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2',3'-Cyclic-nucleotide 3'-phosphodiesterase

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2′,3′-Cyclic-nucleotide 3'-phosphodiesterase
Identifiers
EC no.3.1.4.37
CAS no.60098-35-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
CNP
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesCNP, CNP1, 2',3'-cyclic nucleotide 3' phosphodiesterase, CNPase, HLD20
External IDsOMIM: 123830; MGI: 88437; HomoloGene: 7672; GeneCards: CNP; OMA:CNP - orthologs
EC number3.1.4.37
Orthologs
SpeciesHumanMouse
Entrez

1267

12799

Ensembl

ENSG00000173786

ENSMUSG00000006782

UniProt

P09543

P16330

RefSeq (mRNA)

NM_033133
NM_001330216

NM_001146318
NM_009923

RefSeq (protein)

NP_001317145
NP_149124

NP_001139790
NP_034053

Location (UCSC)Chr 17: 41.97 – 41.98 MbChr 11: 100.47 – 100.48 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

2′,3′-Cyclic-nucleotide 3'-phosphodiesterase (EC 3.1.4.37, CNPase, systematic name nucleoside-2′,3′-cyclic-phosphate 2′-nucleotidohydrolase) is an enzyme that in humans is encoded by the CNP gene.[5][6]

Reaction

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CNPase catalyzes the following reaction:

nucleoside 2′,3′-cyclic phosphate + H2O nucleoside 2′-phosphate

Function

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CNPase is a myelin-associated enzyme that makes up 4% of total CNS myelin protein, and is thought to undergo significant age-associated changes.[7] It is named for its ability to catalyze the phosphodiester hydrolysis of 2',3'-cyclic nucleotides to 2'-nucleotides, though a cohesive understanding of its specific physiologic functions are still ambiguous.[8]

Structural studies have revealed that four classes of CNPases belong to one protein superfamily. CNPase's catalytic core consists of three alpha-helices and nine beta-strands. The proposed mechanism of CNPases phosphodiesterase catalytic activity is similar to the second step of the reaction mechanism for RNase A.[9]

CNPase is expressed exclusively by oligodendrocytes in the CNS, and the appearance of CNPase seems to be one of the earliest events of oligodendrocyte differentiation.[10] CNPase is thought to play a critical role in the events leading up to myelination.[11]

CNPase also associates with microtubules in brain tissue and FRTL-5 thyroid cells, and is reported to have microtubule-associated protein-like activity (MAP; see MAP2), being able to catalyze microtubule formation at low molar ratios. Deletion of the C-terminus of CNPase or phosphorylation abolish the catalytic activity of microtubule formation. CNPase can link tubulin to cellular membranes, and might be involved in the regulation cytoplasmic microtubule distribution.[12]

CNPase has also been demonstrated to inhibit the replication of HIV-1 and other primate lentiviruses by binding the retroviral Gag protein and inhibiting the genesis of nascent viral particles. Whether this is a biological function of CNPase or a coincidental activity remains unclear.[13]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000173786 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000006782 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Sprinkle TJ, Lanclos KD, Lapp DF (Jul 1992). "Assignment of the human 2′,3′-cyclic nucleotide 3′-phosphohydrolase gene to chromosome 17". Genomics. 13 (3): 877–80. doi:10.1016/0888-7543(92)90174-Q. PMID 1322358.
  6. ^ "Entrez Gene: CNP 2′,3′-cyclic nucleotide 3′-phosphodiesterase".
  7. ^ Hinman JD, Chen CD, Oh SY, Hollander W, Abraham CR (Jan 2008). "Age-dependent accumulation of ubiquitinated 2',3'-cyclic nucleotide 3'-phosphodiesterase in myelin lipid rafts". Glia. 56 (1): 118–33. doi:10.1002/glia.20595. PMID 17963267. S2CID 8729201.
  8. ^ Kursula P (Feb 2008). "Structural properties of proteins specific to the myelin sheath". Amino Acids. 34 (2): 175–85. doi:10.1007/s00726-006-0479-7. PMID 17177074. S2CID 20270722.
  9. ^ Sakamoto Y, Tanaka N, Ichimiya T, Kurihara T, Nakamura KT (Feb 2005). "Crystal structure of the catalytic fragment of human brain 2',3'-cyclic-nucleotide 3'-phosphodiesterase". Journal of Molecular Biology. 346 (3): 789–800. doi:10.1016/j.jmb.2004.12.024. PMID 15713463.
  10. ^ Kasama-Yoshida H, Tohyama Y, Kurihara T, Sakuma M, Kojima H, Tamai Y (Oct 1997). "A comparative study of 2',3'-cyclic-nucleotide 3'-phosphodiesterase in vertebrates: cDNA cloning and amino acid sequences for chicken and bullfrog enzymes". Journal of Neurochemistry. 69 (4): 1335–42. doi:10.1046/j.1471-4159.1997.69041335.x. PMID 9326261.
  11. ^ Gravel M, Peterson J, Yong VW, Kottis V, Trapp B, Braun PE (Jun 1996). "Overexpression of 2',3'-cyclic nucleotide 3'-phosphodiesterase in transgenic mice alters oligodendrocyte development and produces aberrant myelination". Molecular and Cellular Neurosciences. 7 (6): 453–66. doi:10.1006/mcne.1996.0033. PMID 8875429. S2CID 35687881.
  12. ^ Bifulco M, Laezza C, Stingo S, Wolff J (Feb 2002). "2',3'-Cyclic nucleotide 3'-phosphodiesterase: a membrane-bound, microtubule-associated protein and membrane anchor for tubulin". Proceedings of the National Academy of Sciences of the United States of America. 99 (4): 1807–12. Bibcode:2002PNAS...99.1807B. doi:10.1073/pnas.042678799. PMC 122275. PMID 11842207.
  13. ^ Wilson SJ, Schoggins JW, Zang T, Kutluay SB, Jouvenet N, Alim MA, Bitzegeio J, Rice CM, Bieniasz PD (Oct 2012). "Inhibition of HIV-1 particle assembly by 2′,3′-cyclic-nucleotide 3′-phosphodiesterase". Cell Host & Microbe. 12 (4): 585–97. doi:10.1016/j.chom.2012.08.012. PMC 3498451. PMID 23084924.
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Further reading

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