Uridine 5'-monophosphate synthase: Difference between revisions
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<StructureSection load=' | <StructureSection load='' size='350' side='right' caption='Human uridine 5-monophosphate synthase OPD subunit dimer complex with UMP [[2qcd]]' scene='52/526172/Cv/1' pspeed='8'> | ||
== Function == | == Function == | ||
'''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 | '''Uridine 5’-monophosphate synthase''' (UMPS) is a bifunctional enzyme which 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) or '''OMP decarboxylase''' which decarboxylates OMP to form UMP. Potent inhibitors of OPD are BMP – a barbituric acid derivative and xanthosine-5'-monophosphate (XMP). | ||
== Disease == | == Disease == | ||
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== Structural highlights == | == Structural highlights == | ||
UMPS contains UMP in its nucleotide-binding pocket<ref>PMID:18184586</ref>. | <scene name='52/526172/Cv/8'>UMPS contains UMP</scene> in its <scene name='52/526172/Cv/9'>nucleotide-binding pocket</scene><ref>PMID:18184586</ref> (the surface of chain B doesn't shown). Water molecules are shown as red spheres. | ||
==3D structures of uridine 5'-monophosphate synthase== | |||
[[Uridine 5'-monophosphate synthase 3D structures]] | |||
</StructureSection> | </StructureSection> | ||
==References== | ==References== | ||
<references /> | <references /> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] |