2.7.1.36: mevalonate kinase
This is an abbreviated version!
For detailed information about mevalonate kinase, go to the full flat file.
Word Map on EC 2.7.1.36
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2.7.1.36
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fever
-
autoinflammatory
-
cholesterol
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isoprenoids
-
mediterranean
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aciduria
-
hereditary
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receptor-associated
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hyperimmunoglobulinemia
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vinyl
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ketone
-
cryopyrin-associated
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phosphomevalonate
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febrile
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igd
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isopentenyl
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monogenic
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farnesyl
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tnfrsf1a
-
isoprene
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hyper-igd
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anakinra
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rash
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lymphadenopathy
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hmg-coa
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inflammasome
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geranylgeranylation
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amyloidosis
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aphthous
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porokeratosis
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arthralgia
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non-sterol
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pyoderma
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nod2
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papa
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autoinflammation
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gangrenosum
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canakinumab
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adenitis
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pstpip1
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hyperimmunoglobulin
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medicine
-
hepatosplenomegaly
-
cholesterogenesis
-
etanercept
-
cryopyrin
-
synthesis
-
diagnostics
- 2.7.1.36
- fever
- autoinflammatory
- cholesterol
-
isoprenoids
-
mediterranean
- aciduria
- hereditary
-
receptor-associated
- hyperimmunoglobulinemia
-
vinyl
- ketone
-
cryopyrin-associated
- phosphomevalonate
-
febrile
- igd
-
isopentenyl
-
monogenic
-
farnesyl
-
tnfrsf1a
- isoprene
-
hyper-igd
-
anakinra
- rash
- lymphadenopathy
- hmg-coa
- inflammasome
-
geranylgeranylation
- amyloidosis
-
aphthous
- porokeratosis
- arthralgia
-
non-sterol
-
pyoderma
- nod2
- papa
- autoinflammation
- gangrenosum
-
canakinumab
- adenitis
-
pstpip1
-
hyperimmunoglobulin
- medicine
-
hepatosplenomegaly
-
cholesterogenesis
-
etanercept
-
cryopyrin
- synthesis
- diagnostics
Reaction
Synonyms
ATP: mevalonate 5-phosphotransferase, ATP:mevalonate 5-phosphotransferase, GbMVK, kinase, mevalonate (phosphorylating), mevalonate 5-phosphotransferase, mevalonate phosphokinase, mevalonic acid kinase, mevalonic kinase, MmMK, MVA kinase, MVK, SSO0383, TcMVK, TeMVK
ECTree
2.7.1.36 mevalonate kinaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 2.7.1.36 - mevalonate kinase
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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
adenosine 5'-O-(1-thio-triphosphate) + mevalonate
adenosine 5'-O-(1-thio-diphosphate) + 5-phosphomevalonate
-
40% of activity with ATP in the presence of 2 mM Mg2+
-
?
adenosine 5'-O-(2-thio-triphosphate) + mevalonate
adenosine 5'-O-(2-thio-diphosphate) + 5-phosphomevalonate
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54% of activity with ATP in the presence of 2 mM Mg2+
-
?
adenosine 5'-O-(3-thio-triphosphate) + mevalonate
adenosine 5'-O-(3-thio-diphosphate) + 5-phosphomevalonate
-
4% of activity with ATP in the presence of 2 mM Mg2+
-
?
dATP + mevalonate
dADP + phosphomevalonate
-
67% of the activity with ATP
-
?
dCTP + mevalonate
dCDP + phosphomevalonate
-
17% of the activity with ATP
-
?
dGTP + mevalonate
dGDP + phosphomevalonate
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17% of the activity with ATP
-
?
TTP + mevalonate
TDP + phosphomevalonate
-
15% of the activity with ATP
-
?
XTP + mevalonate
XDP + phosphomevalonate
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27% of the activity with ATP
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
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100% activity with ATP
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
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involved in isopentenyl diphosphate synthesis
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
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involved in cholesterol synthesis
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
involved in cholesterol synthesis, decreased enzyme activity involved in mevalonic aciduria and hyperimmunoglobulin D syndrome
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
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a step in the production of farnesyldiphosphate and geranylgeranyl diphosphate, overview
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
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involved in cholesterol synthesis
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
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involved in cholesterol, steroid hormones und terpenoids synthesis
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
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a step in the mevalonate pathway, overview
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
the enzyme is involved in the modified mevalonate pathway. The recombinant protein is active. However in vitro conversion of the intermediates in the classical and modified pathways by cell-free extract from Sulfolobus solfataricus indicates that only the classical pathway likely works in the organism
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
the enzyme is involved in the modified mevalonate pathway. The recombinant protein is active. However in vitro conversion of the intermediates in the classical and modified pathways by cell-free extract from Sulfolobus solfataricus indicates that only the classical pathway likely works in the organism
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
involved in isopentenyl diphosphate synthesis
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
the enzyme catalyzes a step in the isoprenoid biosynthetic pathway via the essential intermediate 5-diphosphomevalonate
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
substrate binding structure, overview
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
ATP is the most effective phosphate donor
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
via mevalonate pathway involved in isoprenoid biosynthesis
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
no activity with GTP
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
no activity with CTP
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
no activity with ADP
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
mevalonate kinase is probably involved in regulation of cholesterol biosynthesis
-
?
