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
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isoprenoids
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pyrophosphate
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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
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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
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General Information
General Information on EC 2.7.1.185 - mevalonate 3-kinase
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evolution
malfunction
metabolism
physiological function
additional information
mevalonate 3-kinase is an enzyme involved in the modified mevalonate pathway specific to limited species of thermophilic archaea
evolution
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mevalonate 3-kinase is an enzyme involved in the modified mevalonate pathway specific to limited species of thermophilic archaea
-
evolution
-
mevalonate 3-kinase is an enzyme involved in the modified mevalonate pathway specific to limited species of thermophilic archaea
-
evolution
-
mevalonate 3-kinase is an enzyme involved in the modified mevalonate pathway specific to limited species of thermophilic archaea
-
evolution
-
mevalonate 3-kinase is an enzyme involved in the modified mevalonate pathway specific to limited species of thermophilic archaea
-
-
site-directed mutagenesis on Asp281 creates mutants that only show diphosphomevalonate 3-kinase activity, demonstrating that the residue is required in the process of phosphate elimination/decarboxylation, rather than in the preceding phosphorylation step
malfunction
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site-directed mutagenesis on Asp281 creates mutants that only show diphosphomevalonate 3-kinase activity, demonstrating that the residue is required in the process of phosphate elimination/decarboxylation, rather than in the preceding phosphorylation step
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malfunction
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site-directed mutagenesis on Asp281 creates mutants that only show diphosphomevalonate 3-kinase activity, demonstrating that the residue is required in the process of phosphate elimination/decarboxylation, rather than in the preceding phosphorylation step
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malfunction
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site-directed mutagenesis on Asp281 creates mutants that only show diphosphomevalonate 3-kinase activity, demonstrating that the residue is required in the process of phosphate elimination/decarboxylation, rather than in the preceding phosphorylation step
-
malfunction
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site-directed mutagenesis on Asp281 creates mutants that only show diphosphomevalonate 3-kinase activity, demonstrating that the residue is required in the process of phosphate elimination/decarboxylation, rather than in the preceding phosphorylation step
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key enzyme of the Thermoplasma acidophilum-type mevalonate pathway
metabolism
mevalonate 3-kinase plays a key role in a recently discovered modified mevalonate pathway specific to thermophilic archaea of the order Thermoplasmatales, pathway overview. In the pathway called modified MVA pathway II, mevalonate (MVA) is phosphorylated at the 3-hydroxyl group to yield 3-phosphomevalonate (MVA-3-P) by the action of mevalonate 3-kinase (M3K) rather than at the 5-hydroxyl group as in the reaction of MVK (EC 2.7.4.2). M3K is also homologous to diphosphomevalonate decarboxylase (DMD, EC 4.1.1.33). After the formation of MVA-3-P, another kinase, MVA-3-P 5-kinase (M3P5K), catalyzes its 5-phosphorylation, and a subsequent decarboxylation is catalyzed by another DMD homologue, 3,5-bisphosphomevalonate decarboxylase (BMD), to give isopentenyl phosphate (IP). IP is then phosphorylated by isopentenyl phosphate kinase (IPK) to yield isopentenyl diphosphate (IPP). The M3K enzyme is homologous to diphosphomevalonate decarboxylase, which is involved in the widely distributed classical mevalonate pathway, and to phosphomevalonate decarboxylase, which is possessed by halophilic archaea and some Chloroflexi bacteria. Neither wild-type TacM3K nor any mutants show reactivity toward MVA 5-diphosphate
