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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
-
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+
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
ATP + mevalonate
ADP + phosphomevalonate
Ca-adenosine 5'-O-(2-thio-(R)-triphosphate) + (R)-mevalonate
?
-
-
-
-
?
Ca-adenosine 5'-O-(2-thio-(S)-triphosphate) + (R)-mevalonate
?
-
-
-
-
?
Cd-adenosine 5'-O-(1-thio-(R)-triphosphate) + (R)-mevalonate
?
-
-
-
-
?
Cd-adenosine 5'-O-(1-thio-(S)-triphosphate) + (R)-mevalonate
?
-
-
-
-
?
Cd-adenosine 5'-O-(2-thio-(R)-triphosphate) + (R)-mevalonate
?
-
-
-
-
?
Cd-adenosine 5'-O-(2-thio-(S)-triphosphate) + (R)-mevalonate
?
-
-
-
-
?
Co-adenosine 5'-O-(1-thio-(R)-triphosphate) + (R)-mevalonate
?
-
-
-
-
?
Co-adenosine 5'-O-(1-thio-(S)-triphosphate) + (R)-mevalonate
?
-
-
-
-
?
Co-adenosine 5'-O-(2-thio-(R)-triphosphate) + (R)-mevalonate
?
-
-
-
-
?
Co-adenosine 5'-O-(2-thio-(S)-triphosphate) + (R)-mevalonate
?
-
-
-
-
?
CTP + (R)-mevalonate
CDP + (R)-5-phosphomevalonate
CTP + mevalonate
CDP + phosphomevalonate
dATP + mevalonate
dADP + phosphomevalonate
-
67% of the activity with ATP
-
?
dCTP + mevalonate
dCDP + phosphomevalonate
-
17% of the activity with ATP
-
?
dGTP + mevalonate
dGDP + phosphomevalonate
-
17% of the activity with ATP
-
?
GTP + (R)-mevalonate
GDP + (R)-5-phosphomevalonate
GTP + mevalonate
GDP + phosphomevalonate
ITP + (R)-mevalonate
IDP + (R)-5-phosphomevalonate
-
-
-
-
?
ITP + mevalonate
IDP + phosphomevalonate
Mg-adenosine 5'-O-(1-thio-(R)-triphosphate) + (R)-mevalonate
?
-
-
-
-
?
Mg-adenosine 5'-O-(1-thio-(S)-triphosphate) + (R)-mevalonate
?
-
-
-
-
?
Mg-adenosine 5'-O-(2-thio-(R)-triphosphate) + (R)-mevalonate
?
-
-
-
-
?
Mg-adenosine 5'-O-(2-thio-(S)-triphosphate) + (R)-mevalonate
?
-
-
-
-
?
Mn-adenosine 5'-O-(2-thio-(R)-triphosphate) + (R)-mevalonate
?
-
-
-
-
?
Mn-adenosine 5'-O-(2-thio-(S)-triphosphate) + (R)-mevalonate
?
-
-
-
-
?
Ni-adenosine 5'-O-(2-thio-(R)-triphosphate) + (R)-mevalonate
?
-
-
-
-
?
Ni-adenosine 5'-O-(2-thio-(S)-triphosphate) + (R)-mevalonate
?
-
-
-
-
?
TTP + (R)-mevalonate
TDP + (R)-5-phosphomevalonate
TTP + mevalonate
TDP + phosphomevalonate
-
15% of the activity with ATP
-
?
UTP + (R)-mevalonate
UDP + (R)-5-phosphomevalonate
-
-
-
-
?
UTP + mevalonate
UDP + phosphomevalonate
XTP + mevalonate
XDP + phosphomevalonate
-
27% of the activity with ATP
-
?
Zn-adenosine 5'-O-(2-thio-(R)-triphosphate) + (R)-mevalonate
?
-
-
-
-
?
Zn-adenosine 5'-O-(2-thio-(S)-triphosphate) + (R)-mevalonate
?
-
-
-
-
?
additional information
?
-
ADP + mevalonate
?
-
-
-
-
?
ADP + mevalonate
?
-
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
100% activity with ATP
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
involved in isopentenyl diphosphate synthesis
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
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
-
-
-
r
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
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
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
involved in cholesterol synthesis
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
involved in cholesterol, steroid hormones und terpenoids synthesis
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
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
-
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
involved in isopentenyl diphosphate synthesis
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
-
-
?
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 + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
-
-
-
r
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
-
-
-
?
