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Literature summary extracted from

  • Labesse, G.; Benkali, K.; Salard-Arnaud, I.; Gilles, A.M.; Munier-Lehmann, H.
    Structural and functional characterization of the Mycobacterium tuberculosis uridine monophosphate kinase: insights into the allosteric regulation (2011), Nucleic Acids Res., 39, 3458-3472.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.4.22 5-fluoro-UTP below 0.15 mM 5-fluoro-UTP increases the activity of the enzyme by 80% Mycobacterium tuberculosis
2.7.4.22 GMP much weaker activator (only 30% increase in activity at 2.5 mM) Mycobacterium tuberculosis
2.7.4.22 GMP-4-nitrophenol much weaker activator (only 50% increase in activity at 1 mM) Mycobacterium tuberculosis
2.7.4.22 GTP GTP increases the reaction rate by a factor of 3.5, with half-saturation at 0.1 mM Mycobacterium tuberculosis
2.7.4.22 additional information GMP-PCP and 8-bromo-GTP are ineffective as activators Mycobacterium tuberculosis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.4.22 expressed in Escherichia coli BL21(DE3)/pDIA17 cells Mycobacterium tuberculosis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.4.22 using sodium/potassium tartrate (1.2 M) at pH 7.4 and 10 mM GTP Mycobacterium tuberculosis

Protein Variants

EC Number Protein Variants Comment Organism
2.7.4.22 D113A the mutant shows an increased Km value for UMP compared to the wild type enzyme Mycobacterium tuberculosis
2.7.4.22 F81W the mutant shows an increased Km value for UMP compared to the wild type enzyme Mycobacterium tuberculosis
2.7.4.22 F81W/S96A the mutant shows a decreased Km value for UMP compared to the wild type enzyme Mycobacterium tuberculosis
2.7.4.22 P139A the mutant shows a decreased Km value for UMP compared to the wild type enzyme Mycobacterium tuberculosis
2.7.4.22 P139H the mutant shows a decreased Km value for UMP compared to the wild type enzyme Mycobacterium tuberculosis
2.7.4.22 P139W the mutant shows a decreased Km value for UMP compared to the wild type enzyme Mycobacterium tuberculosis
2.7.4.22 R150A the mutant shows a decreased Km value for UMP compared to the wild type enzyme Mycobacterium tuberculosis
2.7.4.22 R82H the mutant shows an increased Km value for UMP compared to the wild type enzyme and 0.7% of the wild-type specific activity Mycobacterium tuberculosis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.4.22 5-bromo-UMP weak competitive inhibitor Mycobacterium tuberculosis
2.7.4.22 5-fluoro-UTP at 0.6mM 5-fluoro-UTP, the enzyme activity is decreased by 40% Mycobacterium tuberculosis
2.7.4.22 5-iodo-UTP strongest inhibitor Mycobacterium tuberculosis
2.7.4.22 dTTP
-
 Mycobacterium tuberculosis
2.7.4.22 dUMP weak competitive inhibitor Mycobacterium tuberculosis
2.7.4.22 dUTP
-
 Mycobacterium tuberculosis
2.7.4.22 UTP
-
 Mycobacterium tuberculosis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.4.22 0.0023
-
 UMP mutant enzyme P139H, at pH 7.4 and 30°C Mycobacterium tuberculosis
2.7.4.22 0.0034
-
 UMP mutant enzyme F81W/S96A, at pH 7.4 and 30°C Mycobacterium tuberculosis
2.7.4.22 0.0061
-
 UMP mutant enzyme P139W, at pH 7.4 and 30°C Mycobacterium tuberculosis
2.7.4.22 0.0066
-
 UMP mutant enzyme P139A, at pH 7.4 and 30°C Mycobacterium tuberculosis
2.7.4.22 0.014
-
 UMP mutant enzyme R150A, at pH 7.4 and 30°C Mycobacterium tuberculosis
2.7.4.22 0.0177
-
 UMP wild type enzyme, at pH 7.4 and 30°C Mycobacterium tuberculosis
2.7.4.22 0.0639
-
 UMP mutant enzyme F81W, at pH 7.4 and 30°C Mycobacterium tuberculosis
2.7.4.22 0.0891
-
 UMP mutant enzyme R82H, at pH 7.4 and 30°C Mycobacterium tuberculosis
2.7.4.22 0.2
-
 UMP mutant enzyme D113A, at pH 7.4 and 30°C Mycobacterium tuberculosis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.4.22 Mg2+ required Mycobacterium tuberculosis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.4.22 173200
-
 sedimentation equilibrium ultracentrifugation Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
2.7.4.22 Mycobacterium tuberculosis P9WHK5
-
-
2.7.4.22 Mycobacterium tuberculosis H37Rv P9WHK5
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.4.22 TALON resin column chromatography and Superdex 200 gel filtration Mycobacterium tuberculosis

Storage Stability

EC Number Storage Stability Organism
2.7.4.22 4°C, in 20 mM phosphate (pH 7.0) and 100 mM NaCl, about 2 months, no apparent loss of activity Mycobacterium tuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.4.22 ATP + UMP
-
 Mycobacterium tuberculosis ADP + UDP
-
 ?
2.7.4.22 ATP + UMP
-
 Mycobacterium tuberculosis H37Rv ADP + UDP
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.4.22 hexamer
-
 Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
2.7.4.22 Rv2883c
-
 Mycobacterium tuberculosis
2.7.4.22 UMPK
-
 Mycobacterium tuberculosis
2.7.4.22 uridine monophosphate kinase
-
 Mycobacterium tuberculosis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.7.4.22 60 75 the enzyme shows Tm values of 60°C in the absence of nucleotides and 65°C and 75°C with 1 mM GTP and UTP, respectively Mycobacterium tuberculosis

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.7.4.22 1
-
 5-bromo-UMP Ki above 1 mM, wild type enzyme, at pH 7.4 and 30°C Mycobacterium tuberculosis

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
2.7.4.22 0.02
-
 wild type enzyme, at pH 7.4 and 30°C Mycobacterium tuberculosis 5-iodo-UTP
2.7.4.22 0.1
-
 wild type enzyme, at pH 7.4 and 30°C Mycobacterium tuberculosis UTP
2.7.4.22 0.24
-
 wild type enzyme, at pH 7.4 and 30°C Mycobacterium tuberculosis dUTP
2.7.4.22 0.4
-
 wild type enzyme, at pH 7.4 and 30°C Mycobacterium tuberculosis dTTP