Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(3R)-3-cyclopropyl-3-hydroxy-5-[[hydroxy(phosphonooxy)phosphoryl]oxy]pentanoic acid + ATP
?
-
-
-
-
?
(3R)-3-ethyl-3-hydroxy-5-[[hydroxy(phosphonooxy)phosphoryl]oxy]pentanoic acid + ATP
?
-
-
-
-
?
(3R)-3-hydroxy-3-(2-[[hydroxy(phosphonooxy)phosphoryl]oxy]ethyl)-4-methylpent-4-enoic acid + ATP
?
-
-
-
-
?
(3R)-3-hydroxy-3-(2-[[hydroxy(phosphonooxy)phosphoryl]oxy]ethyl)-4-methylpentanoic acid + ATP
?
-
-
-
-
?
(3R)-3-hydroxy-3-(2-[[hydroxy(phosphonooxy)phosphoryl]oxy]ethyl)-5-methylhexanoic acid + ATP
?
-
-
-
-
?
(3R)-3-hydroxy-3-(2-[[hydroxy(phosphonooxy)phosphoryl]oxy]ethyl)heptanoic acid + ATP
?
-
-
-
-
?
(3R)-3-hydroxy-3-(2-[[hydroxy(phosphonooxy)phosphoryl]oxy]ethyl)hex-4-ynoic acid + ATP
?
-
-
-
-
?
(3R)-3-hydroxy-3-(2-[[hydroxy(phosphonooxy)phosphoryl]oxy]ethyl)hex-5-enoic acid + ATP
?
-
-
-
-
?
(3R)-3-hydroxy-3-(2-[[hydroxy(phosphonooxy)phosphoryl]oxy]ethyl)pent-4-enoic acid + ATP
?
-
-
-
-
?
(3R)-3-hydroxy-3-(2-[[hydroxy(phosphonooxy)phosphoryl]oxy]ethyl)pent-4-ynoic acid + ATP
?
-
-
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
ATP + (R,S)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
ir
ATP + 3-hydroxy-3-methylbutyrate
ADP + isobutene + CO2
-
isobutene is identified by gas chromatography with flame ionization detection as well as by GC-mass spectrometry. Isobutene is an important commercial chemical used for the synthesis of butyl rubber, terephthalic acid, specialty chemicals, and a gasoline performance additive known as alkylate
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
CTP + 5-diphosphomevalonate
CDP + phosphate + isopentenyl diphosphate + CO2
dATP + 5-diphosphomevalonate
dADP + phosphate + isopentenyl diphosphate + CO2
-
about 59% of the activity with ATP
-
-
?
diphosphomevalonate + ATP
isopentenyl diphosphate + ADP
-
-
-
-
?
GTP + 5-diphosphomevalonate
GDP + phosphate + isopentenyl diphosphate + CO2
ITP + 5-diphosphomevalonate
IDP + phosphate + isopentenyl diphosphate + CO2
-
about 6% of the activity with ATP
-
-
?
UTP + 5-diphosphomevalonate
UDP + phosphate + isopentenyl diphosphate + CO2
-
13% of the activity with ATP
-
?
additional information
?
-
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
the enzyme is implicated in latex metabolism
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
the enzyme catalyzes a reaction of the classical mevalonate pathway
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
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
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
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
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
the enzyme catalyzes a reaction of the classical mevalonate pathway
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
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
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
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
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
the enzyme catalyzes a reaction of the classical mevalonate pathway
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
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
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
ir
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
high specificity for ATP
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
high specificity for ATP
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
high specificity for ATP
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
the enzyme may play a significant role in the coordinate regulation of the enzymes implied in cholesterol biosynthesis
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
the enzyme may play a significant role in the regulation of cholesterol synthesis in the small intestine
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
the enzyme is responsible for regulation of cholesterogenesis. Response to lipoprotein content of culture medium
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
enzyme activity is increased by 5fold after feeding young rats 2.5% cholestyramine for ten days to four weeks
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
enzyme catalyzes one of the early steps in the biosynthesis of cholesterol from mevalonic acid
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
CTP + 5-diphosphomevalonate
CDP + phosphate + isopentenyl diphosphate + CO2
-
about 10% of the activity with ATP
-
-
?
CTP + 5-diphosphomevalonate
CDP + phosphate + isopentenyl diphosphate + CO2
-
12% of the activity with ATP
-
?
CTP + 5-diphosphomevalonate
CDP + phosphate + isopentenyl diphosphate + CO2
-
no activity
-
-
?
GTP + 5-diphosphomevalonate
GDP + phosphate + isopentenyl diphosphate + CO2
-
about 15% of the activity with ATP
-
-
?
