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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: | |||
: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}} | |||
Revision as of 20:00, 5 April 2013
Nucleotidyltransferases are transferase enzymes of phosphorus-containing groups, e.g., substituents of nucleotidylic acids or simply nucleoside monophosphates. The general reaction of transferring a nucleoside monophosphate moiety from A to B, can be written as:
- A-P-N + B A + B-P-N
For example, in the case of polymerases, A is pyrophosphate and B is the nascent polynucleotide. They are classified under EC number 2.7.7 and they can be categorised into:
- Uridylyltransferases, which transfer uridylyl- groups
- Adenylyltransferases, which transfer adenylyl- groups
- Guanylyltransferases, which transfer guanylyl- groups
- Cytitidylyltransferases, which transfer cytidylyl- groups
- Thymidylyltransferases, 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. [1]
References
- ↑
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