Any feedback?
Information on EC 2.7.1.185 - mevalonate 3-kinase
for references in articles please use BRENDA:EC2.7.1.185Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.7.1.185 mevalonate 3-kinaseIUBMB Comments
Mevalonate 3-kinase and mevalonate-3-phosphate-5-kinase (EC 2.7.1.186) act sequentially in an alternate mevalonate pathway in the archaeon Thermoplasma acidophilum. Mevalonate 3-kinase is different from mevalonate kinase, EC 2.7.1.36, which transfers phosphate to position 5 of (R)-mevalonate and is part of the classical mevalonate pathway in eukaryotes and archaea.
Specify your search results
Word Map
- 2.7.1.185
- acidophilum
-
thermoplasma
-
isopentenyl
-
isoprenoids
- pyrophosphate
- decarboxylases
-
picrophilus
- archaea
- torridus
- cholesterol
- synthesis
The enzyme appears in viruses and cellular organisms
Synonyms
mevalonate 3-kinase, mevalonate-3-kinase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
M3K
mevalonate 3-kinase
mevalonate-3-kinase
PtM3K
PTO1356
Ta1305
TacM3K
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + (R)-mevalonate = ADP + (R)-3-phosphomevalonate
-
-
-
-
ATP + (R)-mevalonate = ADP + (R)-3-phosphomevalonate
catalytic mechanism of this rare type of decarboxylase, the enzyme is bifunctional showing the reactions of diphosphomevalonate decarboxylase (EC 4.1.1.33) and mevalonate 3-kinase (EC 2.7.1.185), overview
-
ATP + (R)-mevalonate = ADP + (R)-3-phosphomevalonate
catalytic mechanism of this rare type of decarboxylase, the enzyme is bifunctional showing the reactions of diphosphomevalonate decarboxylase (EC 4.1.1.33) and mevalonate 3-kinase (EC 2.7.1.185), overview
-
-
ATP + (R)-mevalonate = ADP + (R)-3-phosphomevalonate
catalytic mechanism of this rare type of decarboxylase, the enzyme is bifunctional showing the reactions of diphosphomevalonate decarboxylase (EC 4.1.1.33) and mevalonate 3-kinase (EC 2.7.1.185), overview
-
-
ATP + (R)-mevalonate = ADP + (R)-3-phosphomevalonate
catalytic mechanism of this rare type of decarboxylase, the enzyme is bifunctional showing the reactions of diphosphomevalonate decarboxylase (EC 4.1.1.33) and mevalonate 3-kinase (EC 2.7.1.185), overview
-
-
ATP + (R)-mevalonate = ADP + (R)-3-phosphomevalonate
catalytic mechanism of this rare type of decarboxylase, the enzyme is bifunctional showing the reactions of diphosphomevalonate decarboxylase (EC 4.1.1.33) and mevalonate 3-kinase (EC 2.7.1.185), overview
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
ATP:(R)-mevalonate 3-phosphotransferase
Mevalonate 3-kinase and mevalonate-3-phosphate-5-kinase (EC 2.7.1.186) act sequentially in an alternate mevalonate pathway in the archaeon Thermoplasma acidophilum. Mevalonate 3-kinase is different from mevalonate kinase, EC 2.7.1.36, which transfers phosphate to position 5 of (R)-mevalonate and is part of the classical mevalonate pathway in eukaryotes and archaea.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + (R)-2,3-dihydroxyisovalerate
ADP + (R)-2-hydroxy-3-phosphoisovalerate
the Picrophilus torridus mevalonate-3-kinase (M3K) exhibits adenosine triphosphate (ATP) hydrolysis activity when mixed with (R)-2,3-dihydroxyisovalerate (DHIV), indicating phosphorylation activity towards DHIV
-
-
?
ATP + (R)-2,3-dihydroxyisovalerate
ADP + (R)-2-hydroxy-3-phosphoisovalerate
the Picrophilus torridus mevalonate-3-kinase (M3K) exhibits adenosine triphosphate (ATP) hydrolysis activity when mixed with (R)-2,3-dihydroxyisovalerate (DHIV), indicating phosphorylation activity towards DHIV
-
-
?