ATP + (R)-mevalonate
ADP + (R)-5-phosphomevalonate
-
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
ATP is the most effective phosphate donor
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
via mevalonate pathway involved in isoprenoid biosynthesis
-
?
ATP + mevalonate
ADP + phosphomevalonate
Citrus sp.
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
?
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
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
mevalonate kinase is probably involved in regulation of cholesterol biosynthesis
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
part of the cholesterol and nonsterol isoprene biosynthetic pathway
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
involved in mevalonate pathway of terpenoid biosynthesis
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
?
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
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
no activity with GTP
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
no activity with ITP, UTP and ADP
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
?
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
-
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
no activity with ADP
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
?
ATP + mevalonate
ADP + phosphomevalonate
-
-
-
-
?
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
-
5% activity with GTP compared to ATP
-
-
?
CTP + (R)-mevalonate
CDP + (R)-5-phosphomevalonate
-
-
-
-
?
CTP + mevalonate
CDP + phosphomevalonate
-
weak activity
-
?
CTP + mevalonate
CDP + phosphomevalonate
-
-
-
?
CTP + mevalonate
CDP + phosphomevalonate
-
18% of activity with ATP
-
?
GTP + (R)-mevalonate
GDP + (R)-5-phosphomevalonate
-
15% activity with GTP compared to ATP
-
-
?
GTP + (R)-mevalonate
GDP + (R)-5-phosphomevalonate
-
-
-
-
?
GTP + mevalonate
GDP + phosphomevalonate
-
-
-
?
GTP + mevalonate
GDP + phosphomevalonate
-
weak activity
-
?
GTP + mevalonate
GDP + phosphomevalonate
-
-
-
?
GTP + mevalonate
GDP + phosphomevalonate
-
18% of the activity with ATP
-
?
ITP + mevalonate
IDP + phosphomevalonate
-
-
-
?
ITP + mevalonate
IDP + phosphomevalonate
-
as effective as ATP
-
?
ITP + mevalonate
IDP + phosphomevalonate
-
36% of activity with ATP
-
?
ITP + mevalonate
IDP + phosphomevalonate
-
-
-
?
ITP + mevalonate
IDP + phosphomevalonate
-
-
-
?
ITP + mevalonate
IDP + phosphomevalonate
-
88% of activity with ATP
-
?
TTP + (R)-mevalonate
TDP + (R)-5-phosphomevalonate
-
11% activity with GTP compared to ATP
-
-
?
TTP + (R)-mevalonate
TDP + (R)-5-phosphomevalonate
-
-
-
-
?
UTP + mevalonate
UDP + phosphomevalonate
-
-
-
?
UTP + mevalonate
UDP + phosphomevalonate
-
weak activity
-
?
UTP + mevalonate
UDP + phosphomevalonate
-
-
-
?
UTP + mevalonate
UDP + phosphomevalonate
-
-
-
?
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
?
-
-
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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(3R),(5S)-P'-geranyl 3,5,8-trihydroxy-3-methyloctanate 8-diphosphate
-
-
(3S),(5R)-P'-geranyl 3,5,8-trihydroxy-3-methyloctanate 8-diphosphate
-
-
25-hydroxycholesterol
-
expression of mevalonate kinase is regulated by sterol response element-binding protein-1, which is sensitive to the cllular concentration of 25-hydroxycholesterol. Presence of 25-hydroxycholesterol inhibits mevalonate kinase expression and subsequently its binding to luteinizing hormone receptor mRNA
3,3-dimethylallyl diphosphate
-
-
5-diphosphomevalonate
-
allosteric and potent inhibition, the molecule functions as a partial bisubstrate analogue that elicits a ternary-complex-like form of the enzyme, binding structure, overview
5-phosphomevalonate
-
product inhibition, non-competitive with ATP and mevalonate
8-[[hydroxy(phosphonooxy)phosphoryl]oxy]octanoic acid
-
-
estradiol
-
together with follicle-stimulating hormone, decreases mevalonate kinase mRNA levels, resulting in up-regulation of luteinizing hormone receptor mRNA that is inversely correlated to mevalonate kinase mRNA expression
follicle-stimulating hormone
-
together with estradiol, decreases mevalonate kinase mRNA levels, resulting in up-regulation of luteinizing hormone receptor mRNA that is inversely correlated to mevalonate kinase mRNA expression
-
geranylgeranyl diphosphate
HgCl2
-
0.1 mM, 90% inhibition
isopentenyl diphosphate
-
-
lovastatin
-
inhibition of isoprenoid pathway, resulting in a dose-dependent reduction of amyloid formed compared with mononuclear cells that are exposed only to serum amyloid. The inhibitory effects of lovastatin are reversible by addition of farnesol but not geranylgeraniol. Farnesyl transferase inhibition also inhibits amyloidogenesis
mevalonate 5-diphosphate
-
-
N-ethylmaleimide
-
0.1 mM, 66% inhibition, 1 mM, 94% inhibition
P'-geranyl 3,5,7-trihydroxy-3-methylheptanate 7-diphosphate
-
-
P'-geranyl 3,5,8-trihydroxy-3-methyloctanate 8-diphosphate
-
-
P'-geranyl 3,5,9-trihydroxy-3-methylnonanate 9-diphosphate
-
-
P'-geranyl octanate 8-diphosphate
-
-
prenyl phosphates
-
competitive with ATP
pyridoxal 5'-phosphate
-
-
SH-group directed reagent
-
-
-
ZnSO4
-
0.1 mM, 90% inhibition
ADP
-
product inhibition vs. ATP at concentration above 2 mM
ADP
-
very weak inhibition
CuSO4
-
0.1 mM, 56% inhibition, 1 mM, 77% inhibition
CuSO4
-
10 mM, almost complete inhibition
diphosphomevalonate
-
functions as a partial bisubstrate analogue and elicits a ternary-complex like form of the enzyme
diphosphomevalonate
strong feedback inhibitor of the enzyme
EDTA
-
-
EDTA
-
10 mM, almost complete inhibition
farnesyl diphosphate
-
-
farnesyl diphosphate
-
competitive vs. ATP
farnesyl diphosphate
-
feedback inhibition, competitive with ATP
farnesyl diphosphate
feedback regulation
farnesyl diphosphate
-
0.01 mM, 65% inhibition
farnesyl diphosphate
-
0.3 mM, approx. 75% inhibition
farnesyl diphosphate
-
feedback inhibition, competitive with ATP
farnesyl diphosphate
-
competitive with ATP
farnesyl diphosphate
-
feedback inhibition, competitive with ATP
farnesyl diphosphate
-
potent inhibitor
farnesyl thiodiphosphate
-
feedback inhibition, competitive with ATP
farnesyl thiodiphosphate
-
feedback inhibition, competitive with ATP
farnesyl thiodiphosphate
competitive with ATP, feedback regulation
farnesyl thiodiphosphate
-
feedback inhibition, competitive with ATP
geranyl diphosphate
-
-
geranyl diphosphate
-
0.01 mM, 55% inhibition
geranyl diphosphate
-
0.3 mM, approx. 10% inhibition
geranyl diphosphate
-
competitive with ATP
geranyl diphosphate
-
potent inhibitor
geranylgeranyl diphosphate
-
-
geranylgeranyl diphosphate
-
-
geranylgeranyl diphosphate
-
-
geranylgeranyl diphosphate
-
-
geranylgeranyl diphosphate
-
-
geranylgeranyl diphosphate
-
0.3 mM, approx. 90% inhibition
geranylgeranyl diphosphate
-
competitive with ATP
geranylgeranyl diphosphate
-
-
mevalonate
-
at high concentrations
mevalonate
-
substrate inhibition at millimolar concentrations, 50% inhibition at 2.88 mM
mevalonate 5-phosphate
-
noncompetitive vs. ATP, mixed-type vs. mevalonate
mevalonate 5-phosphate
-
0.3 mM, approx. 45% inhibition
Mn2+
-
inhibition at high concentrations
Mn2+
-
inhibition at high concentrations
