2.7.4.22: UMP kinase
This is an abbreviated version!
For detailed information about UMP kinase, go to the full flat file.
Reaction
Synonyms
ATP:UMP phosphotransferase, HP0777 protein, More, pyrH, Rv2883c, SsUMPK, UMP kinase, UMP-kinase, UMPK, UMPKs, uridine monophosphate kinase, uridylate kinase, XC1936
ECTree
2.7.4.22 UMP kinaseAdvanced search results
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results (Engineering
Engineering on EC 2.7.4.22 - UMP kinase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
D159N
D168N
D174N
D201N
D77N
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
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
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/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
R11H
lowered catalytic activity, 45% of the wild-type, resistance to heat denaturation is impaired
R62H
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
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
F133A
F133N
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
D168N
97% of wild-type activity in the pellet of the sonicated bacterial extract
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
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
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