ATP + (R)-2,3-dihydroxyisovalerate
ADP + (R)-2-hydroxy-3-phosphoisovalerate
the Picrophilus torridus mevalonate-3-kinase (M3K) exhibits adenosine triphosphate (ATP) hydrolysis activity when mixed with (R)-2,3-dihydroxyisovalerate (DHIV), indicating phosphorylation activity towards DHIV
-
-
?
ATP + (R)-2,3-dihydroxyisovalerate
ADP + (R)-2-hydroxy-3-phosphoisovalerate
the Picrophilus torridus mevalonate-3-kinase (M3K) exhibits adenosine triphosphate (ATP) hydrolysis activity when mixed with (R)-2,3-dihydroxyisovalerate (DHIV), indicating phosphorylation activity towards DHIV
-
-
?
ATP + (R)-2,3-dihydroxyisovalerate
ADP + (R)-2-hydroxy-3-phosphoisovalerate
the Picrophilus torridus mevalonate-3-kinase (M3K) exhibits adenosine triphosphate (ATP) hydrolysis activity when mixed with (R)-2,3-dihydroxyisovalerate (DHIV), indicating phosphorylation activity towards DHIV
-
-
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
key enzyme of the Thermoplasma acidophilum-type mevalonate pathway
-
-
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
key enzyme of the Thermoplasma acidophilum-type mevalonate pathway
-
-
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
mevalonate-3-kinase and mevalonate-3-phosphate-5-kinase act sequentially in a putative alternate mevalonate pathway in Thermoplasma acidophilum
-
-
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
the enzyme is part of a putative alternate mevalonate pathway in Thermoplasma acidophilum
-
-
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
-
-
?
ATP + 3-hydroxyisovalerate
ADP + phosphate + isobutene + CO2
the potential of the enzyme in isobutene formation is due to the conversion of 3-hydroxyisovalerate to an unstable 3-phosphate intermediate that undergoes consequent spontaneous decarboxylation to form isobutene
-
-
?
ATP + 3-hydroxyisovalerate
ADP + phosphate + isobutene + CO2
the potential of the enzyme in isobutene formation is due to the conversion of 3-hydroxyisovalerate to an unstable 3-phosphate intermediate that undergoes consequent spontaneous decarboxylation to form isobutene
-
-
?
additional information
?
-
a first reaction strategy is the activaion of (R)-2,3-dihydroxyisovalerate (DHIV) to 3-phospho-DHIV using M3K followed by dehydration by PpManR, StPutD or other sugar acid dehydratases. A second strategy is to use M3K and/or mevalonate decarboxylase (MVD) to convert DHIV to isobutyraldehyde, which can be an alternative pathway for isobutanol biosynthesis
-
-
-
additional information
?
-
-
a first reaction strategy is the activaion of (R)-2,3-dihydroxyisovalerate (DHIV) to 3-phospho-DHIV using M3K followed by dehydration by PpManR, StPutD or other sugar acid dehydratases. A second strategy is to use M3K and/or mevalonate decarboxylase (MVD) to convert DHIV to isobutyraldehyde, which can be an alternative pathway for isobutanol biosynthesis
-
-
-
additional information
?
-
a first reaction strategy is the activaion of (R)-2,3-dihydroxyisovalerate (DHIV) to 3-phospho-DHIV using M3K followed by dehydration by PpManR, StPutD or other sugar acid dehydratases. A second strategy is to use M3K and/or mevalonate decarboxylase (MVD) to convert DHIV to isobutyraldehyde, which can be an alternative pathway for isobutanol biosynthesis
-
-
-
additional information
?
-
a first reaction strategy is the activaion of (R)-2,3-dihydroxyisovalerate (DHIV) to 3-phospho-DHIV using M3K followed by dehydration by PpManR, StPutD or other sugar acid dehydratases. A second strategy is to use M3K and/or mevalonate decarboxylase (MVD) to convert DHIV to isobutyraldehyde, which can be an alternative pathway for isobutanol biosynthesis
-
-
-
additional information
?
