Information on EC 2.7.1.185 - mevalonate 3-kinase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.1.185
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RECOMMENDED NAME
GeneOntology No.
mevalonate 3-kinase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + (R)-mevalonate = ADP + (R)-3-phosphomevalonate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
mevalonate pathway III (archaea)
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Terpenoid backbone biosynthesis
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mevalonate metabolism
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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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
show the reaction diagram
ATP + 3-hydroxyisovalerate
ADP + phosphate + isobutene + CO2
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
show the reaction diagram
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.097 - 3.1
(R)-mevalonate
0.023
ATP
pH 7.5, 30C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.31 - 5.8
(R)-mevalonate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.19 - 51.5
(R)-mevalonate
1361
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9.5
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pH 7.0: about 75% of maximal activity, pH 9.5: about 85% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 60
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40C: about 55% of maximal activity, 60C: about 95% of maximal activity
PDB
SCOP
CATH
ORGANISM
UNIPROT
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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the monomeric and dimeric forms have equal activity under optimal conditions
monomer
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the monomeric and dimeric forms have equal activity under optimal conditions
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
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1 h, enzyme retains more than 95% of its activity
70
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1 h, about 75% loss of activity
75
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1 h, complete loss of activity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L18A
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kcat/KM for (R)-mevalonate is 4.4% compared to the wild-type value
R185A
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mutation results in no detectable activity
R185K
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kcat/KM for (R)-mevalonate is 0.5% compared to the wild-type value
S105A
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kcat/KM for (R)-mevalonate is 10.3% compared to the wild-type value
T275A
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kcat/KM for (R)-mevalonate is 25.6% compared to the wild-type value
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis