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Literature summary for 2.7.4.22 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
Search for more literature for 2.7.4.22

Activating Compound

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

Cloned(Commentary)

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

Crystallization (Commentary)

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

Protein Variants

Protein Variants Comment Organism
D113A the mutant shows an increased Km value for UMP compared to the wild type enzyme Mycobacterium tuberculosis
F81W the mutant shows an increased Km value for UMP compared to the wild type enzyme Mycobacterium tuberculosis
F81W/S96A the mutant shows a decreased Km value for UMP compared to the wild type enzyme Mycobacterium tuberculosis
P139A the mutant shows a decreased Km value for UMP compared to the wild type enzyme Mycobacterium tuberculosis
P139H the mutant shows a decreased Km value for UMP compared to the wild type enzyme Mycobacterium tuberculosis
P139W the mutant shows a decreased Km value for UMP compared to the wild type enzyme Mycobacterium tuberculosis
R150A the mutant shows a decreased Km value for UMP compared to the wild type enzyme Mycobacterium tuberculosis
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

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

KM Value [mM]

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

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Mycobacterium tuberculosis

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WHK5
-
-
Mycobacterium tuberculosis H37Rv P9WHK5
-
-

Purification (Commentary)

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

Storage Stability

Storage Stability Organism
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)

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

Subunits

Subunits Comment Organism
hexamer
-
 Mycobacterium tuberculosis

Synonyms

Synonyms Comment Organism
Rv2883c
-
 Mycobacterium tuberculosis
UMPK
-
 Mycobacterium tuberculosis
uridine monophosphate kinase
-
 Mycobacterium tuberculosis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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]

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

IC50 Value

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