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Literature summary extracted from

  • Meier, C.; Carter, L.G.; Sainsbury, S.; Mancini, E.J.; Owens, R.J.; Stuart, D.I.; Esnouf, R.M.
    The crystal structure of UMP kinase from Bacillus anthracis (BA1797) reveals an allosteric nucleotide-binding site (2008), J. Mol. Biol., 381, 1098-1105.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.4.22 GTP UTP inhibition, but not GTP activation, is sensitive to Mg2+ levels Bacillus anthracis

Application

EC Number Application Comment Organism
2.7.4.22 medicine interest in new therapies against anthrax has arisen from its potential for bioterrorism. The allosteric pocket of the enzyme, with its atypical configuration of side chains, may provide a particularly suitable site for pharmacological intervention Bacillus anthracis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.4.22 expression of the His-tagged enzyme in Escherichia coli strain B834(DE3) Bacillus anthracis
2.7.4.22 vector pDEST14 is transformed into Escherichia coli B834(DE3) Bacillus anthracis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.4.22 purified recombinant enzyme in complex with ATP, 300 nl sitting drops containing 1.5 mg/mL purified protein are mixed with 3.3 mM ATP, 0.33 mM MgCl2, 66 mM Li2SO4, 3% PEG 3000, 33 mM imidazole, pH 8.0, and 20 mM spermine tetrahydrochloride, equilibration against a reservoir solution of 200 mM Li2SO4, 10% PEG 3000, and 100 mM imidazole, pH 8.0, cryoprotection in 70% reservoir solution with 30% glycerol, 2 days, X-ray diffraction structure determination and analysis at 2.82 A resolution Bacillus anthracis
2.7.4.22 UMP kinase in complex with ATP and Mg2+ at 2.82 A resolution, 0.2 M lithium sulfate, 10% polyethylene glycol 3000, 0.1 M imidazole, pH 8.0, space group P 61 2 2, allosteric nucleotide-binding site identified, a structural model for the allosteric regulation presented Bacillus anthracis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.4.22 UTP UTP inhibition, but not GTP activation, is sensitive to Mg2+ levels Bacillus anthracis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.4.22 cytosol
-
 Bacillus anthracis 5829
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.4.22 Mg2+
-
 Bacillus anthracis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.4.22 ATP + UMP Bacillus anthracis
-
 ADP + UDP
-
 ?
2.7.4.22 ATP + UMP Bacillus anthracis an essential metabolic step with a structure-based mechanism for the allosteric behavior of bacterial enzyme, overview ADP + UDP
-
 ?
2.7.4.22 ATP + UMP Bacillus anthracis BA1797 an essential metabolic step with a structure-based mechanism for the allosteric behavior of bacterial enzyme, overview ADP + UDP
-
 ?
2.7.4.22 ATP + UMP Bacillus anthracis BA1797
-
 ADP + UDP
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.4.22 Bacillus anthracis
-
-
-
2.7.4.22 Bacillus anthracis Q81S73 vector pDEST14 is transformed into Escherichia coli B834(DE3)
-
2.7.4.22 Bacillus anthracis BA1797
-
-
-
2.7.4.22 Bacillus anthracis BA1797 Q81S73 vector pDEST14 is transformed into Escherichia coli B834(DE3)
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.4.22 Ni-NTA affinity chromatography and gel filtration Bacillus anthracis
2.7.4.22 recombinant His-tagged enzyme from Escherichia coli strain B834(DE3) by nickel affinity chromatography and gel filtration Bacillus anthracis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.4.22 ATP + UMP
-
 Bacillus anthracis ADP + UDP
-
 ?
2.7.4.22 ATP + UMP an essential metabolic step with a structure-based mechanism for the allosteric behavior of bacterial enzyme, overview Bacillus anthracis ADP + UDP
-
 ?
2.7.4.22 ATP + UMP
-
 Bacillus anthracis BA1797 ADP + UDP
-
 ?
2.7.4.22 ATP + UMP an essential metabolic step with a structure-based mechanism for the allosteric behavior of bacterial enzyme, overview Bacillus anthracis BA1797 ADP + UDP
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.4.22 hexamer trimer of dimers forming a staggered hexagonal ring Bacillus anthracis
2.7.4.22 homohexamer
-
 Bacillus anthracis

Synonyms

EC Number Synonyms Comment Organism
2.7.4.22 More the enzyme belongs to the NMP family Bacillus anthracis
2.7.4.22 UMP kinase
-
 Bacillus anthracis
2.7.4.22 uridine monophosphate kinase
-
 Bacillus anthracis
2.7.4.22 uridylate kinase
-
 Bacillus anthracis

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.4.22 ATP the cofactor, in addition to binding in the active sites, also interacts with separate binding pocket, with an allosteric binding site, located near the center of the hexameric structure Bacillus anthracis