Mn2+
-
inhibition at 10 mM in crude extracts
Mn2+
-
inhibition above 2.5 mM
p-chloromercuribenzoate
-
0.1 mM, 95% inhibition, 1 mM, complete inhibition
p-chloromercuribenzoate
-
activity can be almost completely restored by incubation with an excess of cysteine
p-chloromercuribenzoate
-
1 mM, almost complete inhibition
p-chloromercuribenzoate
-
0.1 mM, 83% inhibition, completely reversed by reduced glutathione
phytyl diphosphate
-
-
phytyl diphosphate
-
0.3 mM, almost complete inhibition
additional information
-
not inhibited by by isopentenyl diphosphate and dimethylallyl diphosphate
-
additional information
-
no inhibition with AMP
-
additional information
-
-
-
additional information
-
not inhibited by iodoacetamide
-
additional information
-
not inhibited by R-mevalonate 5-diphosphate, geraniol and dolichol up to 0.084, 0.226 and 0.68 mM, respectively
-
additional information
-
the enzyme is not inhibited by dimethylallyl diphosphate, geranyl diphosphate, farnesyl diphosphate, isopentenyl monophosphate, and diphosphomevalonate
-
additional information
-
organic synthesis of bisubstrate analogues, organic synthesis and biological characterization of bifunctional molecules, which can inhibit both MVK and mevalonate 5-diphosphate decarboxylase
-
additional information
synthesis of a series of C3-substituted mevalonate analogues to probe the steric and electronic requirements of the mevalonate kinase active site for development of specific mechanism-based inhibitors, overview
-
additional information
-
synthesis of a series of C3-substituted mevalonate analogues to probe the steric and electronic requirements of the mevalonate kinase active site for development of specific mechanism-based inhibitors, overview
-
additional information
-
not inhibited by isopentenyl and dimethyldiphosphate and phosphate
-
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0.0324 - 2.16
(R)-mevalonate
0.035 - 2.88
(R,S)-mevalonate
0.024 - 0.167
(R,S)mevalonate
0.27
(RS)-mevalonate
-
pH 7.0, 25°C
0.019 - 0.27
(RS)mevalonate
0.6
Ca-adenosine 5'-O-(2-thio-(R)-triphosphate)
-
pH 8.0
0.14
Ca-adenosine 5'-O-(2-thio-(S)-triphosphate)
-
pH 8.0
0.22
Cd-adenosine 5'-O-(1-thio-(R)-triphosphate)
-
pH 8.0
0.28
Cd-adenosine 5'-O-(1-thio-(S)-triphosphate)
-
pH 8.0
0.059
Cd-adenosine 5'-O-(2-thio-(R)-triphosphate)
-
pH 8.0
0.46
Cd-adenosine 5'-O-(2-thio-(S)-triphosphate)
-
pH 8.0
0.09
Co-adenosine 5'-O-(1-thio-(R)-triphosphate)
-
pH 8.0
0.2
Co-adenosine 5'-O-(1-thio-(S)-triphosphate)
-
pH 8.0
0.05
Co-adenosine 5'-O-(2-thio-(R)-triphosphate)
-
pH 8.0
0.1
Co-adenosine 5'-O-(2-thio-(S)-triphosphate)
-
pH 8.0
2.44
Mg-adenosine 5'-O-(1-thio-(R)-triphosphate)
-
pH 8.0
0.16
Mg-adenosine 5'-O-(1-thio-(S)-triphosphate)
-
pH 8.0
0.59
Mg-adenosine 5'-O-(2-thio-(R)-triphosphate)
-
pH 8.0
0.12
Mg-adenosine 5'-O-(2-thio-(S)-triphosphate)
-
pH 8.0
0.29
Mn-adenosine 5'-O-(2-thio-(R)-triphosphate)
-
pH 8.0
0.075
Mn-adenosine 5'-O-(2-thio-(S)-triphosphate)
-
pH 8.0
0.091
Ni-adenosine 5'-O-(2-thio-(R)-triphosphate)
-
pH 8.0
0.14
Ni-adenosine 5'-O-(2-thio-(S)-triphosphate)
-
pH 8.0
0.041
R,S-mevalonate
-
pH 7.5, 30°C
0.0426 - 0.046
RS-mevalonate
0.12
Zn-adenosine 5'-O-(2-thio-(R)-triphosphate)
-
pH 8.0
0.058
Zn-adenosine 5'-O-(2-thio-(S)-triphosphate)
-
pH 8.0
additional information
additional information
-
Michaelis-Menten kinetics
-
0.0324
(R)-mevalonate
mutant T104A, 30°C, pH 7.5
0.035
(R)-mevalonate
-
native enzyme, pH 7.5, 25°C
0.035
(R)-mevalonate
-
wild-type, pH 7.5, 34°C
0.0408
(R)-mevalonate
wild-type, 30°C, pH 7.5
0.0459
(R)-mevalonate
mutant R388X, 30°C, pH 7.5
0.0473