metabolism
-
mevalonate 3-kinase plays a key role in a recently discovered modified mevalonate pathway specific to thermophilic archaea of the order Thermoplasmatales, pathway overview. In the pathway called modified MVA pathway II, mevalonate (MVA) is phosphorylated at the 3-hydroxyl group to yield 3-phosphomevalonate (MVA-3-P) by the action of mevalonate 3-kinase (M3K) rather than at the 5-hydroxyl group as in the reaction of MVK (EC 2.7.4.2). M3K is also homologous to diphosphomevalonate decarboxylase (DMD, EC 4.1.1.33). After the formation of MVA-3-P, another kinase, MVA-3-P 5-kinase (M3P5K), catalyzes its 5-phosphorylation, and a subsequent decarboxylation is catalyzed by another DMD homologue, 3,5-bisphosphomevalonate decarboxylase (BMD), to give isopentenyl phosphate (IP). IP is then phosphorylated by isopentenyl phosphate kinase (IPK) to yield isopentenyl diphosphate (IPP). The M3K enzyme is homologous to diphosphomevalonate decarboxylase, which is involved in the widely distributed classical mevalonate pathway, and to phosphomevalonate decarboxylase, which is possessed by halophilic archaea and some Chloroflexi bacteria. Neither wild-type TacM3K nor any mutants show reactivity toward MVA 5-diphosphate
-
metabolism
-
mevalonate 3-kinase plays a key role in a recently discovered modified mevalonate pathway specific to thermophilic archaea of the order Thermoplasmatales, pathway overview. In the pathway called modified MVA pathway II, mevalonate (MVA) is phosphorylated at the 3-hydroxyl group to yield 3-phosphomevalonate (MVA-3-P) by the action of mevalonate 3-kinase (M3K) rather than at the 5-hydroxyl group as in the reaction of MVK (EC 2.7.4.2). M3K is also homologous to diphosphomevalonate decarboxylase (DMD, EC 4.1.1.33). After the formation of MVA-3-P, another kinase, MVA-3-P 5-kinase (M3P5K), catalyzes its 5-phosphorylation, and a subsequent decarboxylation is catalyzed by another DMD homologue, 3,5-bisphosphomevalonate decarboxylase (BMD), to give isopentenyl phosphate (IP). IP is then phosphorylated by isopentenyl phosphate kinase (IPK) to yield isopentenyl diphosphate (IPP). The M3K enzyme is homologous to diphosphomevalonate decarboxylase, which is involved in the widely distributed classical mevalonate pathway, and to phosphomevalonate decarboxylase, which is possessed by halophilic archaea and some Chloroflexi bacteria. Neither wild-type TacM3K nor any mutants show reactivity toward MVA 5-diphosphate
-
metabolism
-
key enzyme of the Thermoplasma acidophilum-type mevalonate pathway
-
metabolism
-
mevalonate 3-kinase plays a key role in a recently discovered modified mevalonate pathway specific to thermophilic archaea of the order Thermoplasmatales, pathway overview. In the pathway called modified MVA pathway II, mevalonate (MVA) is phosphorylated at the 3-hydroxyl group to yield 3-phosphomevalonate (MVA-3-P) by the action of mevalonate 3-kinase (M3K) rather than at the 5-hydroxyl group as in the reaction of MVK (EC 2.7.4.2). M3K is also homologous to diphosphomevalonate decarboxylase (DMD, EC 4.1.1.33). After the formation of MVA-3-P, another kinase, MVA-3-P 5-kinase (M3P5K), catalyzes its 5-phosphorylation, and a subsequent decarboxylation is catalyzed by another DMD homologue, 3,5-bisphosphomevalonate decarboxylase (BMD), to give isopentenyl phosphate (IP). IP is then phosphorylated by isopentenyl phosphate kinase (IPK) to yield isopentenyl diphosphate (IPP). The M3K enzyme is homologous to diphosphomevalonate decarboxylase, which is involved in the widely distributed classical mevalonate pathway, and to phosphomevalonate decarboxylase, which is possessed by halophilic archaea and some Chloroflexi bacteria. Neither wild-type TacM3K nor any mutants show reactivity toward MVA 5-diphosphate
-
metabolism
-
mevalonate 3-kinase plays a key role in a recently discovered modified mevalonate pathway specific to thermophilic archaea of the order Thermoplasmatales, pathway overview. In the pathway called modified MVA pathway II, mevalonate (MVA) is phosphorylated at the 3-hydroxyl group to yield 3-phosphomevalonate (MVA-3-P) by the action of mevalonate 3-kinase (M3K) rather than at the 5-hydroxyl group as in the reaction of MVK (EC 2.7.4.2). M3K is also homologous to diphosphomevalonate decarboxylase (DMD, EC 4.1.1.33). After the formation of MVA-3-P, another kinase, MVA-3-P 5-kinase (M3P5K), catalyzes its 5-phosphorylation, and a subsequent decarboxylation is catalyzed by another DMD homologue, 3,5-bisphosphomevalonate decarboxylase (BMD), to give isopentenyl phosphate (IP). IP is then phosphorylated by isopentenyl phosphate kinase (IPK) to yield isopentenyl diphosphate (IPP). The M3K enzyme is homologous to diphosphomevalonate decarboxylase, which is involved in the widely distributed classical mevalonate pathway, and to phosphomevalonate decarboxylase, which is possessed by halophilic archaea and some Chloroflexi bacteria. Neither wild-type TacM3K nor any mutants show reactivity toward MVA 5-diphosphate