-
a first reaction strategy is the activaion of (R)-2,3-dihydroxyisovalerate (DHIV) to 3-phospho-DHIV using M3K followed by dehydration by PpManR, StPutD or other sugar acid dehydratases. A second strategy is to use M3K and/or mevalonate decarboxylase (MVD) to convert DHIV to isobutyraldehyde, which can be an alternative pathway for isobutanol biosynthesis
-
-
-
additional information
?
-
a first reaction strategy is the activaion of (R)-2,3-dihydroxyisovalerate (DHIV) to 3-phospho-DHIV using M3K followed by dehydration by PpManR, StPutD or other sugar acid dehydratases. A second strategy is to use M3K and/or mevalonate decarboxylase (MVD) to convert DHIV to isobutyraldehyde, which can be an alternative pathway for isobutanol biosynthesis
-
-
-
additional information
?
-
-
NMR analysis of the product
-
-
-
additional information
?
-
-
NMR analysis of the product
-
-
-
additional information
?
-
-
NMR analysis of the product
-
-
-
additional information
?
-
substrate specificity, overview
-
-
-
additional information
?
-
substrate specificity, overview
-
-
-
additional information
?
-
substrate specificity, overview
-
-
-
additional information
?
-
substrate specificity, overview
-
-
-
additional information
?
-
substrate specificity, overview
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
key enzyme of the Thermoplasma acidophilum-type mevalonate pathway
-
-
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
key enzyme of the Thermoplasma acidophilum-type mevalonate pathway
-
-
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
mevalonate-3-kinase and mevalonate-3-phosphate-5-kinase act sequentially in a putative alternate mevalonate pathway in Thermoplasma acidophilum
-
-
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
the enzyme is part of a putative alternate mevalonate pathway in Thermoplasma acidophilum
-
-
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
8.5
the monomeric and dimeric forms have equal activity under optimal conditions
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9.5
pH 7.0: about 75% of maximal activity, pH 9.5: about 85% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
55
the monomeric and dimeric forms have equal activity under optimal conditions
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 60
40°C: about 55% of maximal activity, 60°C: about 95% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
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
-
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
-
malfunction
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
physiological function
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
-
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
-
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MV3K_PICTO
Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)
324
0
36791
Swiss-Prot
-
MV3K_THEAC
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
318
0
35201
Swiss-Prot
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
the monomeric and dimeric forms have equal activity under optimal conditions
monomer
the monomeric and dimeric forms have equal activity under optimal conditions
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme in complex with (R)-5-diphosphomevalonate and adenosine 5'-O-(3-thio)triphosphate or with (R)-5-diphosphomevalonate and ADP, X-ray diffraction structure determination and analysis at 1.5-1.7 A resolution
-
analysis of the substrate-complex crystal structure of TacM3K (PDB ID 4RKS)
hanging drop method, crystal structure of mevalonate-3-kinase in the apo form, and with bound substrates is determined and compared to mevalonate diphosphate decarboxylase structures. The crystal structure of mevalonate-3-kinase provides insight into the mechanism of mevalonate diphosphate decarboxylase. Despite sharing nearly identical overall folds, important active site differences are identified. Glu140 in the center of the mevalonate-3-kinase active site is responsible for binding mevalonate while excluding mevalonate 5-diphosphate, Arg185/Ser105 catalyze phosphate transfer, and an invariant Asp/Lys pair previously thought to be responsible for phosphorylation in mevalonate diphosphate decarboxylase, is missing in mevalonate-3-kinase and replaced by non-essential Thr275/Leu18. A model is proposed in which mevalonate-3-kinase and mevalonate diphosphate decarboxylase both phosphorylate by stabilizing a phosphotransfer transition state (mevalonate-3-kinase via Arg185/Ser105, mevalonate diphosphate decarboxylase via Lys188), suggesting the invariant Asp/Lys pair unique to mevalonate diphosphate decarboxylase may be critical for the decarboxylation step rather than phosphorylation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene Ta1305, the pBAD-TacM plasmid series contains the genes of M3K, M3P5K, BMD, and IPK for the expression of part of modified MVA pathway II. Although the M3K, M3P5K, and IPK genes are derived from Thermoplasma acidophilum, various BMD genes have been utilized for plasmid construction. Recombinant expression of His-tagged enzyme in Escherichia coli strain BL21
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
isobutene production rates are 507 pmol/min*g cells using Escherichia coli cells expressing the enzyme and 2880 pmol/min*mg protein with the purified histidine-tagged enzyme. Isobutene is a small, highly reactive molecule, used extensively as a platform chemical to manufacture a wide variety of products including fuel additives, rubbers, and speciality chemicals
synthesis
-
isobutene production rates are 507 pmol/min*g cells using Escherichia coli cells expressing the enzyme and 2880 pmol/min*mg protein with the purified histidine-tagged enzyme. Isobutene is a small, highly reactive molecule, used extensively as a platform chemical to manufacture a wide variety of products including fuel additives, rubbers, and speciality chemicals
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vinokur, J.M.; Korman, T.P.; Cao, Z.; Bowie, J.U.