(R)-mevalonate
mutant L54A, 30°C, pH 7.5
0.061
(R)-mevalonate
-
mutant C281S, pH 7.5, 34°C
0.068
(R)-mevalonate
-
apparent value, in 50 mM Tris, 50 mM NaCl (pH 7.6), at 30°C
0.07
(R)-mevalonate
-
mutant C107A, pH 7.5, 34°C
0.071
(R)-mevalonate
-
mutant C107A/C281A, pH 7.5, 34°C
0.0745
(R)-mevalonate
mutant T104A/I196A, 30°C, pH 7.5
0.076
(R)-mevalonate
-
mutant C107S, pH 7.5, 34°C
0.09
(R)-mevalonate
-
at pH 7.5, temperature not specified in the publication
0.106
(R)-mevalonate
-
mutant C281A, pH 7.5, 34°C
0.106
(R)-mevalonate
-
wild-type, pH 7.5, 34°C
0.111
(R)-mevalonate
-
mutant C107S/C281S, pH 7.5, 34°C
0.1163
(R)-mevalonate
mutant I196A, 30°C, pH 7.5
0.186
(R)-mevalonate
-
mutant A141C, pH 7.5, 34°C
0.228
(R)-mevalonate
mutant I56A, 30°C, pH 7.5
0.323
(R)-mevalonate
mutant Y149A, 30°C, pH 7.5
0.33
(R)-mevalonate
-
pH 10, 37°C
0.3319
(R)-mevalonate
at pH 7.0 and 30°C
0.4591
(R)-mevalonate
mutant T104A/I196A/R388X, 30°C, pH 7.5
0.616
(R)-mevalonate
-
H20L mutant enzyme, pH 7.5, 25°C
2.16
(R)-mevalonate
-
H20Y mutant enzyme, pH 7.5, 25°C
0.035
(R,S)-mevalonate
-
pH 7.5, 25°C, recombinant mevalonate kinase
0.069
(R,S)-mevalonate
-
pH 8.0, 70°C, recombinant mevalonate kinase
0.15
(R,S)-mevalonate
-
pH 7.0, 25°C, recombinant mevalonate kinase
0.288
(R,S)-mevalonate
-
pH 7.0, 30°C
2.88
(R,S)-mevalonate
-
pH 7.0, 30°C, K13M mutant mevalonate kinase
0.024
(R,S)mevalonate
-
-
0.167
(R,S)mevalonate
-
V377I mutant mevalonate kinase
0.019
(RS)mevalonate
-
liver mevalonate kinase
0.069
(RS)mevalonate
-
recombinant mevalonate kinase
0.27
(RS)mevalonate
liver mevalonate kinase
0.025
ATP
-
mutant D204A, pH 7.0, 30°C
0.0403
ATP
mutant T104A, 30°C, pH 7.5
0.066
ATP
-
mutant D204N, pH 7.0, 30°C
0.074
ATP
-
wild-type, pH 7.0, 30°C
0.092
ATP
-
pH 8.0, 70°C, recombinant mevalonate kinase
0.092
ATP
-
recombinant mevalonate kinase
0.1
ATP
-
V377I mutant mevalonate kinase
0.113
ATP
-
mutant E19D, pH 7.0, 30°C
0.131
ATP
-
mutant E296Q, pH 7.0, 30°C
0.14
ATP
-
at pH 7.5, temperature not specified in the publication
0.1474
ATP
at pH 7.0 and 30°C
0.15
ATP
-
pH 7.5, 30°C, recombinant S145A mutant mevalonate kinase
0.166
ATP
-
pH 7.0, 30°C, K13M mevalonate kinase
0.1784
ATP
wild-type, 30°C, pH 7.5
0.2321
ATP
mutant L54A, 30°C, pH 7.5
0.3
ATP
-
liver mevalonate kinase
0.3018
ATP
mutant I196A, 30°C, pH 7.5
0.3077
ATP
mutant T104A/I196A, 30°C, pH 7.5
0.38
ATP
-
pH 7.5, 30°C, recombinant T243A mevalonate kinase
0.3954
ATP
mutant T104A/I196A/R388X, 30°C, pH 7.5
0.41
ATP
-
pH 7.5, 30°C, recombinant S146A mevalonate kinase
0.44
ATP
-
pH 7.0, 25°C, recombinant mevalonate kinase
0.464
ATP
-
apparent value, in 50 mM Tris, 50 mM NaCl (pH 7.6), at 30°C
0.51
ATP
-
pH 7.5, 30°C, recombinant S201A mevalonate kinase
0.614
ATP
mutant R388X, 30°C, pH 7.5
0.68
ATP
-
pH 6.5, 30°C, at 1 mM Mg2+
0.68
ATP
-
ATP in form of MgATP2-
0.6896
ATP
mutant Y149A, 30°C, pH 7.5
0.8097
ATP
mutant I56A, 30°C, pH 7.5
0.95
ATP
-
pH 7.5, 25°C, recombinant mevalonate kinase
0.95
ATP
-
wild-type, pH 7.5, 34°C
0.953
ATP
-
native enzyme, pH 7.5, 25°C
0.97
ATP
-
mutant A141C, pH 7.5, 34°C
1.18
ATP
-
wild-type, pH 7.5, 34°C
1.22
ATP
-
pH 7.5, 34°C, K272R mutant mevalonate kinase
1.54
ATP
-
pH 7.0, 30°C, enzyme from etiolated cotyledons
1.54
ATP
-
pH 7.5, 34°C, R196L mutant mevalonate kinase
1.56
ATP
-
mutant E193Q, pH 7.0, 30°C
1.58
ATP
-
mutant C107A/C281A, pH 7.5, 34°C
1.75
ATP
-
pH 7.0, 30°C, enzyme fom green leaves
1.75
ATP
liver mevalonate kinase
1.75
ATP
-
ATP in form of MgATP2-
1.81
ATP
-
H20L mutant enzyme, pH 7.5, 25°C
2.61
ATP
-
mutant C107A, pH 7.5, 34°C
2.7
ATP
-
H20Y mutant enzyme enzyme, pH 7.5, 25°C
