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Concept
PDE1
Summary
Phosphodiesterase 1, PDE1, EC 3.1.4.1, systematic name oligonucleotide 5-nucleotidohydrolase) is a phosphodiesterase enzyme also known as calcium- and calmodulin-dependent phosphodiesterase. It is one of the 11 families of phosphodiesterase (PDE1-PDE11). Phosphodiesterase 1 has three subtypes, PDE1A, PDE1B and PDE1C which divide further into various isoforms. The various isoforms exhibit different affinities for cAMP and cGMP.
The existence of the Ca2+-stimulated Phosphodiesterase 1 was first demonstrated by Cheung (1970), Kakiuchi and Yamazaki (1970) as a result of their research on bovine brain and rat brain respectively. It has since been found to be widely distributed in various mammalian tissues as well as in other eukaryotes. It is now one of the most intensively studied member of the PDE superfamily of enzymes, which today represents 11 gene families, and the best characterized one as well.
Further research in the field along with increased availability of monoclonal antibodies has shown that various phosphodiesterase 1 isoenzymes exist and have been identified and purified. It is now known that phosphodiesterase 1 exists as tissue specific isozymes.
The phosphodiesterase 1 isozyme family belongs to a Class I enzymes, which includes all vertebrate phosphodiesterases and some yeast enzymes. Class I enzymes all have a catalytic core of at least 250 amino acids whereas Class II enzymes lack such a common feature.
Usually vertebrate PDEs are dimers of linear 50–150 kDa proteins. They consist of three functional domains; a conserved catalytic core, a regulatory N-terminus and a C-terminus [3-5]. The proteins are chimeric and each domain is associated with their particular function.
The regulatory N-terminus is substantially different in various phosphodiesterase types. They are flanked by the catalytic core and include regions that auto-inhibit the catalytic domains. They also target sequences that control subcellular localization. In phosphodiesterase 1 this region contains a calmodulin binding domain.
Official source
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