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ATP + 5-fluoro-UMP
ADP + 5-fluoro-UDP
ATP + 6-aza-UMP
ADP + 6-aza-UDP
ATP + dUMP
ADP + dUDP
3.7% of the activity detected with UMP
-
-
?
GTP + UMP
GDP + UDP
reaction rate is 3-5% of that with ATP
-
-
r
MgATP2- + UMP
MgADP- + UDP
-
-
-
?
additional information
?
-
ATP + 5-fluoro-UMP
ADP + 5-fluoro-UDP
-
-
-
?
ATP + 5-fluoro-UMP
ADP + 5-fluoro-UDP
-
-
-
?
ATP + 6-aza-UMP
ADP + 6-aza-UDP
-
-
-
?
ATP + 6-aza-UMP
ADP + 6-aza-UDP
-
-
-
?
ATP + UMP
ADP + UDP
Q81S73
-
-
-
?
ATP + UMP
ADP + UDP
Q81S73
an essential metabolic step with a structure-based mechanism for the allosteric behavior of bacterial enzyme, overview
-
-
?
ATP + UMP
ADP + UDP
Q81S73
-
-
-
?
ATP + UMP
ADP + UDP
Q81S73
an essential metabolic step with a structure-based mechanism for the allosteric behavior of bacterial enzyme, overview
-
-
?
ATP + UMP
ADP + UDP
-
-
-
?
ATP + UMP
ADP + UDP
-
-
-
r
ATP + UMP
ADP + UDP
pH 7.4, 2 mM MgCl2, 30°C
-
-
?
ATP + UMP
ADP + UDP
-
-
-
-
r
ATP + UMP
ADP + UDP
-
-
-
?
ATP + UMP
ADP + UDP
-
-
-
-
?
ATP + UMP
ADP + UDP
-
-
-
?
ATP + UMP
ADP + UDP
-
-
-
-
?
ATP + UMP
ADP + UDP
-
-
-
?
ATP + UMP
ADP + UDP
-
-
-
-
?
ATP + UMP
ADP + UDP
-
-
-
?
ATP + UMP
ADP + UDP
-
-
-
r
ATP + UMP
ADP + UDP
-
-
-
r
ATP + UMP
ADP + UDP
30°C, pH 6, 7.4 or 8, 2 mM MgCl2
-
-
?
ATP + UMP
ADP + UDP
30°C, pH 7.4
-
-
?
ATP + UMP
ADP + UDP
30°C, pH 7.4, 2 mM MgCl2
-
-
?
ATP + UMP
ADP + UDP
30°C, pH 7.4, 2 mM MgCl2
-
-
r
ATP + UMP
ADP + UDP
30°C, pH 7.4, 5 mM MgCl2
-
-
?
ATP + UMP
ADP + UDP
at 30°C, pH 7.4, in the presence of 2 mM MgCl2
-
-
?
ATP + UMP
ADP + UDP
pH 7.4, 2 mM MgCl2, 30°C
-
-
?
ATP + UMP
ADP + UDP
the enzyme regulatory mechanisms involve GTP and UTP, overview
-
-
?
ATP + UMP
ADP + UDP
movements induced by binding uridine nucleotides, GTP and UTP interaction mechanism, analysis, overview
-
-
?
ATP + UMP
ADP + UDP
-
-
-
-
r
ATP + UMP
ADP + UDP
-
-
-
?
ATP + UMP
ADP + UDP
-
-
-
-
?
ATP + UMP
ADP + UDP
-
-
-
?
ATP + UMP
ADP + UDP
-
-
-
r
ATP + UMP
ADP + UDP
-
-
-
?
ATP + UMP
ADP + UDP
-
-
-
r
ATP + UMP
ADP + UDP
-
-
-
r
ATP + UMP
ADP + UDP
-
-
-
?
ATP + UMP
ADP + UDP
low activity with dUMP as substrate, no activity with CMP, dTMP, AMP, IMP, XMP, GMP, low activity with dATP, GTP, CTP and UTP as substrate
-
-
r
ATP + UMP
ADP + UDP
high substrate specificity toward UMP and ATP
-
-
?
ATP + UMP
ADP + UDP
-
-
-
-
r
ATP + UMP
ADP + UDP
-
-
-
?
ATP + UMP
ADP + UDP
30°C, pH 7.4
-
-
?
ATP + UMP
ADP + UDP
37°C, pH 7.8, 7.5 mM MgCl2
-
-
?
ATP + UMP
ADP + UDP
-
-
-
?
ATP + UMP
ADP + UDP
37°C, pH 7.8, 7.5 mM MgCl2
-
-
?
ATP + UMP
ADP + UDP
-
-
-
?
ATP + UMP
ADP + UDP
37°C, pH 7.8, 7.5 mM MgCl2
-
-
?
ATP + UMP
ADP + UDP
-
-
-
?
ATP + UMP
ADP + UDP
37°C, pH 7.8, 7.5 mM MgCl2
-
-
?
ATP + UMP
ADP + UDP
-
-
-
?
ATP + UMP
ADP + UDP
37°C, pH 7.8, 7.5 mM MgCl2
-
-
?
ATP + UMP
ADP + UDP
-
-
-
?
ATP + UMP
ADP + UDP
37°C, pH 7.8, 7.5 mM MgCl2
-
-
?
ATP + UMP
ADP + UDP
-
-
-
-
r
ATP + UMP
ADP + UDP
-
-
-
?
ATP + UMP
ADP + UDP
-
UMP kinase catalyzes the transfer of the gamma-phosphate of ATP to UMP
-
-
r
ATP + UMP
ADP + UDP
-
-
-
?
ATP + UMP
ADP + UDP
-
-
-
-
r
ATP + UMP
ADP + UDP
-
UMP kinase catalyzes the transfer of the gamma-phosphate of ATP to UMP
-
-
r
ATP + UMP
ADP + UDP
-
-
-
-
r
ATP + UMP
ADP + UDP
-
-
-
?
ATP + UMP
ADP + UDP
at 37°C, pH 7.5, in the presence of MnCl2 or MgCl2
-
-
?
ATP + UMP
ADP + UDP
two-substrate kinetics with UMP and ATP
-
-
r
ATP + UMP
ADP + UDP
-
-
-
-
r
ATP + UMP
ADP + UDP
-
-
-
-
r
ATP + UMP
ADP + UDP
-
-
-
-
r
ATP + UMP
ADP + UDP
-
-
-
-
r
additional information
?
-
no reaction with dUMP, CMP, dCMP or TMP as substrate
-
-
?
additional information
?
-
-
no reaction with dUMP, CMP, dCMP or TMP as substrate
-
-
?
additional information
?