2.76
ATP
-
mutant C281A, pH 7.5, 34°C
2.95
ATP
-
pH 7.5, 34°C, K272A mutant mevalonate kinase
2.97
ATP
-
mutant C281S, pH 7.5, 34°C
2.98
ATP
-
pH 7.5, 34°C, R196Q mutant mevalonate kinase
3
ATP
-
pH 7.5, 34°C, R196V mutant mevalonate kinase
3.11
ATP
-
mutant C107S, pH 7.5, 34°C
3.36
ATP
-
mutant C107S/C281S, pH 7.5, 34°C
0.13
DL-mevalonate
-
pH 7.5, 30°C
5.1
DL-mevalonate
-
pH 7.0, 35°C
0.012
mevalonate
-
mutant D204N, pH 7.0, 30°C
0.024
mevalonate
-
wild-type, pH 7.0, 30°C
0.05
mevalonate
-
pH 7.9, 37°C
0.052
mevalonate
-
mutant E19D, pH 7.0, 30°C
0.076
mevalonate
-
pH 7.5, 30°C
0.08
mevalonate
-
pH 7.9, 37°C
0.11
mevalonate
-
pH 7.5, 34°C
0.11
mevalonate
-
mutant E296Q, pH 7.0, 30°C
0.2
mevalonate
-
mutant D204A, pH 7.0, 30°C
0.25
mevalonate
-
pH 7.5, 34°C, K272R mutant mevalonate kinase
0.253
mevalonate
-
pH 7.5, 30°C, recombinant S145A mevalonate kinase
0.47
mevalonate
-
pH 7.5, 30°C, recombinant T243A mevalonate kinase
0.51
mevalonate
-
pH 7.5, 30°C, recombinant S146A mevalonate kinase
0.51
mevalonate
-
pH 7.5, 34°C, K272A mutant mevalonate kinase
1.02
mevalonate
-
mutant E193Q, pH 7.0, 30°C
1.43
mevalonate
-
pH 7.5, 34°C, R196L mutant mevalonate kinase
2.5
mevalonate
-
pH 7.5, 30°C, recombinant S201A mevalonate kinase
4.03
mevalonate
-
pH 7.5, 34°C, R196V mutant mevalonate kinase
9.28
mevalonate
-
pH 7.5, 34°C, R196Q mutant mevalonate kinase
0.0426
RS-mevalonate
-
pH 7.0, 30°C, enzyme from etiolated cotyledons
0.046
RS-mevalonate
-
pH 7.0, 30°C, leaf enzyme
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A148T
mutation may be responsible for the hyperimmunoglobulinemia phenotype
C152Y
identification of a mevalonate kinase heterozygous missense point mutation in exon 5 (c.455:G[A]), resulting in the substitution of tyrosine for cysteine (p.C152Y) in a predicted functional domain of the MVK enzyme. The patient shows disseminated superficial actinic porokeratosis (DSAP), which is a genodermatosis with autosomal dominant inheritance and near-complete penetrance clinically featuring uniform 3- to 7-mm annular lesions with scaly borders on sun-exposed face and extremities. The hyperkeratotic rim correlates histopathologically with the presence of a cornoid lamella. Phenotype, overview
D204A
-
stable, with 40000fold diminution in kcat. Mutant is able to bind a spin-labeled ATP analogue with stoichiometries and equilibrium binding constants comparable to wild-type
D204N
-
stable, with 40000fold diminution in kcat. Mutant is able to bind a spin-labeled ATP analogue with stoichiometries and equilibrium binding constants comparable to wild-type
E148Q
-
mutation detected in patient with hyperimmunoglobulinemia D and periodic fever syndrome
E193Q
-
50fold diminution in Vmax and 20fold increase Km values for ATP, 40fold increase in Km for mevalonate
E19D
-
stable, decrease in Vmax to 40% of wild-type
E296Q
-
stable. Kinetic parameters similar to wild-type
G336S
-
homozygous mutation determined in a patient with severe deficiency in mevalonate kinase associated with nephritis. Catalytic activity is less than 1% of wild-type activity
H20A
-
insoluble upon expression in Escherichia coli
H20P
markedly decreased mevalonate kinase activity when expressed in Escherichia coli
I196A
modest changes in Km and Ki values
I56A
4.5fold increase in Km value for ATP
L264F
markedly decreased mevalonate kinase activity when expressed in Escherichia coli
L265P
markedly decreased mevalonate kinase activity when expressed in Escherichia coli
L53A
modest changes in Km and Ki values
N301T
5-20% of wild-type activity
P165L
