| Description | 3'5'-cyclic nucleotide phosphodiesterases ( ) (PDEases) catalyse the hydrolysis of cAMP or cGMP to the corresponding nucleoside 5' monophosphates [ ]. There are at least seven different subfamilies of PDEases []: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. This entry has a signature pattern from a stretch of 12 residues that contains two conserved histidines.The PDEase catalytic domains adopt a compact α-helical structure consisting of 16 α-helices that can be divided into three subdomains. The active site of PDEases is a deep pocket formed by the treesubdomains and can be divided into two major subpockets for binding of divalent metals and substrate/inhibitors, respectively. The active site of allPDEase domains contains two divalent metal ions: zinc and probably magnesium [, , ]. | Name | 3'5'-cyclic nucleotide phosphodiesterase, conserved site |
| Short Name | PDEase_CS | Type | Conserved_site |
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