-
Asp93 appears as one of the key amino acids in the transfer of information from the regulatory site to the active site
-
-
?
additional information
?
-
-
Asp93 appears as one of the key amino acids in the transfer of information from the regulatory site to the active site
-
-
?
additional information
?
-
-
no activity with CMP, dTMP, or the purine nucleotides (AMP, IMP, XMP, and GMP), ATP is by far the most effective phosphoryl donor, although a very weak activity (less than 1% of ATP activity) is seen with dATP, GTP, CTP, and UTP
-
-
?
additional information
?
-
no activity with CMP, dTMP, or the purine nucleotides (AMP, IMP, XMP, and GMP), ATP is by far the most effective phosphoryl donor, although a very weak activity (less than 1% of ATP activity) is seen with dATP, GTP, CTP, and UTP
-
-
?
additional information
?
-
-
UMP kinase exhibits an intrinsic fluorescence, due to its unique tryptophan, decreasing with the increase of UTP concentration
-
-
?
additional information
?
-
-
enzyme activity detection by the coupled pyruvate kinase/lactate dehydrogenase assay, UMP kinase assay development and optimization, overview
-
-
?
additional information
?
-
-
enzyme activity detection by the coupled pyruvate kinase/lactate dehydrogenase assay, UMP kinase assay development and optimization, overview
-
-
?
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
-
-
?
additional information
?
-
-
the enzyme possesses well defined loop regions involved in substrate-analogue binding, overview
-
-
?
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1-[([5-oxo-4-[(2R)-tetrahydrofuran-2-ylmethyl]-4,5-dihydro-1H-1,2,4-triazol-3-yl]sulfanyl)acetyl]piperidine-4-carboxylic acid
-
1-[2-[(2-amino-6-phenylpyrimidin-4-yl)amino]phenyl]ethanone
-
-
2-(4-acetyl-3,5-dimethyl-1H-pyrazol-1-yl)-N-[1-(2-methoxybenzyl)-1H-pyrazol-5-yl]acetamide
-
2-amino-8-(2-oxo-2-phenylethoxy)-1,4,5,9-tetrahydro-6H-purin-6-one
-
10 micromol, 60 min, room temperature, 75% inhibition, crystal enzyme complex structure, overview
2-amino-8-hydroxy-1,4,5,9-tetrahydro-6H-purin-6-one
-
10 micromol, 60 min, room temperature, 18% inhibition
2-amino-8-[2-(2-methylphenyl)-2-oxoethoxy]-1,4,5,9-tetrahydro-6H-purin-6-one
-
10 micromol, 60 min, room temperature, 48% inhibition
2-amino-8-[2-(3-methylphenyl)-2-oxoethoxy]-1,4,5,9-tetrahydro-6H-purin-6-one
-
10 micromol, 60 min, room temperature, 77% inhibition
2-amino-8-[2-(4-fluorophenyl)-2-oxoethoxy]-1,4,5,9-tetrahydro-6H-purin-6-one
-
10 micromol, 60 min, room temperature, 73% inhibition
2-amino-8-[2-(4-hydroxyphenyl)-2-oxoethoxy]-1,4,5,9-tetrahydro-6H-purin-6-one
-
10 micromol, 60 min, room temperature, 77% inhibition
2-amino-8-[2-(4-methoxyphenyl)-2-oxoethoxy]-1,4,5,9-tetrahydro-6H-purin-6-one
-
10 micromol, 60 min, room temperature, 74% inhibition
2-amino-8-[2-(4-methylphenyl)-2-oxoethoxy]-1,4,5,9-tetrahydro-6H-purin-6-one
-
10 micromol, 60 min, room temperature, 80% inhibition
4-[(2-amino-6-oxo-4,5,6,9-tetrahydro-1H-purin-8-yl)methyl]benzonitrile
-
10 micromol, 60 min, room temperature, 53% inhibition, crystal enzyme complex structure, overview
4-[2-amino-4-(4-chlorophenyl)-7-oxo-5,7-dihydro-6H-pyrrolo[3,4-d]pyrimidin-6-yl]butanoic acid
-
4-[2-amino-4-(4-methoxyphenyl)-7-oxo-5,7-dihydro-6H-pyrrolo[3,4-d]pyrimidin-6-yl]butanoic acid
-
4-[[(2-amino-6-oxo-4,5,6,9-tetrahydro-1H-purin-8-yl)oxy]acetyl]benzonitrile
-
10 micromol, 60 min, room temperature, 68% inhibition
5-[(9H-[1,2,4]triazolo[4,3-a]benzimidazol-3-ylsulfanyl)methyl]furan-2-carboxylic acid
hydrogen bonding interactions of ZINC12561276 molecule with the active site residues of Mtb-UMPK homology model, overview
dUMP
weak competitive inhibitor
guanylyl imidodiphosphate
mutant D201N
N-benzyl-2-[(2S,3R,4S,5R)-3,4-dihydroxy-5-[[(methylsulfonyl)amino]methyl]tetrahydrofuran-2-yl]-N-methylacetamide
-
N4,6-diphenylpyrimidine-2,4-diamine
-
-
N4-(2-methoxyphenyl)-6-phenylpyrimidine-2,4-diamine
-
-
N4-(2-methylphenyl)-6-phenylpyrimidine-2,4-diamine
-
-
N4-(3-methylphenyl)-6-phenylpyrimidine-2,4-diamine
-
-
N4-(4-methoxyphenyl)-6-phenylpyrimidine-2,4-diamine
-
-
N4-(4-methylphenyl)-6-phenylpyrimidine-2,4-diamine
-
-
N4-ethyl-N4,6-diphenylpyrimidine-2,4-diamine
-
-
N6-[(4-nitrophenyl)methyl]-N2-[[3-(trifluoromethyl)phenyl]methyl]-1H-purine-2,6-diamine
-
-
phosphate
phosphate-inhibited UpUMPK activity with an IC50 value of 1 mM, the molar content of phosphate in the soluble UMPK is 4%
5-bromo-UMP
-
not inhibitory
5-bromo-UMP
not inhibitory
5-bromo-UMP
-
not inhibitory
5-bromo-UMP
weak competitive inhibitor
5-bromo-UMP
-
not inhibitory
5-Bromo-UTP
-
5-Bromo-UTP
-
less inhibitory than UTP
5-Bromo-UTP
less inhibitory than UTP
5-Bromo-UTP
-
less inhibitory than UTP
5-Bromo-UTP
-
more inhibitory than UTP
5-fluoro-UTP
-
5-fluoro-UTP
at 0.6mM 5-fluoro-UTP, the enzyme activity is decreased by 40%
5-fluoro-UTP
-
less inhibitory than UTP
5-iodo-UMP
-
not inhibitory
5-iodo-UMP
not inhibitory
5-iodo-UMP
-
not inhibitory
5-iodo-UMP
-
not inhibitory
5-iodo-UTP
-
5-iodo-UTP
