2.7.1.185: mevalonate 3-kinase
This is an abbreviated version!
For detailed information about mevalonate 3-kinase, go to the full flat file.
Word Map on EC 2.7.1.185
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2.7.1.185
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acidophilum
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thermoplasma
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isopentenyl
-
isoprenoids
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pyrophosphate
-
decarboxylases
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picrophilus
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archaea
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torridus
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cholesterol
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synthesis
- 2.7.1.185
- acidophilum
-
thermoplasma
-
isopentenyl
-
isoprenoids
- pyrophosphate
- decarboxylases
-
picrophilus
- archaea
- torridus
- cholesterol
- synthesis
Reaction
Synonyms
ATP:(R)-MVA 3-phosphotransferase, M3K, mevalonate 3-kinase, mevalonate-3-kinase, More, PtM3K, PTO1356, Ta1305, TacM3K
ECTree
2.7.1.185 mevalonate 3-kinaseAdvanced search results
results (
results (Engineering
Engineering on EC 2.7.1.185 - mevalonate 3-kinase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D281A
-
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
-
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
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
D281A
-
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
-
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
-
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
-
D281A
-
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
-
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
-
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
-
D281A
-
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
-
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
-
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
-
D281A
-
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
-
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
-
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
-
E140G
site-directed mutagenesis, the mutation results in the conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase, which can synthesize 3,5-bisphosphomevalonate from 5-phosphomevalonate
E140S
site-directed mutagenesis, the mutation results in the conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase, which can synthesize 3,5-bisphosphomevalonate from 5-phosphomevalonate
L18A
kcat/KM for (R)-mevalonate is 4.4% compared to the wild-type value
R185K
kcat/KM for (R)-mevalonate is 0.5% compared to the wild-type value
S105A
kcat/KM for (R)-mevalonate is 10.3% compared to the wild-type value
T275A
kcat/KM for (R)-mevalonate is 25.6% compared to the wild-type value
E140G
-
site-directed mutagenesis, the mutation results in the conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase, which can synthesize 3,5-bisphosphomevalonate from 5-phosphomevalonate
-
E140S
-
site-directed mutagenesis, the mutation results in the conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase, which can synthesize 3,5-bisphosphomevalonate from 5-phosphomevalonate
-
E140G
-
site-directed mutagenesis, the mutation results in the conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase, which can synthesize 3,5-bisphosphomevalonate from 5-phosphomevalonate
-
E140S
-
site-directed mutagenesis, the mutation results in the conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase, which can synthesize 3,5-bisphosphomevalonate from 5-phosphomevalonate
-
E140G
-
site-directed mutagenesis, the mutation results in the conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase, which can synthesize 3,5-bisphosphomevalonate from 5-phosphomevalonate
-
E140S
-
site-directed mutagenesis, the mutation results in the conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase, which can synthesize 3,5-bisphosphomevalonate from 5-phosphomevalonate
-
E140G
-
site-directed mutagenesis, the mutation results in the conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase, which can synthesize 3,5-bisphosphomevalonate from 5-phosphomevalonate
-
E140S
-
site-directed mutagenesis, the mutation results in the conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase, which can synthesize 3,5-bisphosphomevalonate from 5-phosphomevalonate
-
additional information
additional information