GTP + 5-diphosphomevalonate
GDP + phosphate + isopentenyl diphosphate + CO2
-
25% of the activity with ATP
-
?
GTP + 5-diphosphomevalonate
GDP + phosphate + isopentenyl diphosphate + CO2
-
about 10% of the activity with ATP
-
-
?
additional information
?
-
-
liver-specific induction of the enzyme by pravastatin
-
?
additional information
?
-
-
major enzyme involved in cholesterol biosynthesis in rat liver
-
?
additional information
?
-
-
the enzyme is involved in cholesterol biosynthesis
-
?
additional information
?
-
no substrate: mevalonate 5-phosphate
-
-
?
additional information
?
-
-
no substrate: mevalonate 5-phosphate
-
-
?
additional information
?
-
NMR analysis of the product
-
-
-
additional information
?
-
-
NMR analysis of the product
-
-
-
additional information
?
-
NMR analysis of the product
-
-
-
additional information
?
-
no substrate: mevalonate 5-phosphate
-
-
?
additional information
?
-
NMR analysis of the product
-
-
-
additional information
?
-
NMR analysis of the product
-
-
-
additional information
?
-
no substrate: mevalonate 5-phosphate
-
-
?
additional information
?
-
NMR analysis of the product
-
-
-
additional information
?
-
molecular dynamics simulation to characterize the active site of mevalonate 5-diphosphate decarboxylase to predict a probable mechanism in the transition state
-
-
?
additional information
?
-
-
molecular dynamics simulation to characterize the active site of mevalonate 5-diphosphate decarboxylase to predict a probable mechanism in the transition state
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
N17A
mutant exhibits a 15fold inflation in Km for 5-diphosphomevalonate
R161Q
mutant exhibits an about 1000fold diminution in specific activity, while binding the fluorescent substrate analog, TNP-ATP, comparably to wild type enzyme
S162A
mutant shows reduced activity with 2fold decrease in Vm and 4 to 7fold increases in substrate Km values
C210S
decrease in melting temperature by 12 degrees
D281N
site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity and 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
D281N
-
site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity and 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
-
C210S
-
decrease in melting temperature by 12 degrees
-
D281N
-
site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity and 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
-
D281N
-
site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity and 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
-
D281N
-
site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity and 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
-
D302A
1000fold decrease in kcat value, still retains ability to stoichiometrically bind nucleotide triphosphates at the active site
D302N
100000fold decrease in kcat value, still retains ability to stoichiometrically bind nucleotide triphosphates at the active site
K18M
30fold decrease in kcat value, still retains ability to stoichiometrically bind nucleotide triphosphates at the active site
R74H
mutant increases specific activity on non-native substrate (3-hydroxy-3-methylbutyrate) by 4.8fold
S120A
8fold diminution in kcat-value
S121A
42000fold diminution in kcat-value
S153A
18fold inflation in Kd-value for Mg-ATP, 35fold inflation in Km-value for Mg-ATP
S155A
26fold inflation in Km-value for Mg-ATP, 16fold inflation in Km-value for diphosphomevalonate
S36A
limited solubility, impaired binding of fluorescent ATP analogue trinitrophenyl-ATP
R193T
modest effects on kinetics
W153F
modest effects on kinetics
W19F
130fold increase in Km for (R)-5-diphosphomevalonate, 10fold increase in Km for ATP
L79P
-
mutation drastically impairs the oligomerization of the protein
L79P
molecular dynamics simutation of the mutated enzyme, it is suggested that the temperature sensitive mutant phenotype of Saccharomyces cerevisiae is a result of a significant conformational change associates with the Leu 79 to Pro mutation
D283A
catalytically deficient enzyme with 100000fold decreased kcat value
D283A
10000fold decrease in kcat value
S192A
the mutation decreases kcat by about 1000fold
S192A
catalytically deficient enzyme with 1000fold decreased kcat value
S192A
1000fold decrease in kcat value
additional information
the DMD activity, which yields IPP from MVA-5-PP in the presence of ATP, is observed only with the wild type and with the D281N mutant
additional information
-
the DMD activity, which yields IPP from MVA-5-PP in the presence of ATP, is observed only with the wild type and with the D281N mutant
additional information
-
the DMD activity, which yields IPP from MVA-5-PP in the presence of ATP, is observed only with the wild type and with the D281N mutant
-
additional information
-
the DMD activity, which yields IPP from MVA-5-PP in the presence of ATP, is observed only with the wild type and with the D281N mutant
-
additional information
-
the DMD activity, which yields IPP from MVA-5-PP in the presence of ATP, is observed only with the wild type and with the D281N mutant
-
additional information
-
the DMD activity, which yields IPP from MVA-5-PP in the presence of ATP, is observed only with the wild type and with the D281N mutant
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Alvear, M.; Jabalquinto, A.M.; Eyzaguirre, J.; Cardemil, E.
