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Phosphodiesterase enzymes have been shown to be different in different types of cells, including normal and leukemic lymphocytes [11] and are often targets for pharmacological inhibition due to their unique tissue distribution, structural properties, and functional properties.
The phosphodiesterase 1 isozyme family belongs to a Class I enzymes, [2] [5] which includes all vertebrate phosphodiesterases and some yeast enzymes. [5] Class I enzymes all have a catalytic core of at least 250 amino acids whereas Class II enzymes lack such a common feature. [5] Usually vertebrate PDEs are dimers of linear 50–150 kDa ...
Structure of PDE2 with phosphate shown as sticks and catalytic metals as spheres. (The PDE2 (phosphodiesterase 2) enzyme is one of 21 different phosphodiesterases (PDE) found in mammals. These different PDEs can be subdivided to 11 families (PDE1 – PDE11).
PDE3 is a phosphodiesterase. The PDEs belong to at least eleven related gene families, which are different in their primary structure, substrate affinity, responses to effectors, and regulation mechanism. Most of the PDE families are composed of more than one gene.
Retinal 3′,5′-cGMP phosphodiesterase (PDE) is located in photoreceptor outer segments and is an important enzyme in phototransduction. [2]3′,5′-cyclic-nucleotide phosphodiesterases in rod cells are oligomeric, made up of two heavy catalytic subunits, α (90 kDa) and β (85 kDa,) and two lighter inhibitory γ subunits (11 kDa each).
Phosphodiesterase 5 is widely expressed in several tissues in the body for example brain, lung, kidney, urinary bladder, smooth muscle and platelets. [1] It is possible to prevent cGMP hydrolysis by inhibiting PDE5 and therefore treat diseases associated with low cGMP levels, because of this, PDE5 is an ideal target for the development of ...
This ability to catalyze a reaction with a secondary substrate is known as enzyme promiscuity, [1] and may have played a role in NPP's evolutionary history. [15] NPP's promiscuity enables the enzyme to share substrates with alkaline phosphatase (AP), another member of the alkaline phosphate superfamily. Alkaline phosphatase primarily hydrolyzes ...
ENPP1 has broad specificity and cleaves a variety of substrates, including phosphodiester bonds of nucleotides and nucleotide sugars. ENPP1 protein may function to hydrolyze nucleoside 5′-triphosphates to their corresponding monophosphates and may also hydrolyze diadenosine polyphosphates.