Cellular redox metabolism is modulated by the distinct localization of cyclic nucleotide phosphodiesterase 5a isoforms

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SUMMARY

    The latter contains several structural motifs which confer specificity to each isoform, such as peculiar quaternary_structure, subcellular localization, different post-translational modifications, binding_sites for allosteric modulators and for interactions with unique scaffolding and regulatory proteins and effectors. In mammals, three isoforms of PDE5 have been identified-called A1, A2 and A3- which show similar cGMP catalytic activities, while differing in the very first N-terminal amino_acids. In bold the one-letter amino_acid code of the common sequence. The result is that MmPDE5A1 has 41 amino_acids more and MmPDE5A2 10 amino_acids more than MmPDE5A3. To . . .

     

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