ArticleScientific reports2015
Determinants of ligand binding and catalytic activity in the myelin enzyme 2',3'-cyclic nucleotide 3'-phosphodiesterase.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 35 citations in OpenAlex.
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- A study on the effect of JNJ-10397049 on proliferation and differentiation of neural precursor cells.Anatomy & cell biology · 2022Article
- Metabolically-incorporated deuterium in myelin localized by neutron diffraction and identified by mass spectrometry.Current research in structural biology · 2022Article
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- An unexpected 2-histidine phosphoesterase activity of suppressor of T-cell receptor signaling protein 1 contributes to the suppression of cell signaling.The Journal of biological chemistry · 2020Article
- Structural basis for the evolution of cyclic phosphodiesterase activity in the U6 snRNA exoribonuclease Usb1.Nucleic acids research · 2020Article
- Flexible Players within the Sheaths: The Intrinsically Disordered Proteins of Myelin in Health and Disease.Cells · 2020Review
- Raptor-Mediated Proteasomal Degradation of Deamidated 4E-BP2 Regulates Postnatal Neuronal Translation and NF-κB Activity.Cell reports · 2019Article
- Stability and flexibility of full-length human oligodendrocytic QKI6.BMC research notes · 2019Article
- Sub-Atomic Resolution Crystal Structures Reveal Conserved Geometric Outliers at Functional Sites.Molecules (Basel, Switzerland) · 2019Article
- Possible Involvement of 2',3'-Cyclic Nucleotide-3'-Phosphodiesterase in the Protein Phosphorylation-Mediated Regulation of the Permeability Transition Pore.International journal of molecular sciences · 2018Article
- Olig2 Silence Ameliorates Cuprizone-Induced Schizophrenia-Like Symptoms in Mice.Medical science monitor : international medical journal of experimental and clinical research · 2017Article
- Structural similarities and functional differences clarify evolutionary relationships between tRNA healing enzymes and the myelin enzyme CNPase.BMC biochemistry · 2017Article
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Authors and funding
8 authors at 4 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
2',3'-cyclic nucleotide 3'-phosphodiesterase (CNPase) is an enzyme highly abundant in the central nervous system myelin of terrestrial vertebrates. The catalytic domain of CNPase belongs to the 2H phosphoesterase superfamily and catalyzes the hydrolysis of nucleoside 2',3'-cyclic monophosphates to nucleoside 2'-monophosphates. The detailed reaction mechanism and the essential catalytic amino acids involved have been described earlier, but the roles of many amino acids in the vicinity of the active site have remained unknown. Here, several CNPase catalytic domain mutants were studied using enzyme kinetics assays, thermal stability experiments, and X-ray crystallography. Additionally, the crystal structure of a perdeuterated CNPase catalytic domain was refined at atomic resolution to obtain a detailed view of the active site and the catalytic mechanism. The results specify determinants of ligand binding and novel essential residues required for CNPase catalysis. For example, the aromatic side chains of Phe235 and Tyr168 are crucial for substrate binding, and Arg307 may affect active site electrostatics and regulate loop dynamics. The β5-α7 loop, unique for CNPase in the 2H phosphoesterase family, appears to have various functions in the CNPase reaction mechanism, from coordinating the nucleophilic water molecule to providing a binding pocket for the product and being involved in product release.
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