substrate-interacting glutamate residue E140 of Thermoplasma acidophilum mevalonate 3-kinase is replaced by smaller amino acids, including its counterparts in diphosphomevalonate decarboxylase and phosphomevalonate decarboxylase, with the aim of altering substrate specificity. These single amino acid mutations results in the conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase, which can synthesize 3,5-bisphosphomevalonate from 5-phosphomevalonate. The mutants catalyzing the hitherto undiscovered reaction enables the construction of an artificial mevalonate pathway in Escherichia coli cells, as is demonstrated by the accumulation of lycopene, a red carotenoid pigment. Neither wild-type TacM3K nor any mutants show reactivity toward MVA 5-diphosphate. Alternative MVA pathway II overview. Constructed plasmids and strains, overview
additional information
-
substrate-interacting glutamate residue E140 of Thermoplasma acidophilum mevalonate 3-kinase is replaced by smaller amino acids, including its counterparts in diphosphomevalonate decarboxylase and phosphomevalonate decarboxylase, with the aim of altering substrate specificity. These single amino acid mutations results in the conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase, which can synthesize 3,5-bisphosphomevalonate from 5-phosphomevalonate. The mutants catalyzing the hitherto undiscovered reaction enables the construction of an artificial mevalonate pathway in Escherichia coli cells, as is demonstrated by the accumulation of lycopene, a red carotenoid pigment. Neither wild-type TacM3K nor any mutants show reactivity toward MVA 5-diphosphate. Alternative MVA pathway II overview. Constructed plasmids and strains, overview
additional information
-
substrate-interacting glutamate residue E140 of Thermoplasma acidophilum mevalonate 3-kinase is replaced by smaller amino acids, including its counterparts in diphosphomevalonate decarboxylase and phosphomevalonate decarboxylase, with the aim of altering substrate specificity. These single amino acid mutations results in the conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase, which can synthesize 3,5-bisphosphomevalonate from 5-phosphomevalonate. The mutants catalyzing the hitherto undiscovered reaction enables the construction of an artificial mevalonate pathway in Escherichia coli cells, as is demonstrated by the accumulation of lycopene, a red carotenoid pigment. Neither wild-type TacM3K nor any mutants show reactivity toward MVA 5-diphosphate. Alternative MVA pathway II overview. Constructed plasmids and strains, overview
-
additional information
-
substrate-interacting glutamate residue E140 of Thermoplasma acidophilum mevalonate 3-kinase is replaced by smaller amino acids, including its counterparts in diphosphomevalonate decarboxylase and phosphomevalonate decarboxylase, with the aim of altering substrate specificity. These single amino acid mutations results in the conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase, which can synthesize 3,5-bisphosphomevalonate from 5-phosphomevalonate. The mutants catalyzing the hitherto undiscovered reaction enables the construction of an artificial mevalonate pathway in Escherichia coli cells, as is demonstrated by the accumulation of lycopene, a red carotenoid pigment. Neither wild-type TacM3K nor any mutants show reactivity toward MVA 5-diphosphate. Alternative MVA pathway II overview. Constructed plasmids and strains, overview
-
additional information
-
substrate-interacting glutamate residue E140 of Thermoplasma acidophilum mevalonate 3-kinase is replaced by smaller amino acids, including its counterparts in diphosphomevalonate decarboxylase and phosphomevalonate decarboxylase, with the aim of altering substrate specificity. These single amino acid mutations results in the conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase, which can synthesize 3,5-bisphosphomevalonate from 5-phosphomevalonate. The mutants catalyzing the hitherto undiscovered reaction enables the construction of an artificial mevalonate pathway in Escherichia coli cells, as is demonstrated by the accumulation of lycopene, a red carotenoid pigment. Neither wild-type TacM3K nor any mutants show reactivity toward MVA 5-diphosphate. Alternative MVA pathway II overview. Constructed plasmids and strains, overview
-
additional information
-
substrate-interacting glutamate residue E140 of Thermoplasma acidophilum mevalonate 3-kinase is replaced by smaller amino acids, including its counterparts in diphosphomevalonate decarboxylase and phosphomevalonate decarboxylase, with the aim of altering substrate specificity. These single amino acid mutations results in the conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase, which can synthesize 3,5-bisphosphomevalonate from 5-phosphomevalonate. The mutants catalyzing the hitherto undiscovered reaction enables the construction of an artificial mevalonate pathway in Escherichia coli cells, as is demonstrated by the accumulation of lycopene, a red carotenoid pigment. Neither wild-type TacM3K nor any mutants show reactivity toward MVA 5-diphosphate. Alternative MVA pathway II overview. Constructed plasmids and strains, overview
-
