Jump to content
 







Main menu
   


Navigation  



Main page
Contents
Current events
Random article
About Wikipedia
Contact us
Donate
 




Contribute  



Help
Learn to edit
Community portal
Recent changes
Upload file
 








Search  

































Create account

Log in
 









Create account
 Log in
 




Pages for logged out editors learn more  



Contributions
Talk
 



















Contents

   



(Top)
 


1 References  





2 Further reading  





3 External links  














Nucleotidase







Deutsch
Français

Русский
Српски / srpski
Srpskohrvatski / српскохрватски
 

Edit links
 









Article
Talk
 

















Read
Edit
View history
 








Tools
   


Actions  



Read
Edit
View history
 




General  



What links here
Related changes
Upload file
Special pages
Permanent link
Page information
Cite this page
Get shortened URL
Download QR code
Wikidata item
 




Print/export  



Download as PDF
Printable version
 
















Appearance
   

 






From Wikipedia, the free encyclopedia
 


Nucleotidase
Identifiers
EC no.3.1.3.31
CAS no.9033-33-4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

Anucleotidase is a hydrolytic enzyme that catalyzes the hydrolysis of a nucleotide into a nucleoside and a phosphate.[1]

Anucleotide + H2O = a nucleoside + phosphate

For example, it converts adenosine monophosphatetoadenosine, and guanosine monophosphatetoguanosine.

Nucleotidases have an important function in digestion in that they break down consumed nucleic acids.

They can be divided into two categories, based upon the end that is hydrolyzed:

5'-Nucleotidases cleave off the phosphate from the 5' end of the sugar moiety. They can be classified into various kinds depending on their substrate preferences and subcellular localization. Membrane-bound 5'-nucleotidases display specificity toward adenosine monophosphates and are involved predominantly in the salvage of preformed nucleotides and in signal transduction cascades involving purinergic receptors. Soluble 5'-nucleotidases are all known to belong to the haloacid dehalogenase superfamily of enzymes, which are two domain proteins characterised by a modified Rossman fold as the core and variable cap or hood. The soluble forms are further subclassified based on the criterion mentioned above. mdN and cdN are mitochondrial and cytosolic 5'-3'-pyrimidine nucleotidases. cN-I is a cytosolic nucleotidase(cN) characterized by its affinity toward AMP as its substrate. cN-II is identified by its affinity toward either IMP or GMP or both. cN-III is a pyrimidine 5'-nucleotidase. A new class of nucleotidases called IMP-specific 5'-nucleotidase has been recently defined. 5'-Nucleotidases are involved in varied functions like cell–cell communication, nucleic acid repair, purine salvage pathway for the synthesis of nucleotides, signal transduction, membrane transport, etc.

References[edit]

  1. ^ Zimmermann H, Zebisch M, Sträter N (2012). "Cellular function and molecular structure of ecto-nucleotidases". Purinergic Signalling. 8 (3): 437–502. doi:10.1007/s11302-012-9309-4. PMC 3360096. PMID 22555564.

Further reading[edit]

External links[edit]


  • t
  • e

  • Retrieved from "https://en.wikipedia.org/w/index.php?title=Nucleotidase&oldid=1181635004"

    Categories: 
    EC 3.1.3
    Chemical pathology
    EC 3.1 stubs
    Hidden categories: 
    Articles with short description
    Short description matches Wikidata
    All stub articles
     



    This page was last edited on 24 October 2023, at 08:28 (UTC).

    Text is available under the Creative Commons Attribution-ShareAlike License 4.0; additional terms may apply. By using this site, you agree to the Terms of Use and Privacy Policy. Wikipedia® is a registered trademark of the Wikimedia Foundation, Inc., a non-profit organization.



    Privacy policy

    About Wikipedia

    Disclaimers

    Contact Wikipedia

    Code of Conduct

    Developers

    Statistics

    Cookie statement

    Mobile view



    Wikimedia Foundation
    Powered by MediaWiki