-
less inhibitory than UTP
5-iodo-UTP
less inhibitory than UTP
5-iodo-UTP
-
less inhibitory than UTP
5-iodo-UTP
strongest inhibitor
5-iodo-UTP
-
more inhibitory than UTP
dUTP
five times weaker than UTP
dUTP
five times weaker than UTP
dUTP
-
five times weaker than UTP
dUTP
-
five times weaker than UTP
GTP
mutant D201N
GTP
mutant D201N is inhibited by GTP above 0.2 mM
GTP
when 0.5 M GTP is added in the reaction mixture the affinity of the enzyme towards its UMP substrate decreases almost by 3folds. GTP increases the affinity of ATP towards the enzyme
GTP
at high concentrations
TTP
not inhibitory
UMP
-
UMP
excess UMP at high concentrations, UTP deminishes this inhibition
UMP
-
excess UMP at high concentrations, UTP deminishes this inhibition
UMP
excess UMP at high concentrations, UTP deminishes this inhibition
UMP
-
excess UMP at high concentrations
UTP
Q81S73
UTP inhibition, but not GTP activation, is sensitive to Mg2+ levels
UTP
inhibition not affected by Mg2+ and UMP
UTP
-
inhibition not affected by Mg2+ and UMP
UTP
the inhibitory effect is maximal at pH 8 and a low (0.1 mM) UMP concentration
UTP
0.25 mM, 0.5 mM, GTP, UMP and high concentrations of Mg2+ protects against inhibition by UTP, decreases the affinity for ATP, inhibition only without Mg2+
UTP
Mg-free competitive cooperative inhibitor, the inhibition is reversible by GTP. UTP and GTP are tightly coupled in both wild-type enzyme and N140A variant
UTP
-
0.25 mM, 0.5 mM, GTP, UMP and high concentrations of Mg2+ protects against inhibition by UTP, decreases the affinity for ATP, inhibition only without Mg2+
UTP
43% inhibition at 0.38 mM, 51.2% inhibition at 0.53 mM. About 21% of UMP kinase activity remains at 0.94-1.33 mM of UTP
UTP
physiological inhibitor
UTP
0.25 mM, 0.5 mM, UMP protects against inhibition by UTP, decreases the affinity for ATP, inhibition only without Mg2+
UTP
binds the enzyme, competitive inhibitor for both substrates; feedback inhibition, competitive inhibitor against both substrates
UTP
potent competitive inhibitor
UTP
decreases the affinity for ATP
UTP
an end-product inhibitor competitive against UMP and noncompetitive towards ATP; UTP is a competitive inhibitor against UMP and a noncompetitive inhibitor towards ATP, the positive cooperativity behavior with ATP is altered by the presence of UTP
additional information
no inhibition by dUMP, CMP, dCMP or TMP
-
additional information
-
no inhibition by dUMP, CMP, dCMP or TMP
-
additional information
structure-based inhibitor design, inhibitor screening and molecular docking study
-
additional information
-
structure-based inhibitor design, inhibitor screening and molecular docking study
-
additional information
-
CTP is not inhibitory
-
additional information
CTP is not inhibitory
-
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additional information
additional information
-
0.11
5-fluoro-UMP
-
0.14
6-aza-UMP
-
0.03
ATP
mutant D146N, at pH 6
0.048
ATP
wild-type, at pH 6
0.048
ATP
wild-type, at pH 6.0
0.081
ATP
in presence of 0.1 mM UMP, at 60°C
0.081
ATP
radioactive assay, 500 microM ATP and 100 microM UMP, at 60°C, the more commonly used photometric assay using auxiliary enzymes is incompatible with high temperature
0.095
ATP
mutant D159N, at pH 6
0.095
ATP
mutant D159N, at pH 6.0
0.1
ATP
mutant D146N, at pH 8
0.12
ATP
at 1 mM UMP, wild-type
0.12
ATP
mutant D77N, at pH 6
0.12
ATP
wild-type, at pH 7.4
0.12
ATP
wild-type, at pH 8
0.14
ATP
mutant D168N, at pH 6
0.15
ATP
in presence of 1.0 mM UMP without GTP
0.17
ATP
mutant D174N, at pH 6
0.19
ATP
pH 7.4, 30°C, wild-type enzyme
0.2
ATP
mutant D201N, at pH 6
0.2
ATP
in presence of 1.0 mM UMP and 0.5 mM GTP
0.23
ATP
in presence of 0.1 mM UMP without GTP
0.24
ATP
mutant R62H, at pH 6
0.26
ATP
in presence of 2.0 mM ATP, 0.5 mM UTP and 0.5 mM GTP
0.27
ATP
in presence of 0.1 mM UMP and 0.5 mM GTP
0.286
ATP
mutant D159N, at pH 7.4
0.29
ATP
mutant D159N, at pH 8
0.304
ATP
in the presence of 2 mM Mg2+, at pH 7.4 and 30°C
0.31
ATP
mutant D174N, at pH 8
0.36
ATP
pH 7.4, 30°C, mutant D93A
0.4
ATP
in the presence of 2 mM Mn2+, at pH 7.4 and 30°C
0.42
ATP
mutant D168N, at pH 8
0.42
ATP
mutant T138A/N140A
0.46
ATP
mutant D201N, at pH 8
0.46
ATP
-
in presence of 0.1 mM UMP and 0.5 mM GTP
0.48
ATP
mutant D77N, at pH 8
0.59
ATP
pH 7.4, 30°C, mutants N72A and N72A/D93A
0.6
ATP
-
in presence of 1.0 mM UMP and 0.5 mM GTP
0.742
ATP
-
pH 7.5, 22°C, random BiBi mechanism
0.77
ATP
in presence of 2.0 mM ATP and 0.5 mM UTP
0.83
ATP
in presence of 0.05 mM UMP and 0.5 mM GTP
0.9
ATP
-
in presence of 1.0 mM UMP and 0.5 mM GTP
0.92
ATP
-
in presence of 1.0 mM UMP and 0.5 mM GTP
0.93
ATP
in presence of 0.1 mM UMP and 0.5 mM GTP
1
ATP
in presence of 0.5 mM UTP
1.485
ATP
-
pH 7.5, 22°C, ordered BiBi mechanism
1.57
ATP
-
in presence of 0.1 mM UMP without GTP
1.62
ATP
-
in presence of 1.0 mM UMP without GTP
1.79
ATP
in presence of 1.0 mM UMP and 0.5 mM GTP
1.98
ATP
in presence of 1.0 mM UMP and 0.5 mM GTP
2.64
ATP
-
in presence of 1.0 mM UMP without GTP
