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'''Nucleotidyltransferases''' are [[transferase]] enzymes of phosphorus-containing groups, e.g., [[substituent]]s of nucleotidylic acids or simply [[nucleoside monophosphate]]s. The general reaction of transferring a nucleoside monophosphate moiety from A to B, can be written as:
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:A-'''P-N''' + B <math>\rightleftharpoons</math> A + B-'''P-N'''
For example, in the case of polymerases, A is pyrophosphate and B is the nascent polynucleotide.
They are classified under [[Enzyme Commission number|EC number]] 2.7.7 and they can be categorised into:
#[[Uridylyltransferase]]s, which transfer [[uridylyl]]- groups
#[[Adenylyltransferase]]s, which transfer [[adenylyl]]- groups
#[[Guanylyltransferase]]s, which transfer [[guanylyl]]- groups
#[[Cytitidylyltransferase]]s, which transfer [[cytidylyl]]- groups
#[[Thymidylyltransferase]]s, which transfer [[thymidylyl]]- groups
 
==Role in DNA repair mechanisms==
 
Nucleotidyl transferase is a component of the repair pathway for single nucleotide [[base excision repair]]. This repair mechanism begins when a single nucleotide is recognized by DNA [[glycosylase]] as incorrectly matched or has been mutated in some way (UV light, chemical mutagen, etc.), and is removed.  Later, a nucleotidyl tranferase is used to fill in the gap with the correct base, using the [[template strand]] as the reference.
<ref>
{{cite journal
| doi = 10.1074/jbc.M611295200
| quotes =
| author = Yuan Liu, Rajendra Prasad, William A. Beard, Padmini S. Kedar, Esther W. Hou, David D. Shock, and Samuel H. Wilson
| date = May 4, 2007
| title = Coordination of Steps in Single-nucleotide Base Excision Repair Mediated by Apurinic/Apyrimidinic Endonuclease 1 and DNA Polymerase β
| journal = Journal of Biological Chemistry
| volume = 282
| issue = 18
| pages = 13532–13541
| pmid = 17355977
| pmc = 2366199
| url = http://www.jbc.org/content/282/18/13532.full.pdf+html
| quote = The enzymes and accessory factors involved in the BER subpathways in mammalian cells have received considerable attention. As summarized above, five distinct enzymatic reaction are involved during SN-BER. These are 1) removal of a modified base by a lesion-specific monofunctional DNA N-glycosylase, 2) 5'-incision of the abasic site by a hydrolytic strand incision enzyme, 3) DNA synthesis by a nucleotidyltransferase, 4) removal of the 5'-dRP group by a'-elimination reaction, and 5) nick sealing by DNA ligase (36, 37)
}}
</ref>
 
==References==
<references/>
 
==External links==
* {{MeshName|Nucleotidyltransferases}}
 
{{Kinases}}
 
[[Category:Transferases]]
[[Category:EC 2.7.7|*]]
 
 
{{transferase-stub}}

Latest revision as of 20:26, 24 May 2014

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