Uridine 5'-monophosphate synthase

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<StructureSection load='2qcd' size='450' side='right' caption='Human uridine 5-monophosphate synthase OPD subunit dimer complex with UMP [[2qcd]]' scene='52/526172/Cv/1' pspeed='8'>
<StructureSection load='2qcd' size='450' side='right' caption='Human uridine 5-monophosphate synthase OPD subunit dimer complex with UMP [[2qcd]]' scene='52/526172/Cv/1' pspeed='8'>
== Function ==
== Function ==
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'''Uridine 5’-monophosphate synthase''' (UMPS) is a bifunctional enzyme catalyzes the formation of uridine monophosphate (UMP)<ref>PMID:8631878</ref>. UMPS N-terminal domain is an '''orotate phosphoribosyl transferase''' (OPRT) subunit which catalyzes the addition of ribose-phosphate to orotate forming orotidine 5’-monophosphate (OMP). The C-terminal subunit is '''orotidine 5’-phosphate decarboxylase''' (OPD) which decarboxylates OMP to form UMP. A potent inhibitor of OPD is BMP – a barbituric acid derivative.
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'''Uridine 5’-monophosphate synthase''' (UMPS) is a bifunctional enzyme catalyzes the formation of uridine monophosphate (UMP)<ref>PMID:8631878</ref>. UMPS N-terminal domain is an '''orotate phosphoribosyltransferase''' (OPRT) subunit which catalyzes the addition of ribose-phosphate to orotate forming orotidine 5’-monophosphate (OMP). The C-terminal subunit is '''orotidine 5’-phosphate decarboxylase''' (OPD) which decarboxylates OMP to form UMP. A potent inhibitor of OPD is BMP – a barbituric acid derivative.
== Disease ==
== Disease ==
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**[[3ve7]] – MsOPD + BMP <br />
**[[3ve7]] – MsOPD + BMP <br />
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*Uridine 5’-monophosphate synthase OPRT subunit complex
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*Uridine 5’-monophosphate synthase OPRT subunit see orotate phosphoribosyltransferase in [[Phosphoribosyltransferase]]
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**[[2wns]] - hOPRT + OMP<br />
 
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**[[4wml]] – yOPRT + phosphoribosyl pyrophosphate<br />
 
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**[[1lh0]], [[1opr]] – StOPRT + MgPRPP + orotate – ''Salmonella typhimurium''<br />
 
}}
}}

Revision as of 21:06, 13 October 2017

Human uridine 5-monophosphate synthase OPD subunit dimer complex with UMP 2qcd

Drag the structure with the mouse to rotate

3D structures of uridine 5'-monophosphate synthase

Updated on 13-October-2017

References

  1. ↑ Yablonski MJ, Pasek DA, Han BD, Jones ME, Traut TW. Intrinsic activity and stability of bifunctional human UMP synthase and its two separate catalytic domains, orotate phosphoribosyltransferase and orotidine-5'-phosphate decarboxylase. J Biol Chem. 1996 May 3;271(18):10704-8. PMID:8631878
  2. ↑ Grohmann K, Lauffer H, Lauenstein P, Hoffmann GF, Seidlitz G. Hereditary orotic aciduria with epilepsy and without megaloblastic anemia. Neuropediatrics. 2015 Apr;46(2):123-5. doi: 10.1055/s-0035-1547341. Epub 2015 Mar, 10. PMID:25757096 doi:http://dx.doi.org/10.1055/s-0035-1547341
  3. ↑ Schwenger B, Schober S, Simon D. DUMPS cattle carry a point mutation in the uridine monophosphate synthase gene. Genomics. 1993 Apr;16(1):241-4. PMID:8486364 doi:http://dx.doi.org/10.1006/geno.1993.1165
  4. ↑ Wittmann JG, Heinrich D, Gasow K, Frey A, Diederichsen U, Rudolph MG. Structures of the human orotidine-5'-monophosphate decarboxylase support a covalent mechanism and provide a framework for drug design. Structure. 2008 Jan;16(1):82-92. PMID:18184586 doi:http://dx.doi.org/10.1016/j.str.2007.10.020

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