Application | Comment | Organism |
---|---|---|
pharmacology | human UMP synthase enzyme may be a potential cancer drug target | Homo sapiens |
Cloned (Comment) | Organism |
---|---|
expression of His6-tagged GST-fusion enzyme, containing a tobacco etch virus protease site between His6-GST and the target protein, in Escherichia coli | Homo sapiens |
Crystallization (Comment) | Organism |
---|---|
purified detagged recombinant enzyme, 5 mg/ml protein in 20 mM HEPES-NaOH, pH 7.4, sitting-drop setup, mixing with 0.1 M Tris-HCl, pH 8.0, and 1.8 M (NH4)2SO4 in a 1:1 ratio at 22°C, cryoprotection with 20%v/v glycerol in mother liquor, X-ray diffraction structure determination and analysis at 1.85-1.92 A resolution, molecular replacement using data from a highly twinned monoclinic crystal, pseudo-merohedrally twinned crystals, overview | Homo sapiens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
additional information | no metal ion required | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
Orotidine 5'-phosphate | Homo sapiens | UMP synthase is a bifunctional enzyme that catalyzes the penultimate and last steps in the de novo biosynthesis of UMP, the bifunctional enzyme combines the orotate phosphoribosyltransferase and the orotidine-5'-monophosphate decarboxylase activities on a single polypeptide chain | UMP + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P11172 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography, gel filtration, and ultrafiltration | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Orotidine 5'-phosphate | UMP synthase is a bifunctional enzyme that catalyzes the penultimate and last steps in the de novo biosynthesis of UMP, the bifunctional enzyme combines the orotate phosphoribosyltransferase and the orotidine-5'-monophosphate decarboxylase activities on a single polypeptide chain | Homo sapiens | UMP + CO2 | - |
? | |
Orotidine 5'-phosphate | the decarboxylase shows an extremely fast rate acceleration | Homo sapiens | UMP + CO2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
OMP decarboxylase | - |
Homo sapiens |
OMPD | - |
Homo sapiens |
orotidine-5-monophosphate decarboxylase | - |
Homo sapiens |
UMP synthase | - |
Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | no cofactor required | Homo sapiens |