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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. [12]
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.
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 ...
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).
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 ...
Phosphodiesterases are enzymes that catalyze the hydrolysis of the phosphodiester bond. These enzymes are involved in repairing DNA and RNA sequences, nucleotide salvage, and in the conversion of cGMP and cAMP to GMP and AMP, respectively. [2] Hydrolysis of the phosphodiester bond also occurs chemically and spontaneously, without the aid of ...
cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A is an enzyme that in humans is encoded by the PDE10A gene. [ 5 ] [ 6 ] Various cellular responses are regulated by the second messengers cAMP and cGMP .
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.