Literature summary for 4.1.1.23 extracted from

Wittmann, J.G.; Rudolph, M.G.
Pseudo-merohedral twinning in monoclinic crystals of human orotidine-5-monophosphate decarboxylase (2007), Acta Crystallogr. Sect. D, 63, 744-749.

Application

Application	Comment	Organism
pharmacology	human UMP synthase enzyme may be a potential cancer drug target	Homo sapiens

Cloned(Commentary)

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 (Commentary)

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

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

Metals/Ions	Comment	Organism	Structure
additional information	no metal ion required	Homo sapiens

Natural Substrates/ Products (Substrates)

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

Organism	UniProt	Comment	Textmining
Homo sapiens	P11172	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography, gel filtration, and ultrafiltration	Homo sapiens

Substrates and Products (Substrate)

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

Synonyms	Comment	Organism
OMP decarboxylase	-	Homo sapiens
OMPD	-	Homo sapiens
orotidine-5-monophosphate decarboxylase	-	Homo sapiens
UMP synthase	-	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
additional information	no cofactor required	Homo sapiens