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mevalonate-3-kinase and mevalonate-3-phosphate-5-kinase act sequentially in a putative alternate mevalonate pathway in Thermoplasma acidophilum
physiological function
the enzyme is part of a putative alternate mevalonate pathway in Thermoplasma acidophilum
physiological function
mevalonate 3-kinase catalyzes the ATP-dependent 3-phosphorylation of mevalonate but does not catalyze the subsequent decarboxylation as related decarboxylases do
physiological function
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the biosynthesis of isopentenyl diphosphate, a fundamental precursor for isoprenoids, via the mevalonate pathway is completed by diphosphomevalonate decarboxylase. This enzyme catalyzes the formation of isopentenyl diphosphate through the ATP-dependent phosphorylation of the 3-hydroxyl group of (R)-5-diphosphomevalonate followed by decarboxylation coupled with the elimination of the 3-phosphate group. Involvement of a long predicted intermediate, (R)-3-phospho-5-diphosphomevalonate, in the reaction of the enzyme
physiological function
the enzyme is specialized as a mevalonate 3-kinase catalyzing the first step of the mevalonate decarboxylation (MVD) reaction
physiological function
-
the biosynthesis of isopentenyl diphosphate, a fundamental precursor for isoprenoids, via the mevalonate pathway is completed by diphosphomevalonate decarboxylase. This enzyme catalyzes the formation of isopentenyl diphosphate through the ATP-dependent phosphorylation of the 3-hydroxyl group of (R)-5-diphosphomevalonate followed by decarboxylation coupled with the elimination of the 3-phosphate group. Involvement of a long predicted intermediate, (R)-3-phospho-5-diphosphomevalonate, in the reaction of the enzyme
-
physiological function
-
the biosynthesis of isopentenyl diphosphate, a fundamental precursor for isoprenoids, via the mevalonate pathway is completed by diphosphomevalonate decarboxylase. This enzyme catalyzes the formation of isopentenyl diphosphate through the ATP-dependent phosphorylation of the 3-hydroxyl group of (R)-5-diphosphomevalonate followed by decarboxylation coupled with the elimination of the 3-phosphate group. Involvement of a long predicted intermediate, (R)-3-phospho-5-diphosphomevalonate, in the reaction of the enzyme
-
physiological function
-
mevalonate 3-kinase catalyzes the ATP-dependent 3-phosphorylation of mevalonate but does not catalyze the subsequent decarboxylation as related decarboxylases do
-
physiological function
-
the enzyme is specialized as a mevalonate 3-kinase catalyzing the first step of the mevalonate decarboxylation (MVD) reaction
-
physiological function
-
mevalonate 3-kinase catalyzes the ATP-dependent 3-phosphorylation of mevalonate but does not catalyze the subsequent decarboxylation as related decarboxylases do
-
physiological function
-
the enzyme is specialized as a mevalonate 3-kinase catalyzing the first step of the mevalonate decarboxylation (MVD) reaction
-
physiological function
-
the enzyme is specialized as a mevalonate 3-kinase catalyzing the first step of the mevalonate decarboxylation (MVD) reaction
-
physiological function
-
the biosynthesis of isopentenyl diphosphate, a fundamental precursor for isoprenoids, via the mevalonate pathway is completed by diphosphomevalonate decarboxylase. This enzyme catalyzes the formation of isopentenyl diphosphate through the ATP-dependent phosphorylation of the 3-hydroxyl group of (R)-5-diphosphomevalonate followed by decarboxylation coupled with the elimination of the 3-phosphate group. Involvement of a long predicted intermediate, (R)-3-phospho-5-diphosphomevalonate, in the reaction of the enzyme
-
physiological function
-
