2',3'-Cyclic-nucleotide 3'-phosphodiesterase (CNP)

2',3'-Cyclic-nucleotide 3'-phosphodiesterase (CNP, also known as CNPase) is a highly abundant enzyme predominantly expressed in the myelin sheath of vertebrate central nervous system. It catalyzes the hydrolysis of 2',3'-cyclic nucleotides to 2'-nucleotides and is a member of the 2H phosphoesterase superfamily, with a catalytically essential domain responsible for its enzymatic activity[1][2][3]. CNP is implicated in myelin formation, oligodendrocyte differentiation, microtubule dynamics, and RNA metabolism in myelinating cells. It is a marker for oligodendrocyte maturation and myelin integrity, and also plays a potential role in neurodegenerative diseases such as multiple sclerosis, where it is recognized as an autoantigen and is essential for axonal integrity—its genetic deficiency in mice leads to progressive axonal degeneration[1][2]. Although there are no currently known small-molecule drugs involved in direct modulation of CNP, the enzyme may present future therapeutic opportunities in myelin-related diseases.

Other names

2',3'-cyclic nucleotide 3'-phosphodiesteraseCNPaseCN37CNP1HLD202',3'-cyclic-nucleotide 3'-phosphodiesterase2',3'-cyclic nucleotide 3' phosphohydrolaseCNP

Catalyzes hydrolysis of nucleoside 2',3'-cyclic phosphates to nucleoside 2'-phosphates[2][3] Substrate binding and catalysis via His-X-Thr-X motifs and water-mediated nucleophilic attack[1][3]