Uridine 5'-monophosphate synthase: Difference between revisions
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<StructureSection load='2qcd' size=' | <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 == | ||
'''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. | '''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. | ||