mutation may be responsible for the hyperimmunoglobulinemia phenotype
Q390P
-
mutation determined in patient with mevalonate kinase deficiency. Gene additionally has a four-base deletion c.475-478 delACTG
R388X
modest changes in Km and Ki values
S145A
-
37% of wild-type activity
S146A
-
0.02% of wild-type activity
S201A
-
200% of wild-type activity
S378P/V377I/R92Q
-
naturally occuring mutation in the MVK gene, the mutation leads to reduced enzyme activity, which participates in the development of the hyperimmunoglobulinemia D and periodic fever syndrome, HIDS, an autosomal recessively inherited autoinflammatory disease, R92Q is a low-penetrance mutation, phenotype, overview
T104A
modest changes in Km and Ki values
T104A/I196A
39fold increase in Ki value
T104A/I196A/R388X
11fold increase in Km value for mevalonate
T243A
-
39% of wild-type activity
T243I
markedly decreased mevalonate kinase activity when expressed in Escherichia coli
V310M
markedly decreased mevalonate kinase activity when expressed in Escherichia coli
V377I
mutation may be responsible for the hyperimmunoglobulinemia phenotype
V377I/I268T
-
mutation determined in patients with hyperimmunoglobulinemia D and periodic fever syndrome. Patients developed significant B cell cytopenia with hypogammaglobulinemia. Therapy of prednisone, azathioprine, and intravenous immunoglobulins resulted in reduced incidence and severity of febrile attacks
V377I/R92Q
-
naturally occuring mutation in the MVK gene, the mutation leads to reduced enzyme activity, which participates in the development of the hyperimmunoglobulinemia D and periodic fever syndrome, HIDS, an autosomal recessively inherited autoinflammatory disease, R92Q is a low-penetrance mutation, phenotype, overview
Y149A
8fold increase in Km value for mevalonate
C107A
-
decrease in temperature stability, slight increase in Km value for ATP
C107S
-
decrease in temperature stability, slight increase in Km value for ATP
C107S/C281S
-
decrease in temperature stability, slight increase in Km value for ATP
C197A/C281A
-
decrease in temperature stability, slight increase in Km value for ATP
C281A
-
decrease in temperature stability, slight increase in Km value for ATP
C281S
-
decrease in temperature stability, slight increase in Km value for ATP
K272A
-
18% of wild-type activity
K272R
-
18% of wild-type activity
R196L
-
5% of wild-type activity
R196V
-
60% of wild-type activity
A141C
-
significantly higher thermal activity than wild-type
D204N
-
mutation in active site, decrease in luteinizing hormone receptor mRNA binding
D316A
-
mutation outside tie active site, no change in luteinizing hormone receptor mRNA binding
E193Q
-
mutation in active site, decrease in luteinizing hormone receptor mRNA binding
E193Q/D204N
-
significant decrease in luteinizing hormone receptor mRNA binding
E193Q/K13A
-
significant decrease in luteinizing hormone receptor mRNA binding
H20K
-
expressed in inclusion bodies that can be solubilized in 8 M urea, refolding to a soluble protein was unsuccessful indicating irreversible structural changes
H20L
-
no significant changes in secondary structure, increased Km for both substrates
H20Y
-
no significant changes in secondary structure, increased Km for both substrates
I196A
modest changes in Km and Ki values
I56A
4.5fold increase in Km value for ATP
K13A
-
mutation in active site, decrease in luteinizing hormone receptor mRNA binding
K13M
-
56fold decrease in activity
L53A
modest changes in Km and Ki values
R388X
modest changes in Km and Ki values
S146A
-
mutation in active site, decrease in luteinizing hormone receptor mRNA binding