Evidence of a novel mevalonate pathway in archaea
Biochemistry
53
4161-4168
2014
Thermoplasma acidophilum (Q9HIN1), Thermoplasma acidophilum
brenda
Azami, Y.; Hattori, A.; Nishimura, H.; Kawaide, H.; Yoshimura, T.; Hemmi, H.
(R)-Mevalonate 3-phosphate is an intermediate of the mevalonate pathway in Thermoplasma acidophilum
J. Biol. Chem.
289
15957-15967
2014
Thermoplasma acidophilum (Q9HIN1)
brenda
Rossoni, L.; Hall, S.J.; Eastham, G.; Licence, P.; Stephens, G.
The putative mevalonate diphosphate decarboxylase from Picrophilus torridus is in reality a mevalonate-3-kinase with high potential for bioproduction of isobutene
Appl. Environ. Microbiol.
81
2625-2634
2015
Picrophilus torridus (Q6KZB1), Picrophilus torridus, Picrophilus torridus DSM 9790 (Q6KZB1)
brenda
Vinokur, J.M.; Korman, T.P.; Sawaya, M.R.; Collazo, M.; Cascio, D.; Bowie, J.U.
Structural analysis of mevalonate-3-kinase provides insight into the mechanisms of isoprenoid pathway decarboxylases
Protein Sci.
24
212-220
2015
Thermoplasma acidophilum (Q9HIN1), Thermoplasma acidophilum
brenda
Motoyama, K.; Sobue, F.; Kawaide, H.; Yoshimura, T.; Hemmi, H.
Conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase by single amino acid mutations
Appl. Environ. Microbiol.
85
e00256-19
2019
Thermoplasma acidophilum (Q9HIN1), Thermoplasma acidophilum, Thermoplasma acidophilum JCM 9062 (Q9HIN1), Thermoplasma acidophilum AMRC-C165 (Q9HIN1), Thermoplasma acidophilum ATCC 25905 (Q9HIN1), Thermoplasma acidophilum NBRC 15155 (Q9HIN1)
brenda
Motoyama, K.; Unno, H.; Hattori, A.; Takaoka, T.; Ishikita, H.; Kawaide, H.; Yoshimura, T.; Hemmi, H.
A single amino acid mutation converts (R)-5-diphosphomevalonate decarboxylase into a kinase
J. Biol. Chem.
292
2457-2469
2017
Saccharolobus solfataricus, Saccharolobus solfataricus P2, Saccharolobus solfataricus JCM 11322, Saccharolobus solfataricus ATCC 35092, Saccharolobus solfataricus DSM 1617
brenda
Oki, K.; Lee, F.S.; Mayo, S.L.
Attempts to develop an enzyme converting DHIV to KIV
Protein Eng. Des. Sel.
32
261-270
2019
Picrophilus torridus (Q6KZB1), Picrophilus torridus, Picrophilus torridus ATCC 700027 (Q6KZB1), Picrophilus torridus NBRC 100828 (Q6KZB1), Picrophilus torridus DSM 9790 (Q6KZB1), Picrophilus torridus JCM 10055 (Q6KZB1)
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 2.7.1.185)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
