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 |
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 |
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 |
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 |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.7.4.22 | UTP | UTP inhibition, but not GTP activation, is sensitive to Mg2+ levels | Bacillus anthracis |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
2.7.4.22 | cytosol | - |
Bacillus anthracis | 5829 | - |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.7.4.22 | Mg2+ | - |
Bacillus anthracis |
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 | - |
? |
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) | - |
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 |
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 | - |
? |
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 |
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 |
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 |