2.98
ATP
in presence of 0.05 mM UMP without GTP
3
ATP
mutant R62H, at pH 8
3.22
ATP
in presence of 1.0 mM UMP without GTP
4.5
ATP
-
in presence of 0.5 mM UTP
9.8
ATP
-
in presence of 1.0 mM UMP without GTP
10.4
ATP
in presence of 0.1 mM UMP without GTP
14.5
ATP
in presence of 1.0 mM UMP without GTP
30
ATP
in presence of 0.5 mM UTP
0.19
MgATP2-
D159N mutant protein, 0.3 mM UMP
0.2
MgATP2-
D159N mutant protein, 1 mM UMP, 0.5 mM GTP
0.21
MgATP2-
D159N mutant protein, 0.3 mM UMP
0.21
MgATP2-
N140A/D159N mutant protein, 0.3 mM UMP, 0.5 mM GTP
0.23
MgATP2-
N140A/D159N mutant protein, 0.3 mM UMP, 0.5 mM GTP, 0.5 mM UTP
0.24
MgATP2-
D159N mutant protein, 0.3 mM UMP, 0.5 mM GTP
0.25
MgATP2-
N140A/D159N mutant protein, 0.3 mM UMP
0.26
MgATP2-
D159N mutant protein, 0.3 mM UMP, 0.5 mM GTP, 0.5 mM UTP
0.27
MgATP2-
D93A/D159N mutant protein, 0.3 mM UMP
0.27
MgATP2-
D93A/D159N mutant protein, 0.3 mM UMP, 0.5 mM GTP
0.36
MgATP2-
D93A/D159N mutant protein, 0.3 mM UMP
0.4
MgATP2-
N72A/D159N mutant protein, 1 mM UMP, 0.5 mM GTP
0.41
MgATP2-
D93A/D159N mutant protein, 1 mM UMP, 0.5 mM GTP
0.53
MgATP2-
N140A/D159N mutant protein, 0.3 mM UMP, 0.5 mM UTP
0.59
MgATP2-
D93A/D159N mutant protein, 0.3 mM UMP, 0.5 mM GTP, 0.5 mM UTP
0.59
MgATP2-
N72A/D159N mutant protein, 0.3 mM UMP
0.59
MgATP2-
N72A/D93A/D159N mutant protein, 0.3 mM UMP
0.64
MgATP2-
D93A/D159N mutant protein, 0.3 mM UMP, 0.5 mM UTP
0.66
MgATP2-
N72A/D93A/D159N mutant protein, 1 mM UMP, 0.5 mM GTP
0.77
MgATP2-
D159N mutant protein, 0.3 mM UMP, 0.5 mM UTP
0.0023
UMP
mutant enzyme P139H, at pH 7.4 and 30°C
0.00276
UMP
purified enzyme, in 50 mM Tris-HCl pH 7.4, at 30°C
0.00281
UMP
crude cytosolic extract, in 50 mM Tris-HCl pH 7.4, at 30°C
0.0034
UMP
mutant enzyme F81W/S96A, at pH 7.4 and 30°C
0.0061
UMP
mutant enzyme P139W, at pH 7.4 and 30°C
0.0066
UMP
mutant enzyme P139A, at pH 7.4 and 30°C
0.008
UMP
in the absence of GTP
0.0087
UMP
in presence of 2.0 mM ATP without GTP
0.01
UMP
in presence of 2.0 mM ATP without GTP
0.014
UMP
in presence of 0.5 mM ATP at 60°C
0.014
UMP
radioactive assay, 500 microM ATP and 100 microM UMP, at 60°C, the more commonly used photometric assay using auxiliary enzymes is incompatible with high temperature
0.014
UMP
mutant enzyme R150A, at pH 7.4 and 30°C
0.0156
UMP
in presence of 10.0 mM ATP without GTP
0.0177
UMP
wild type enzyme, at pH 7.4 and 30°C
0.0238
UMP
pH 7.4, 30°C, mutant D93A
0.0238
UMP
D93A/D159N mutant protein, 2 mM ATP
0.024
UMP
pH 7.4, 30°C, mutant N72A/D93A
0.024
UMP
N72A/D93A/D159N mutant protein, 2 mM ATP
0.0244
UMP
D93A/D159N mutant protein, 2 mM ATP, 0.5 mM GTP
0.0246
UMP
N72A/D93A/D159N mutant protein, 2 mM ATP, 0.5 mM GTP
0.0274
UMP
in presence of 2.0 mM ATP and 0.5 mM GTP
0.0275
UMP
D93A/D159N mutant protein, 0.2 mM ATP, 0.5 mM GTP
0.03
UMP
in the presence of GTP
0.0321
UMP
pH 7.4, 30°C, mutant N72A
0.0321
UMP
N72A/D159N mutant protein, 2 mM ATP
0.0357
UMP
D93A/D159N mutant protein, 0.2 mM ATP
0.04
UMP
-
in presence of 1.0 mM ATP and 0.5 mM GTP
0.04
UMP
-
in presence of 1.0 mM ATP without GTP
0.043
UMP
wild-type, at pH 7.4
0.043
UMP
wild-type, at pH 8
0.043
UMP
-
pH 7.5, 22°C, random BiBi mechanism
0.046
UMP
pH 7.4, 30°C, wild-type enzyme
0.046
UMP
in presence of 2.0 mM ATP without GTP
0.046
UMP
D159N mutant protein, 2 mM ATP
0.047
UMP
in presence of 0.2 mM ATP and 0.5 mM GTP
0.0478
UMP
N72A/D159N mutant protein, 2 mM ATP, 0.5 mM GTP
0.0492
UMP
in presence of 0.2 mM ATP without GTP
0.05
UMP
at 1 mM ATP, wild-type
0.05
UMP
-
in presence of 12.0 mM ATP and 0.5 mM GTP
0.05
UMP
D159N mutant protein, 0.2 mM ATP
0.05
UMP
N140A/D159N mutant protein, 0.2 mM ATP
0.051
UMP
in presence of 2.0 mM ATP and 0.5 mM GTP
0.051
UMP
D159N mutant protein, 2 mM ATP, 0.5 mM GTP
0.052
UMP
mutant D159N, at pH 7.4
0.052
UMP
mutant D159N, at pH 8
0.054
UMP
in the presence of 2 mM Mg2+, at pH 7.4 and 30°C
0.0574
UMP
in presence of 10.0 mM ATP and 0.5 mM GTP
0.059
UMP
mutant D146N, at pH 8
0.0593
UMP
D159N mutant protein, 0.2 mM ATP, 0.5 mM GTP
0.06
UMP
mutant D168N, at pH 8
0.0639
UMP
mutant enzyme F81W, at pH 7.4 and 30°C
0.0739
UMP
N140A/D159N mutant protein, 0.2 mM ATP, 0.5 mM GTP
0.0755
UMP
D93A/D159N mutant protein, 0.2 mM ATP, 0.5 mM GTP, 0.5 mM UTP
0.0788
UMP
D93A/D159N mutant protein, 0.2 mM ATP, 0.5 mM UTP
0.086
UMP
-
pH 7.5, 22°C, ordered BiBi mechanism
0.0891
UMP
mutant enzyme R82H, at pH 7.4 and 30°C
0.0997
UMP
-
in presence of 2.0 mM ATP and 0.5 mM GTP
0.1
UMP
in the presence of MgCl2
0.1
UMP
-
in presence of 12.0 mM ATP without GTP
0.1
UMP
in presence of 2.0 mM ATP and 0.5 mM GTP
0.1056
UMP
-
in presence of 30 mM ATP and 0.5 mM GTP
0.1086
UMP
N140A/D159N mutant protein, 0.2 mM ATP, 0.5 mM GTP, 0.5 mM UTP
0.125
UMP
in the presence of 2 mM Mn2+, at pH 7.4 and 30°C
0.131
UMP
in presence of 30 mM ATP without GTP
0.15
UMP
in the presence of MnCl2
0.15
UMP
-
in presence of 30 mM ATP without GTP
0.155
UMP
in presence of 30 mM ATP and 0.5 mM GTP
0.17
UMP
wild-type, at pH 6
0.17
UMP
wild-type, at pH 6.0
0.1812
UMP
