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Literature summary extracted from

  • Tu, J.L.; Chin, K.H.; Wang, A.H.; Chou, S.H.
    The crystallization of apo-form UMP kinase from Xanthomonas campestris is significantly improved in a strong magnetic field (2007), Acta Crystallogr. Sect. F, 63, 438-442.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
2.7.4.22 drug development the enzyme is a target for antimicrobial drug development Xanthomonas campestris

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.4.22 overexpression in Escherichia coli wild type and SeMet-substituted protein Xanthomonas campestris pv. campestris
2.7.4.22 overexpression of N-terminally His6-tagged SeMet-substituted XC1936 apo-form in Escherichia coli strain BL21(DE3) Xanthomonas campestris

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.4.22 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
2.7.4.22 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/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.4.22 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

EC Number Organism UniProt Comment Textmining
2.7.4.22 Xanthomonas campestris
-
 pathovar campestris, strain 17, gene XC1936
-
2.7.4.22 Xanthomonas campestris pv. campestris
-
 XC1936 gene fragment
-
2.7.4.22 Xanthomonas campestris pv. campestris 17
-
 XC1936 gene fragment
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.4.22 of the recombinant protein Xanthomonas campestris pv. campestris
2.7.4.22 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 (Commentary)

EC Number Renatured (Comment) Organism
2.7.4.22 commentary Xanthomonas campestris pv. campestris

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.4.22 ATP + UMP
-
 Xanthomonas campestris pv. campestris ADP + UDP
-
 r
2.7.4.22 ATP + UMP
-
 Xanthomonas campestris pv. campestris 17 ADP + UDP
-
 r
2.7.4.22 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 ?
-
 ?
2.7.4.22 additional information the enzyme possesses well defined loop regions involved in substrate-analogue binding, overview Xanthomonas campestris ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.4.22 hexamer gel permeation Xanthomonas campestris pv. campestris

Synonyms

EC Number Synonyms Comment Organism
2.7.4.22 More the enzyme belongs to the the amino-acid kinase superfamily Xanthomonas campestris
2.7.4.22 UMP kinase
-
 Xanthomonas campestris pv. campestris
2.7.4.22 UMPK
-
 Xanthomonas campestris
2.7.4.22 UMPKs
-
 Xanthomonas campestris pv. campestris
2.7.4.22 uridine monophosphate kinase
-
 Xanthomonas campestris pv. campestris
2.7.4.22 uridylate kinase
-
 Xanthomonas campestris pv. campestris
2.7.4.22 XC1936
-
 Xanthomonas campestris