the biosynthesis of isopentenyl diphosphate, a fundamental precursor for isoprenoids, via the mevalonate pathway is completed by diphosphomevalonate decarboxylase. This enzyme catalyzes the formation of isopentenyl diphosphate through the ATP-dependent phosphorylation of the 3-hydroxyl group of (R)-5-diphosphomevalonate followed by decarboxylation coupled with the elimination of the 3-phosphate group. Involvement of a long predicted intermediate, (R)-3-phospho-5-diphosphomevalonate, in the reaction of the enzyme
-
physiological function
-
mevalonate 3-kinase catalyzes the ATP-dependent 3-phosphorylation of mevalonate but does not catalyze the subsequent decarboxylation as related decarboxylases do
-
physiological function
-
mevalonate 3-kinase catalyzes the ATP-dependent 3-phosphorylation of mevalonate but does not catalyze the subsequent decarboxylation as related decarboxylases do
-
physiological function
-
the enzyme is specialized as a mevalonate 3-kinase catalyzing the first step of the mevalonate decarboxylation (MVD) reaction
-
comparison between the substrate-complex crystal structure of TacM3K (PDB ID 4RKS) and that of Sulfolobus solfataricus DMD (SsoDMD, PDB ID 5GMD) revealing interesting differences in the structures of the active sites. The steric hindrance introduced by Glu140 seems responsible for excluding larger substrates, such as MVA 5-phosphate and MVA 5-diphosphate, from the active site of TacM3K
additional information
-
comparison between the substrate-complex crystal structure of TacM3K (PDB ID 4RKS) and that of Sulfolobus solfataricus DMD (SsoDMD, PDB ID 5GMD) revealing interesting differences in the structures of the active sites. The steric hindrance introduced by Glu140 seems responsible for excluding larger substrates, such as MVA 5-phosphate and MVA 5-diphosphate, from the active site of TacM3K
additional information
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the conserved aspartate residue, Asp281, shows inability for proton abstraction. Substrate-complex structures of DMD (EC 4.1.1.33) and M3K, overview
additional information
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the conserved aspartate residue, Asp281, shows inability for proton abstraction. Substrate-complex structures of DMD (EC 4.1.1.33) and M3K, overview
-
additional information
-
the conserved aspartate residue, Asp281, shows inability for proton abstraction. Substrate-complex structures of DMD (EC 4.1.1.33) and M3K, overview
-
additional information
-
comparison between the substrate-complex crystal structure of TacM3K (PDB ID 4RKS) and that of Sulfolobus solfataricus DMD (SsoDMD, PDB ID 5GMD) revealing interesting differences in the structures of the active sites. The steric hindrance introduced by Glu140 seems responsible for excluding larger substrates, such as MVA 5-phosphate and MVA 5-diphosphate, from the active site of TacM3K
-
additional information
-
comparison between the substrate-complex crystal structure of TacM3K (PDB ID 4RKS) and that of Sulfolobus solfataricus DMD (SsoDMD, PDB ID 5GMD) revealing interesting differences in the structures of the active sites. The steric hindrance introduced by Glu140 seems responsible for excluding larger substrates, such as MVA 5-phosphate and MVA 5-diphosphate, from the active site of TacM3K
-
additional information
-
the conserved aspartate residue, Asp281, shows inability for proton abstraction. Substrate-complex structures of DMD (EC 4.1.1.33) and M3K, overview
-
additional information
-
the conserved aspartate residue, Asp281, shows inability for proton abstraction. Substrate-complex structures of DMD (EC 4.1.1.33) and M3K, overview
-
additional information
-
comparison between the substrate-complex crystal structure of TacM3K (PDB ID 4RKS) and that of Sulfolobus solfataricus DMD (SsoDMD, PDB ID 5GMD) revealing interesting differences in the structures of the active sites. The steric hindrance introduced by Glu140 seems responsible for excluding larger substrates, such as MVA 5-phosphate and MVA 5-diphosphate, from the active site of TacM3K
-
additional information
-
comparison between the substrate-complex crystal structure of TacM3K (PDB ID 4RKS) and that of Sulfolobus solfataricus DMD (SsoDMD, PDB ID 5GMD) revealing interesting differences in the structures of the active sites. The steric hindrance introduced by Glu140 seems responsible for excluding larger substrates, such as MVA 5-phosphate and MVA 5-diphosphate, from the active site of TacM3K
-