3'-nucleotidase

3′-nucleotidase
Identifiers
EC no.3.1.3.6
CAS no.9025-84-7
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

The enzyme 3′-nucleotidase (EC 3.1.3.6) catalyzes the reversible reaction

a 3′-ribonucleotide + H2O a ribonucleoside + phosphate
2D representation of the chemical structure of Q27103969.
3'-adenylic acid
 
H2O
Rightward reaction arrow with minor substrate(s) from top left and minor product(s) to top right
 
 
 

The enzyme originally characterised from the barley hydrolyses 3'-adenylic acid to adenosine and orthophosphate, which form the phosphate ester in the starting material. The enzyme is selective for the isomer with the phosphate group in the 3'-position shown. It can also act on other nucleotides which have the phosphate group at this position in the ribose ring.[1][2] There is evidence that this enzyme helps Leishmania parasites survive in their host.[3][4]

This enzyme is a hydrolase, specifically one acting on phosphoric monoester bonds. The systematic name is 3′-ribonucleotide phosphohydrolase. Other names in common use include 3′-mononucleotidase, 3′-phosphatase, and 3′-ribonucleotidase.[5]

References

  1. ↑ Shuster, Louis; Kaplan, Nathan O. (1953). "A specific b nucleotidase". Journal of Biological Chemistry. 201 (2): 535–546. doi:10.1016/S0021-9258(18)66208-8. PMID 13061389.
  2. ↑ Freitas-Mesquita, Anita Leocadio; Meyer-Fernandes, José Roberto (2017). "3′nucleotidase/Nuclease in protozoan parasites: Molecular and biochemical properties and physiological roles". Experimental Parasitology. 179: 1–6. doi:10.1016/j.exppara.2017.06.001. PMID 28587841.
  3. ↑ Guimarães-Costa, Anderson B.; Desouza-Vieira, Thiago S.; Paletta-Silva, Rafael; Freitas-Mesquita, Anita Leocádio; Meyer-Fernandes, José Roberto; Saraiva, Elvira M. (2014). "3′-Nucleotidase/Nuclease Activity Allows Leishmania Parasites to Escape Killing by Neutrophil Extracellular Traps". Infection and Immunity. 82 (4): 1732–1740. doi:10.1128/iai.01232-13. PMC 3993383. PMID 24516114.
  4. ↑ Freitas-Mesquita, Anita Leocadio; Dick, Claudia F.; Dos-Santos, André L.A.; Nascimento, Michelle T.C.; Rochael, Natalia C.; Saraiva, Elvira M.; Meyer-Fernandes, José Roberto (2019). "Cloning, expression and purification of 3'-nucleotidase/Nuclease, an enzyme responsible for the Leishmania escape from neutrophil extracellular traps". Molecular and Biochemical Parasitology. 229: 6–14. doi:10.1016/j.molbiopara.2019.02.004. PMID 30772424.
  5. ↑ Enzyme 3.1.3.6 at KEGG Pathway Database.