N140A/D159N mutant protein, 0.2 mM ATP, 0.5 mM UTP
0.2
UMP
mutant enzyme D113A, at pH 7.4 and 30°C
0.207
UMP
in presence of 2.0 mM ATP, 0.5 mM UTP and 0.5 mM GTP
0.207
UMP
D159N mutant protein, 0.2 mM ATP, 0.5 mM GTP, 0.5 mM UTP
0.214
UMP
recombinant UpUMPK
0.22
UMP
mutant D201N, at pH 8
0.27
UMP
mutant D159N, at pH 6
0.27
UMP
mutant D159N, at pH 6.0
0.31
UMP
mutant D174N, at pH 8
0.32
UMP
mutant D168N, at pH 6
0.32
UMP
mutant R62H, at pH 8
0.45
UMP
mutant D146N, at pH 6
0.47
UMP
mutant D77N, at pH 8
0.6
UMP
mutant T138A/N140A
0.86
UMP
mutant D201N, at pH 6
1.26
UMP
mutant R62H, at pH 6
1.69
UMP
in presence of 2.0 mM ATP and 0.5 mM UTP
1.69
UMP
D159N mutant protein, 0.2 mM ATP, 0.5 mM UTP
1.78
UMP
mutant D77N, at pH 6
3.7
UMP
mutant D174N, at pH 6
22.2
UMP
-
in presence of 2.0 mM ATP without GTP
additional information
additional information
reaction kinetics
-
additional information
additional information
-
reaction kinetics
-
additional information
additional information
with ATP as the variable substrate, the kinetic curves show a detectable deviation from Michaelis-Menten kinetics, especially at low substrate concentrations, the best fit is therefore to the Hill equation, giving an n value of 1.54 +/- 0.10, demonstrating positive cooperativity with ATP, coupled spectrophotometric assay
-
additional information
additional information
-
with ATP as the variable substrate, the kinetic curves show a detectable deviation from Michaelis-Menten kinetics, especially at low substrate concentrations, the best fit is therefore to the Hill equation, giving an n value of 1.54 +/- 0.10, demonstrating positive cooperativity with ATP, coupled spectrophotometric assay
-
additional information
additional information
MPK exhibited Michaelis-Menten kinetics
-
additional information
additional information
-
MPK exhibited Michaelis-Menten kinetics
-
additional information
additional information
-
steady-state kinetics, velocity curves for the enzyme fit to a steady state random Bi Bi mechanism or ordered Bi Bi mechanism. Data fits both models equally well
-
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4.6
1-[2-[(2-amino-6-phenylpyrimidin-4-yl)amino]phenyl]ethanone
Staphylococcus aureus
-
pH 7.5, 22°C
139
2-amino-8-(2-oxo-2-phenylethoxy)-1,4,5,9-tetrahydro-6H-purin-6-one
Staphylococcus aureus
-
pH 8.5, 23°C
243
2-amino-8-[2-(2-methylphenyl)-2-oxoethoxy]-1,4,5,9-tetrahydro-6H-purin-6-one
Staphylococcus aureus
-
pH 8.5, 23°C
51
2-amino-8-[2-(3-methylphenyl)-2-oxoethoxy]-1,4,5,9-tetrahydro-6H-purin-6-one
Staphylococcus aureus
-
pH 8.5, 23°C
79
2-amino-8-[2-(4-fluorophenyl)-2-oxoethoxy]-1,4,5,9-tetrahydro-6H-purin-6-one
Staphylococcus aureus
-
pH 8.5, 23°C
82
2-amino-8-[2-(4-hydroxyphenyl)-2-oxoethoxy]-1,4,5,9-tetrahydro-6H-purin-6-one
Staphylococcus aureus
-
pH 8.5, 23°C
44
2-amino-8-[2-(4-methoxyphenyl)-2-oxoethoxy]-1,4,5,9-tetrahydro-6H-purin-6-one
Staphylococcus aureus
-
pH 8.5, 23°C
64
2-amino-8-[2-(4-methylphenyl)-2-oxoethoxy]-1,4,5,9-tetrahydro-6H-purin-6-one
Staphylococcus aureus
-
pH 8.5, 23°C
254
4-[(2-amino-6-oxo-4,5,6,9-tetrahydro-1H-purin-8-yl)methyl]benzonitrile
Staphylococcus aureus
-
pH 8.5, 23°C
88
4-[[(2-amino-6-oxo-4,5,6,9-tetrahydro-1H-purin-8-yl)oxy]acetyl]benzonitrile
Staphylococcus aureus
-
pH 8.5, 23°C
0.02
5-iodo-UTP
Mycobacterium tuberculosis
wild type enzyme, at pH 7.4 and 30°C
0.4
dTTP
Mycobacterium tuberculosis
wild type enzyme, at pH 7.4 and 30°C
0.24
dUTP
Mycobacterium tuberculosis
wild type enzyme, at pH 7.4 and 30°C
0.0156
N4,6-diphenylpyrimidine-2,4-diamine
Staphylococcus aureus
-
pH 7.5, 22°C
32.9
N4-(2-methoxyphenyl)-6-phenylpyrimidine-2,4-diamine
Staphylococcus aureus
-
pH 7.5, 22°C
53.8
N4-(2-methylphenyl)-6-phenylpyrimidine-2,4-diamine
Staphylococcus aureus
-
pH 7.5, 22°C
0.1
N4-(3-methylphenyl)-6-phenylpyrimidine-2,4-diamine
Staphylococcus aureus
-
above, pH 7.5, 22°C
0.1
N4-(4-methoxyphenyl)-6-phenylpyrimidine-2,4-diamine
Staphylococcus aureus
-
above, pH 7.5, 22°C
0.1
N4-(4-methylphenyl)-6-phenylpyrimidine-2,4-diamine
Staphylococcus aureus
-
above, pH 7.5, 22°C
0.025
N4-ethyl-N4,6-diphenylpyrimidine-2,4-diamine
Staphylococcus aureus
-
pH 7.5, 22°C
1
phosphate
Ureaplasma parvum
phosphate ion is found in the active site
0.01
UTP
Neisseria meningitidis
at 0.05 mM UMP, UMP protects for inhibition by Mg2+ free UTP
0.1
UTP
Mycobacterium tuberculosis
wild type enzyme, at pH 7.4 and 30°C
0.13
UTP
Neisseria meningitidis
at 0.2 mM UMP, UMP protects for inhibition by Mg2+ free UTP
0.45
UTP
Helicobacter pylori
at pH 7.4 and 30°C
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0.00014
-
R62H/D77N mutant, without UTP, no activity with 1 mM UTP
0.0002
-
R62H mutant, without UTP, no activity with 1 mM UTP
0.0003
-
D77N mutant, without UTP, no activity with 1 mM UTP
0.00613
-
wild-type, with 1 mM UTP
0.011
0-45% ammonium sulfate precipitate
0.01238
-
wild-type, without UTP
0.033
45-55% ammonium sulfate precipitate
0.053
55-80% ammonium sulfate precipitate
0.13
mutant D201N, rate of the reverse reaction
