Uracil phosphoribosyltransferase: Difference between revisions

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'''Uracil phosphoribosyltransferase''' is an enzyme which creates [[Uridine monophosphate|UMP]] from [[uracil]] and [[phosphoribosylpyrophosphate]]. This protein may use the [[morpheein]] model of [[allosteric regulation]].<ref name=pmid22182754>{{cite journal |author1 = T. Selwood |author2 =E. K. Jaffe. | title = Dynamic dissociating homo-oligomers and the control of protein function. | journal = Arch. Biochem. Biophys. | volume = 519| issue = 2| pages = 131–43| year = 2011 | pmid = 22182754 | doi=10.1016/j.abb.2011.11.020 | pmc=3298769}}</ref>
'''Uracil phosphoribosyltransferase''' is an enzyme which creates [[Uridine monophosphate|UMP]] from [[uracil]] and [[phosphoribosylpyrophosphate]]. This protein may use the [[morpheein]] model of [[allosteric regulation]].<ref name=pmid22182754>{{cite journal | vauthors = Selwood T, Jaffe EK | title = Dynamic dissociating homo-oligomers and the control of protein function | journal = Archives of Biochemistry and Biophysics | volume = 519 | issue = 2 | pages = 131–43 | date = March 2012 | pmid = 22182754 | pmc = 3298769 | doi = 10.1016/j.abb.2011.11.020 }}</ref>


== References ==
== References ==
<references />
<references />


==External links==
== External links ==
* {{MeshName|Uracil+phosphoribosyltransferase}}
* {{MeshName|Uracil+phosphoribosyltransferase}}
* {{EC number|2.4.2.9}}
* {{EC number|2.4.2.9}}
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[[Category:EC 2.4.2]]
[[Category:EC 2.4.2]]


{{2.4-enzyme-stub}}
{{2.4-enzyme-stub}}

Latest revision as of 04:58, 20 March 2018

uracil phosphoribosyltransferase (FUR1) homolog (S. cerevisiae)
Identifiers
SymbolUPRT
Entrez139596
HUGO28334
RefSeqNM_145052
UniProtQ96BW1
Other data
LocusChr. X q13.3

Uracil phosphoribosyltransferase is an enzyme which creates UMP from uracil and phosphoribosylpyrophosphate. This protein may use the morpheein model of allosteric regulation.[1]

References

  1. Selwood T, Jaffe EK (March 2012). "Dynamic dissociating homo-oligomers and the control of protein function". Archives of Biochemistry and Biophysics. 519 (2): 131–43. doi:10.1016/j.abb.2011.11.020. PMC 3298769. PMID 22182754.

External links