Application | Comment | Organism |
---|---|---|
drug development | the enzyme is a target for antimicrobial drug development | Xanthomonas campestris |
Cloned (Comment) | Organism |
---|---|
overexpression in Escherichia coli wild type and SeMet-substituted protein | Xanthomonas campestris pv. campestris |
overexpression of N-terminally His6-tagged SeMet-substituted XC1936 apo-form in Escherichia coli strain BL21(DE3) | Xanthomonas campestris |
Crystallization (Comment) | Organism |
---|---|
of the apo-form, crystallization improves by a strong magnetic field, optimum buffer for solubilization is 20 mM N-(2-acetamido)iminodiacetic acid, pH 6.8, 0.02% NaN3 and 5 mM 2-mercaptoethanol | Xanthomonas campestris pv. campestris |
purified recombinant SeMet-substituted apo-enzyme XC1936, crystallization in a strong magnetic field, protein in 5 mM 2-mercaptoethanol, 100 mM N-(2-acetamido)-2-iminodiacetic acid, pH 6.8, and 0.02% NaN3, optimization of the reservoir solution, 25°C, X-ray diffraction structure determination and analysis at 2.35 A resolution | Xanthomonas campestris |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Xanthomonas campestris | bacterial UMP kinases are crucial enzymes that are responsible for microbial UTP biosynthesis, and bacterial UMPKs are specific for the phosphorylation of UMP only showing no dual activity in contrast to eukaryotic enzymes | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Xanthomonas campestris | - |
pathovar campestris, strain 17, gene XC1936 | - |
Xanthomonas campestris pv. campestris | - |
XC1936 gene fragment | - |
Xanthomonas campestris pv. campestris 17 | - |
XC1936 gene fragment | - |
Purification (Comment) | Organism |
---|---|
of the recombinant protein | Xanthomonas campestris pv. campestris |
recombinant N-terminally His6-tagged SeMet-substituted XC1936 apo-form from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis, the His-tag is cleaved off by tobacco etch virus protease | Xanthomonas campestris |
Renatured (Comment) | Organism |
---|---|
commentary | Xanthomonas campestris pv. campestris |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + UMP | - |
Xanthomonas campestris pv. campestris | ADP + UDP | - |
r | |
ATP + UMP | - |
Xanthomonas campestris pv. campestris 17 | ADP + UDP | - |
r | |
additional information | bacterial UMP kinases are crucial enzymes that are responsible for microbial UTP biosynthesis, and bacterial UMPKs are specific for the phosphorylation of UMP only showing no dual activity in contrast to eukaryotic enzymes | Xanthomonas campestris | ? | - |
? | |
additional information | the enzyme possesses well defined loop regions involved in substrate-analogue binding, overview | Xanthomonas campestris | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
hexamer | gel permeation | Xanthomonas campestris pv. campestris |
Synonyms | Comment | Organism |
---|---|---|
More | the enzyme belongs to the the amino-acid kinase superfamily | Xanthomonas campestris |
UMP kinase | - |
Xanthomonas campestris pv. campestris |
UMPK | - |
Xanthomonas campestris |
UMPKs | - |
Xanthomonas campestris pv. campestris |
uridine monophosphate kinase | - |
Xanthomonas campestris pv. campestris |
uridylate kinase | - |
Xanthomonas campestris pv. campestris |
XC1936 | - |
Xanthomonas campestris |