S146A/E193Q
-
significant decrease in luteinizing hormone receptor mRNA binding
S314A
-
mutation outside the active site, no change in luteinizing hormone receptor mRNA binding
T104A
modest changes in Km and Ki values
T104A/I196A
39fold increase in Ki value
T104A/I196A/R388X
11fold increase in Km value for mevalonate
Y149A
8fold increase in Km value for mevalonate
I268T
markedly decreased mevalonate kinase activity when expressed in Escherichia coli
I268T
-
leads in homozygous state to mevalonic aciduria, inactive mevalonate kinase
additional information
-
mutations in the mevalonate kinase gene cause the hyperimmunoglobulin D syndrome, HIDS, an autosomal recessive autoinflammatory disease, phenotype
additional information
recombinant expression of the enzyme in HaCat human keratinocytes causes interference with the expression of other genes. The mRNA and protein expression levels of keratin 1 and involucrin are significantly decreased following interference of MVK expression, and the decrease is markedly attenuated by farnesyl diphosphate (FPP). Furthermore, the apoptotic rate is markedly increased following MVK interference, and the increase is significantly attenuated by geranylxadgeranyl diphosphate (GGPP). Overexpression of MVK significantly decreased the apoptotic rate of HaCat cells. The prenylation levels after MVK interference is notably decreased, which is markedly attenuated by GGPP. The overexpression of MVK significantly increased the prenylation levels of HaCat cells. FPP or GGPP reverse MVK interference-induced decrease in geranylgeranylation levels of lamin A, HRAS, KRAS, NRAS, Rho E, Rho B, Rho A, RAC1 and cdc42
additional information
-
recombinant expression of the enzyme in HaCat human keratinocytes causes interference with the expression of other genes. The mRNA and protein expression levels of keratin 1 and involucrin are significantly decreased following interference of MVK expression, and the decrease is markedly attenuated by farnesyl diphosphate (FPP). Furthermore, the apoptotic rate is markedly increased following MVK interference, and the increase is significantly attenuated by geranylxadgeranyl diphosphate (GGPP). Overexpression of MVK significantly decreased the apoptotic rate of HaCat cells. The prenylation levels after MVK interference is notably decreased, which is markedly attenuated by GGPP. The overexpression of MVK significantly increased the prenylation levels of HaCat cells. FPP or GGPP reverse MVK interference-induced decrease in geranylgeranylation levels of lamin A, HRAS, KRAS, NRAS, Rho E, Rho B, Rho A, RAC1 and cdc42
additional information
-
deletion of one mevalonate kinase allele yields viable mice with significantly reduced liver mevalonate kinase enzyme activity. Cholesterol levels in tissues and blood, and isoprene end-products ubiquinone and dolichol in tissues are normal in Mvk+/- mice. Mevalonate concentrations are increased in spleen, heart, and kidney yet normal in brain and liver. While the trend is for higher IgA levels in Mvk+/- sera, IgD levels are significantly increased and the animals show increased serum tumor necrosis factor-alpha levels
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Tchen, T.T.
Mevalonic kinase: purification and properties
J. Biol. Chem.
233
1100-1103
1958
Saccharomyces cerevisiae
brenda
Markley, K.; Smallan, E.
Mevalonic kinase in rabbit liver
Biochim. Biophys. Acta
47
327-335
1961
Oryctolagus cuniculus
-
brenda
Porter, J.W.
Mevalonate kinase
Methods Enzymol.
110
71-78
1985
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