H., Beier N., Walsh K.A., Beavo J.A.
||Identification of a conserved domain among cyclic nucleotide phosphodiesterases from diverse species.
||Proc. Natl. Acad. Sci. U.S.A. 83:9308-9312(1986).
||Beavo J.A., Reifsnyder D.H.
||Primary sequence of cyclic nucleotide phosphodiesterase isozymes and the design of selective inhibitors.
||Trends Pharmacol. Sci. 11:150-155(1990).
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