A Comparative Study of 2′,3′‐Cyclic‐Nucleotide 3′‐Phosphodiesterase in Vertebrates: cDNA Cloning and Amino Acid Sequences for Chicken and Bullfrog Enzymes

Abstract

Abstract:In mammalian brain, two 2',3'-cyclic-nucleotide 3'-phosphodiesterase (EC 3.1.4.37) isoforms, CNP1 and CNP2, are translated, respectively, from the two mRNAs, which have been transcribed and processed by alternative use of the two transcription start points and by differential splicing. In the present study, the cDNAs encoding chicken CNP2 and bullfrog CNP1, respectively, were isolated, and the amino acid sequences of chicken CNP2 and bullfrog CNP1 were deduced. Western blot analysis showed that chicken brain contains a major CNP2-type protein together with a minor unidentified isoform, and bullfrog brain contains only a CNP1 -type protein. All available amino acid sequences of vertebrate 2' ‚3 '-cyclic-nucleotide 3 '-phosphodiesterases were aligned and compared. Three conserved motif sequences were noted: (a) an ATP-binding site near the amino terminus, (b) an isoprenylation site at the carboxyl terminus, and (c) a probable catalytic site resembling the active site of ß-ketoacyl synthase (EC 2.3

Amyotrophic lateral sclerosis, gene deregulation in the anterior horn of the spinal cord and frontal cortex area 8: implications in frontotemporal lobar degeneration

“…Mal T-cell differentiation protein (encoded by MAL ) is involved in myelin biogenesis [94]. Finally, 2',3'-cyclic nucleotide 3' phosphodiesterase (encoded by CNP1 ) participates in early oligodendrocyte differentiation and myelination [95-97]. …”

Crystal Structure of the Catalytic Fragment of Human Brain 2′,3′-Cyclic-nucleotide 3′-Phosphodiesterase

“…9 This hypothesis was tested by the generation of several site-directed mutants of zebra fish RICH (zRICH) protein in which amino acid residues of the putative active-site domain (Ser331, Arg332, His334, Thr336, and Cys339) were mutated to alanine. 27 The results showed that no activity was detected for the His334Ala or Thr336Ala mutant, which correspond to His310 and Thr312 in hCNP, respectively, and established that the histidine and threonine residues in the second H-X-T-X motif of 2H phosphoesterases are essential for catalysis.…”

“…9 CNP catalyzes the hydrolysis of NOp to N-2 0 p in vitro, but the biological function of CNP in vivo remains unknown. Several functional studies have suggested possible functions of CNP.…”

Assessment of Developmental Toxicants using Human Embryonic Stem Cells

“…As a solute carrier protein, SLC1A2 is the principal transporter that clears the excitatory neurotransmitter glutamate from the extracellular space at synapses in the central nervous system (60). CNP is expressed exclusively by oligodendrocytes in the CNS, and the appearance of CNP seems to be one of the earliest events of oligodendrocyte differentiation (61). GAD1 encodes one of several forms of glutamic acid decarboxylase, which catalyzed production of gamma-aminobutyric acid (GABA) from Lglutamic acid (62).…”