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N17A
mutant exhibits a 15fold inflation in Km for 5-diphosphomevalonate
R161Q
mutant exhibits an about 1000fold diminution in specific activity, while binding the fluorescent substrate analog, TNP-ATP, comparably to wild type enzyme
S162A
mutant shows reduced activity with 2fold decrease in Vm and 4 to 7fold increases in substrate Km values
C210S
decrease in melting temperature by 12 degrees
D281N
site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity and phosphate elimination/decarboxylation
D281T
site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity compared to wild-type, but is inactive in the process of phosphate elimination/decarboxylation
D281V
site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity compared to wild-type, but is inactive in the process of phosphate elimination/decarboxylation
D281N
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site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity and phosphate elimination/decarboxylation
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D281T
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site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity compared to wild-type, but is inactive in the process of phosphate elimination/decarboxylation
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D281V
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site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity compared to wild-type, but is inactive in the process of phosphate elimination/decarboxylation
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C210S
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decrease in melting temperature by 12 degrees
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D281N
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site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity and phosphate elimination/decarboxylation
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D281T
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site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity compared to wild-type, but is inactive in the process of phosphate elimination/decarboxylation
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D281V
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site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity compared to wild-type, but is inactive in the process of phosphate elimination/decarboxylation
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D281N
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site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity and phosphate elimination/decarboxylation
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D281T
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site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity compared to wild-type, but is inactive in the process of phosphate elimination/decarboxylation
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D281V
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site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity compared to wild-type, but is inactive in the process of phosphate elimination/decarboxylation
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D281N
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site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity and phosphate elimination/decarboxylation
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D281T
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site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity compared to wild-type, but is inactive in the process of phosphate elimination/decarboxylation
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D281V
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site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity compared to wild-type, but is inactive in the process of phosphate elimination/decarboxylation
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D302A
1000fold decrease in kcat value, still retains ability to stoichiometrically bind nucleotide triphosphates at the active site
D302N
100000fold decrease in kcat value, still retains ability to stoichiometrically bind nucleotide triphosphates at the active site
K18M
30fold decrease in kcat value, still retains ability to stoichiometrically bind nucleotide triphosphates at the active site
R74H
mutant increases specific activity on non-native substrate (3-hydroxy-3-methylbutyrate) by 4.8fold
S120A
8fold diminution in kcat-value
S121A
42000fold diminution in kcat-value
S153A
18fold inflation in Kd-value for Mg-ATP, 35fold inflation in Km-value for Mg-ATP
S155A
26fold inflation in Km-value for Mg-ATP, 16fold inflation in Km-value for diphosphomevalonate
S36A
limited solubility, impaired binding of fluorescent ATP analogue trinitrophenyl-ATP
R193T
modest effects on kinetics
W153F
modest effects on kinetics
W19F
130fold increase in Km for (R)-5-diphosphomevalonate, 10fold increase in Km for ATP
L79P
-
mutation drastically impairs the oligomerization of the protein
L79P
molecular dynamics simutation of the mutated enzyme, it is suggested that the temperature sensitive mutant phenotype of Saccharomyces cerevisiae is a result of a significant conformational change associates with the Leu 79 to Pro mutation
D283A
catalytically deficient enzyme with 100000fold decreased kcat value
D283A
10000fold decrease in kcat value
S192A
the mutation decreases kcat by about 1000fold
S192A
catalytically deficient enzyme with 1000fold decreased kcat value
S192A
1000fold decrease in kcat value
additional information
the DMD activity, which yields IPP from MVA-5-PP in the presence of ATP, is observed only with the wild type and with the D281N mutant
additional information
-
the DMD activity, which yields IPP from MVA-5-PP in the presence of ATP, is observed only with the wild type and with the D281N mutant
additional information
-
the DMD activity, which yields IPP from MVA-5-PP in the presence of ATP, is observed only with the wild type and with the D281N mutant
-
additional information
-
the DMD activity, which yields IPP from MVA-5-PP in the presence of ATP, is observed only with the wild type and with the D281N mutant
-
additional information
-
the DMD activity, which yields IPP from MVA-5-PP in the presence of ATP, is observed only with the wild type and with the D281N mutant
-
additional information
-
the DMD activity, which yields IPP from MVA-5-PP in the presence of ATP, is observed only with the wild type and with the D281N mutant
-