ATP + mevalonate
ADP + phosphomevalonate
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part of the cholesterol and nonsterol isoprene biosynthetic pathway
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
involved in mevalonate pathway of terpenoid biosynthesis
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
ATP is the most effective phosphate donor
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
no activity with ADP, GTP and UTP
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
no activity with ITP, UTP and ADP
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
ATP is the most effective phosphate donor
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
enzyme may play a key role in regulating cholesterol biosynthesis
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
no activity with ADP
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
stereospecific reaction with R-mevalonate
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
ATP is the most effective phosphate donor
-
ir
ATP + mevalonate
ADP + phosphomevalonate
-
ATPgammaS, ATPalphaS and ATPbetaS can act as substrates in presence of different activating divalent metal cations, in the presence of Mg2+ the R diastereomers of both ATPalphaS and ATPbetaS are the preferred substrates, in presence of Cd2+ the S diastereomers are more active
-
?
CTP + (R)-mevalonate
CDP + (R)-5-phosphomevalonate
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5% activity with GTP compared to ATP
-
-
?
GTP + (R)-mevalonate
GDP + (R)-5-phosphomevalonate
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15% activity with GTP compared to ATP
-
-
?
GTP + mevalonate
GDP + phosphomevalonate
-
18% of the activity with ATP
-
?
ITP + mevalonate
IDP + phosphomevalonate
-
36% of activity with ATP
-
?
TTP + (R)-mevalonate
TDP + (R)-5-phosphomevalonate
-
11% activity with GTP compared to ATP
-
-
?
UTP + mevalonate
UDP + phosphomevalonate
-
61% of the activity with ATP
-
?
additional information
?
-
-
mevalonate kinase is directly involved in regulation of luteinizing hormone receptor expression
-
-
?
additional information
?
-
-
analysis of substrate and product binding by archaeal mevalonate kinase compared to eukaryotic enzymes, a striking lack of direct interactions between this archaeal MK and its substrate is detected, substrate-binding site structure, overview
-
-
-
additional information
?
-
-
the enzyme catalyzes a step in the isoprenoid biosynthetic pathway, which leads to a huge number of compounds that play important roles in plant growth and development
-
-
?
additional information
?
-
the enzyme is involved in the modified mevalonate pathway. The recombinant protein is active. However in vitro conversion of the intermediates in the classical and modified pathways by cell-free extract from Sulfolobus solfataricus indicates that only the classical pathway likely works in the organism
-
-
?
additional information
?
-
-
the enzyme is involved in the modified mevalonate pathway. The recombinant protein is active. However in vitro conversion of the intermediates in the classical and modified pathways by cell-free extract from Sulfolobus solfataricus indicates that only the classical pathway likely works in the organism
-
-
?
additional information
?
-
the enzyme is involved in the modified mevalonate pathway. The recombinant protein is active. However in vitro conversion of the intermediates in the classical and modified pathways by cell-free extract from Sulfolobus solfataricus indicates that only the classical pathway likely works in the organism
-
-
?
additional information
?
-
the recombinant enzyme phosphorylates racemic vinyl, ethyl, n-propyl, n-butyl, i-butyl, 2-propenyl, allyl, ethynyl, and 1-propynyl mevalonate lactone analogues, that are diphosphorylated by phosphomevalonate kinase, EC 2.7.4.2, in a second step, overview
-
-
?
additional information
?
-
-
the recombinant enzyme phosphorylates racemic vinyl, ethyl, n-propyl, n-butyl, i-butyl, 2-propenyl, allyl, ethynyl, and 1-propynyl mevalonate lactone analogues, that are diphosphorylated by phosphomevalonate kinase, EC 2.7.4.2, in a second step, overview
-
-
?
additional information
?
-
-
a coupled assay method is performed using lactic dehydrogenase and pyruvate kinase. Specific activity of the three different oligomeric states of purified TeMVK is evaluated using a fluorescence-based assay. TeMVK is highly active only in its tetrameric form
-
-
-
additional information
?
-
Trypanosoma evansi 29-19
-
a coupled assay method is performed using lactic dehydrogenase and pyruvate kinase. Specific activity of the three different oligomeric states of purified TeMVK is evaluated using a fluorescence-based assay. TeMVK is highly active only in its tetrameric form
-
-
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