0.15
mutant D146N, at pH 6
0.32
mutant D146N, at pH 8
0.6
with 6-aza-UMP as substrate
1.04
mutant D201N, at pH 6
1.7
-
at 2.0 mM ATP, without GTP
10.2
at 8.0 mM ATP, with 0.5 mM GTP
11.3
at 8.0 mM ATP, without GTP
11.8
-
at 8.0 mM ATP, without GTP
110.5
N140A/D159N mutant protein, 0.3 mM UMP, 0.5 mM GTP
12.8
-
at 8.0 mM ATP, without GTP
124.2
-
at 8.0 mM ATP, with 0.5 mM GTP
126
with UMP as substrate
130
with MnCl2 and ATP as phosphate donor
134.3
-
at 2.0 mM ATP, with 0.5 mM GTP
135
at pH 6.5, in the presence of MnCl2
160
wild-type, in the presence of ATP and GTP
162
with 5-fluoro-UMP as substrate
18.1
at 8.0 mM ATP, without GTP
182
at pH 6.5, in the presence of MgCl2
19.4
-
at 8.0 mM ATP, with 0.5 mM GTP
2.7
at 2.0 mM ATP, without GTP
23.5
-
at 2.0 mM ATP, with 0.5 mM GTP
23.6
-
at 8.0 mM ATP, with 0.5 mM GTP
23.8
D159N mutant protein, 0.3 mM UMP, 0.5 mM UTP
24
with 5-fluoro-UMP as substrate
26.1
at 2.0 mM ATP, without GTP
274
at pH 7.5, in the presence of MnCl2
28.1
at 8.0 mM ATP, without GTP
28.6
at 2.0 mM ATP, with 0.5 mM GTP
3.6
mutant D201N, in the presence of 1 mM ATP and 1 mM UMP
3.7
-
at 2.0 mM ATP, without GTP
30.4
N140A/D159N mutant protein, 0.2 mM ATP, 0.5 mM UTP
36.3
D93A/D159N mutant protein, 0.2 mM ATP, 0.5 mM GTP, 0.5 mM UTP
36.8
D159N mutant protein, 0.2 mM ATP, 0.5 mM UTP
38.1
D93A/D159N mutant protein, 0.2 mM ATP, 0.5 mM UTP
38.4
D93A/D159N mutant protein, 0.2 mM ATP, 0.5 mM GTP
38.9
-
at 8.0 mM ATP, without GTP
39.1
at 8.0 mM ATP, with 0.5 mM GTP
399
at pH 7.5, in the presence of MgCl2
4.6
-
at 2.0 mM ATP, without GTP
40.7
D93A/D159N mutant protein, 0.2 mM ATP
46.1
D159N mutant protein, 0.2 mM ATP
46.6
D159N mutant protein, 0.2 mM ATP, 0.5 mM GTP, 0.5 mM UTP
46.8
-
activity independent of concentrations of ATP, at 2.0 mM ATP, without GTP
47.5
-
at 8.0 mM ATP, without GTP
48.9
N140A/D159N mutant protein, 0.2 mM ATP
5.1
activity dependent of concentrations of ATP, at 2.0 mM ATP, without GTP
51.4
N72A/D93A/D159N mutant protein, 2 mM ATP, 0.5 mM GTP
51.9
D159N mutant protein, 0.2 mM ATP, 0.5 mM GTP
52.7
N72A/D93A/D159N mutant protein, 2 mM ATP
52.8
-
at 2.0 mM ATP, with 0.5 mM GTP
55.7
N140A/D159N mutant protein, 0.2 mM ATP, 0.5 mM GTP, 0.5 mM UTP
57.6
D93A/D159N mutant protein, 0.3 mM UMP, 0.5 mM GTP, 0.5 mM UTP
57.7
at 2.0 mM ATP, with 0.5 mM GTP
58.2
N140A/D159N mutant protein, 0.2 mM ATP, 0.5 mM GTP
60.5
-
at 8.0 mM ATP, with 0.5 mM GTP
60.8
D93A/D159N mutant protein, 0.3 mM UMP, 0.5 mM UTP
61.5
D93A/D159N mutant protein, 0.3 mM UMP
62.3
D93A/D159N mutant protein, 0.3 mM UMP, 0.5 mM GTP
62.4
D159N mutant protein, 0.3 mM UMP
65.9
at 2.0 mM ATP, with 0.5 mM GTP
66
with MgCl2 and ATP as phosphate donor
666
at pH 8.5, in the presence of MnCl2
67
with 6-aza-UMP as substrate
68.5
-
at 2.0 mM ATP, with 0.5 mM GTP
71.1
at 8.0 mM ATP, with 0.5 mM GTP
76.1
N72A/D93A/D159N mutant protein, 1 mM UMP, 0.5 mM GTP
77.1
D93A/D159N mutant protein, 2 mM ATP
78.3
N140A/D159N mutant protein, 0.3 mM UMP, 0.5 mM UTP
78.7
N72A/D93A/D159N mutant protein, 0.3 mM UMP
81.9
N140A/D159N mutant protein, 0.3 mM UMP
83.4
D93A/D159N mutant protein, 2 mM ATP, 0.5 mM GTP
86.6
mutant D168N, at pH 8
87.4
-
at 8.0 mM ATP, with 0.5 mM GTP
9.7
-
at 2.0 mM ATP, with 0.5 mM GTP
90.7
D93A/D159N mutant protein, 0.3 mM UMP
91.7
D159N mutant protein, 0.3 mM UMP, 0.5 mM GTP, 0.5 mM UTP
93.9
D93A/D159N mutant protein, 1 mM UMP, 0.5 mM GTP
98.2
N140A/D159N mutant protein, 0.3 mM UMP, 0.5 mM GTP, 0.5 mM UTP
99.6
D159N mutant protein, 0.3 mM UMP, 0.5 mM GTP
0.003
-
100.3
D159N mutant protein, 2 mM ATP, 0.5 mM GTP
100.3
N72A/D159N mutant protein, 2 mM ATP, 0.5 mM GTP
105
wild-type, at pH 6
128
mutant D159N, at pH 6
128
mutant D159N, at pH 6.0
153
mutant D159N, at pH 7.4
153
mutant D159N, at pH 8
61.6
D159N mutant protein, 0.3 mM UMP
61.6
N72A/D159N mutant protein, 0.3 mM UMP
8.2
mutant D201N, at pH 8
84.2
D159N mutant protein, 1 mM UMP, 0.5 mM GTP
84.2
N72A/D159N mutant protein, 1 mM UMP, 0.5 mM GTP
9.1
-
at 8.0 mM ATP, without GTP
9.1
-
activity independent of concentrations of ATP, at 2.0 mM ATP, without GTP
92.5
D159N mutant protein, 2 mM ATP
92.5
N72A/D159N mutant protein, 2 mM ATP
additional information
R92A, H96A, and R127A exhibit increased enzyme activity
additional information
-
R92A, H96A, and R127A exhibit increased enzyme activity
additional information
GTP and UTP are extremely poor substrates with an activity below 1 micromol/min/mg with MnCl2 or MgCl2
additional information
-
GTP and UTP are extremely poor substrates with an activity below 1 micromol/min/mg with MnCl2 or MgCl2
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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
Q81S73
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
Q81S73
bound to the UMP substrate, resolved at 2.3 A resolution, bound to the UDP product, resolved at 2.6 A resolution, bound to UTP, resolved at 2.45 A resolution
D159N, hanging drop vapor diffusion method
purified recombinant UMP kinase mutant D159N, bound to GTP, by hanging drop vapour diffusion method, 0.004 ml of protein solution containing 4 mg/ml UMPK mutant in 50 mM Tris-HCl, pH 8.0, and 100 mM NaCl, mixed with 0.004 ml precipitant solution containing 22.5 mM GTP and 21.5% w/v PEG 400 in 100 mM sodium acetate, pH 4.6, equilibration against reservoir solution containing 43% PEG 400, 20°C, X-ray diffraction structure determination and analysis at 2.8-3.0 A resolution, molecular replacement and structure modelling
complexed with GTP, hanging drop vapor diffusion method, using 150 mM sodium acetate pH 4.8, 270 mM ammonium sulfate, 18% (w/v) PEG MME 550. Complexed with UDP, hanging drop vapor diffusion method, using 0.15 M sodium acetate pH 4.8, 0.35 M ammonium sulfate, 28% (w/v)PEG MME 550
using sodium/potassium tartrate (1.2 M) at pH 7.4 and 10 mM GTP
resolved at 2.4 A resolution. Complexed with AMP-PNP, resolved at 3 A resolution. Complexed with AMP-PNP and UMP, resolved at 2.55 A resolution
ternary complex with UMP and the nonhydrolyzable ATP analogue alpha,beta-methylene-ATP (SsUMPK-UMP-AMPPCP), resolution 2.1 A, a complex with UMP (SsUMPK-UMP), resolution 2.2 A, a complex with UTP (SsUMPK-UTP), resolution 2.8 A, hanging drop vapor diffusion, protein solution (2UL) in 10 mM TRIS/Cl pH 7.6 with 4.6 mg/ml SSUMPK and 2 mM UMP and 5 mM MgCl2 mixed with 2 UL mother solution (0.65 M sodium acetate, 100 mM CdCl2, 0.1 M HEPES), pH 7.5
with ATP and UMP, with UMP, with UTP
purified recombinant enzyme, X-ray diffraction structure determination and analysis at 2.5 A resolution
UMPK with N-terminal His-tag, in complex with a phosphate ion, co-crystallized with UMP, and UTP, cross-talk region between two subunits of UpUMPK is identified, vapor diffusion, hanging drop, 0.2 m ammonium fluoride and 20% (w/v) poly(ethylene glycol) 3350, 15°C, enzyme concentration is 1.8 mg/ml, 5 mM GTP, resolution of 2.5 A, space group P 1 21 1, cell dimensions a =79.8, b = 96.6, c = 96.3 A, beta = 105.8
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
-
apo-form UMPK, 2.35 A resolution, crystallisation is significantly improved in a strong magnetic field, buffer-screening procedure, 20 mM N-(2-acetamido)-2-iminodiacetic acid (ADA) pH 6.8, 5 mM beta-mercaptoethanol and 0.02% NaN3, sitting-drop vapour diffusion in 96-well plates, 100 K, monoclinic space group P212121, unit-cell paramerters a = 111.45, b = 120.07, c = 125.79A
-
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
-
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N137A
Tm 10°C lower than wild type, loss of cooperativity with ATP, sensitive to activation by GTP
T135A
Tm 10°C lower than wild type, loss of cooperativity with ATP, increase in Km for UMP, sensitive to activation by GTP
T135A/N137A
Tm 10°C lower than wild type, at pH 7.4 in 50 mM Tris irreversible inactivated within hours
D115A
little detrimental effect, activated by 5'-guanylyl-imidodiphosphate within a concentration range that is roughly similar to that of wild type enzyme
D146N
84% of wild-type activity in the pellet of the sonicated bacterial extract
D93A
site-directed mutagenesis, inhibition by UTP appears significantly altered in the case of the D93A mutant as compared to the wild-type enzyme, the D93A substitution completely suppresses the related subunit-subunit hydrogen bonds between its main chain and Asp93, no inhibition by UTP in presence or absence of GTP. The Tm of the D93A variant is 10°C lower than that of the wild-type enzyme
D93A/D159N
D93 involved in hydrogen bond between the subunits of a dimer, mutation decreases the cooperativity for UTP binding and suppresses the reversal by GTP of UTP inhibition
G232D
resistance to heat denaturation is altered, catalytic avtivity is reduced to 17% of the wild-type
H96A
involved in GTP activation, abolishing GTP activation
L226Q
more insoluble than wild-type, impairs the stability of the enzyme
N111A
little detrimental effect, activated by 5'-guanylyl-imidodiphosphate within a concentration range that is roughly similar to that of wild type enzyme
N140A/D159N
in N140A mutant protein is the cooperativity of inhibition caused by UTP suppressed
N72A
site-directed mutagenesis, no inhibition by UTP in presence or absence of GTP
N72A/D159N
N72 involved in hydrogen bond between the subunits
N72A/D93A
site-directed mutagenesis, the N72A mutation has less severe effects on enzyme activity regulation than the D93A substitution, reduced inhibition by UTP in absence of GTP, no inhibition in presence of GTP. The Tm of the mutant variant is 15°C lower than that of the wild-type enzyme
N72A/D93A/D159N
N72, D93 involved in hydrogen bonds between the subunits
P141L
affects enzyme activity and especially the allosteric regulation
P141Q
more soluble than wild-type
R103A
involved in GTP activation, abolishing GTP activation
R11H
lowered catalytic activity, 45% of the wild-type, resistance to heat denaturation is impaired
R127A
decreasing affinity for GTP
R130A
involved in GTP activation, abolishing GTP activation
R92A
involved in GTP activation, abolishing GTP activation
S124A
decreasing affinity for GTP
T138A
decreases half-denaturation temperature of UMP kinase by around 10°C, results in 4times higher Km for UMP, moderate loss of sensitivity to UTP inhibition, important loss in activation by GTP
T138A/N140A
decreases half-denaturation temperature of UMP kinase by around 25°C, increases the apparant Km for ATP and UMP by a factor of 2.6 and 12, respectively
W119A
involved in GTP activation, abolishing GTP activation
D113A
the mutant shows an increased Km value for UMP compared to the wild type enzyme
F81W
the mutant shows an increased Km value for UMP compared to the wild type enzyme
F81W/S96A
the mutant shows a decreased Km value for UMP compared to the wild type enzyme
P139A
the mutant shows a decreased Km value for UMP compared to the wild type enzyme
P139H
the mutant shows a decreased Km value for UMP compared to the wild type enzyme
P139W
the mutant shows a decreased Km value for UMP compared to the wild type enzyme
R150A
the mutant shows a decreased Km value for UMP compared to the wild type enzyme
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
D113A
-
the mutant shows an increased Km value for UMP compared to the wild type enzyme
-
F81W
-
the mutant shows an increased Km value for UMP compared to the wild type enzyme
-
F81W/S96A
-
the mutant shows a decreased Km value for UMP compared to the wild type enzyme
-
R150A
-
the mutant shows a decreased Km value for UMP compared to the wild type enzyme
-
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
-
A122T
activity decreased to 26% of the wild-type
D201G
activity decreased to 16% of the wild-type, significant loss of sensitivity to activation by GTP
D201N/E241D
activity decreased to 1% of the wild-type
R62H/D77N
-
strain CMM1474, reduced virulence
R62H/D77N
-
strain CMM1474, reduced virulence
-
D159N
site-directed mutagenesis
D159N
appears at neutral pH almost exclusively as a hexamer
D159N
exhibits higher solubility than the wild-type protein at neutral pH, 10% of wild-type activity in the pellet of the sonicated bacterial extract
D159N
used as reference enzyme
D168N
97% of wild-type activity in the pellet of the sonicated bacterial extract
D168N
as stable as wild-type
D174N
as stable as wild-type, impairs the function of the enzyme
D174N
loss of two-thirds of its activity after 3 months storage at 4°C in 50 mM Tris-HCl (pH 7.4), 98% of wild-type activity in the pellet of the sonicated bacterial extract
D174N
the enzyme is not recognized by a monoclonal antibody
D201N
exhibits 10% of the wild-type activity, has altered stability and regulatory properties
D201N
exhibits higher solubility than the wild-type protein at neutral pH, 42% of wild-type activity in the pellet of the sonicated bacterial extract
D201N
impairs the function of the enzyme
D77N
84% of wild-type activity in the pellet of the sonicated bacterial extract, insensitive to activation by GTP
D77N
affects enzyme activity and especially the allosteric regulation
N140A
decreases half-denaturation temperature of UMP kinase by around 10°C, moderate loss of sensitivity to UTP inhibition, important loss in activation by GTP
N140A
cooperative inhibition by GTP and UTP is altered, lower thermodynamic stability
N140A
site-directed mutagenesis, UTP and GTP are tightly coupled in both wild-type enzyme and N140A variant. The Tm of the mutant variant is 10°C lower than that of the wild-type enzyme
R62H
83% of wild-type activity in the pellet of the sonicated bacterial extract, insensitive to activation by GTP
R62H
as stable as wild-type, affects enzyme activity and especially the allosteric regulation
F133A
site-directed mutagenesis, activity is only 20% of the wild-type, still no activation by GTP, with variable UMP concentration and fixed ATP concentration exhibits negative cooperativity with UMP, Hill coefficient 0.85
F133A
site-directed mutagenesis, the mutant enzyme is not activated by GTP and exhibits negative cooperativity with UMP
F133N
site-directed mutagenesis, activity is only 50% of the wild-type, still no activation by GTP, demonstrating that F133N is involved in subunit interactions but apparently not in GTP activation, with variable UMP concentration and fixed ATP concentration exhibits negative cooperativity with UMP, Hill coefficient 0.65, marked decrease in activity
F133N
site-directed mutagenesis, the mutant enzyme is not activated by GTP and exhibits negative cooperativity with UMP
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The crystallization of apo-form UMP kinase from Xanthomonas campestris is significantly improved in a strong magnetic field
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2007
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Structural and enzymatic investigation of the Sulfolobus solfataricus uridylate kinase shows competitive UTP inhibition and the lack of GTP stimulation
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