Purification and characterization of avian liver mevalonate-5-pyrophosphate decarboxylase
Biochemistry
21
4646-4650
1982
Gallus gallus
brenda
Cardemil, E.; Jabalquinto, A.M.
The mechanism of action of mevalonate-5-pyrophosphate decarboxylase
Trends Biochem. Sci.
8
7
1983
Saccharomyces cerevisiae
-
brenda
Jabalquinto, A.M.; Eyzaguirre, J.; Cardemil, E.
Evidence of essential arginyl residues in chicken liver mevalonate-5-pyrophosphate decarboxylase
Arch. Biochem. Biophys.
225
338-343
1983
Gallus gallus
brenda
Gonzalez-Pacanowska, D.; Marco, C.; Garcia-Martinez, J.; Garcia-Peregrin, E.
Role of mevalonate-5-pyrophosphate decarboxylase in the regulation of chick intestinal cholesterogenesis
Biochim. Biophys. Acta
833
449-455
1985
Gallus gallus
brenda
Cardemil, E.; Jabalquinto, A.M.
Mevalonate 5-pyrophosphate decarboxylase from chicken liver
Methods Enzymol.
110
86-92
1985
Gallus gallus
brenda
Jabalquinto, A.M.; Cardemil, E.
The effect of diabetes, nutritional factors, and sex on rat liver and kidney mevalonate kinase, mevalonate-5-phosphate kinase, and mevalonate-5-pyrophosphate decarboxylase
Arch. Biochem. Biophys.
210
132-139
1981
Rattus norvegicus
brenda
Lalitha, R.; George, R.; Ramasarma, T.
Mevalonate decarboxylation in lemon grass leaves
Phytochemistry
24
2569-2571
1985
Arachis hypogaea, Cymbopogon citratus, Oryza sativa, Vigna radiata, Pisum sativum
-
brenda
Chiew, Y.E.; O'Sullivan, W.J.; Lee, Ch.S.
Studies on pig liver mevalonate-5-diphosphate decarboxylase
Biochim. Biophys. Acta
916
271-278
1987
Sus scrofa
brenda
Jabalquinto, A.M.; Cardemil, E.
Kinetic effect of ATP, divalent metal ions and pH on chicken liver mevalonate 5-diphosphate decarboxylase
Biochim. Biophys. Acta
916
172-178
1987
Gallus gallus
brenda
Iyengar, R.; Cardemil, E.; Frey, P.A.
Mevalonate-5-diphosphate decarboxylase: stereochemical course of ATP-dependent phosphorylation of mevalonate 5-diphosphate
Biochemistry
25
4693-4698
1986
Gallus gallus
brenda
Gonzalez-Pacanowska, D.; Marco, C.; Garcia-Martinez, J.; Garcia-Peregrin, E.
Effects of different nutritional conditions on chick liver mevalonate-activating enzymes
Biochim. Biophys. Acta
875
605-609
1986
Gallus gallus
brenda
Nunez, A.; Castillo, M.; Iglesias, J.; Martinez-Cayuela, M.; Gonzales-Pacanowska, D.; Garcia-Peregrin, E.
Regulation of mevalonate 5-pyrophosphate decarboxylase in HeLa cells. Inhibition of enzymatic protein synthesis by serum lipoproteins
Int. J. Biochem. Cell Biol.
29
1037-1041
1997
Homo sapiens
brenda
Toth, M.J.; Huwyler, L.; Park, J.
Purification of rat liver mevalonate pyrophosphate decarboxylase
Prep. Biochem. Biotechnol.
26
47-51
1996
Rattus norvegicus
brenda
Michihara, A.; Sawamura, M.; Nara, Y.; Ikeda, K.; Yamori, Y.
Purification and characterization of two mevalonate pyrophosphate decarboxylases from rat liver: a novel molecular species of 37 kDa
J. Biochem.
122
647-654
1997
Rattus norvegicus
brenda
Alvear, M.; Jabalquinto, A.M.; Cardemil, E.
Inactivation of chicken liver mevalonate 5-diphosphate decarboxylase by sulfhydryl-directed reagents: evidence of a functional dithiol
Biochim. Biophys. Acta
994
7-11
1989
Gallus gallus
brenda
Jabalquinto, A.M.; Cardemil, E.
Substrate binding order in mevalonate 5-diphosphate decarboxylase from chicken liver
Biochim. Biophys. Acta
996
257-259
1989
Gallus gallus
brenda
Hulcher, F.H.
Modification of the radiochemical assay of rat liver mevalonate-5-diphosphate decarboxylase and induction and stabilization of the activity
Biochem. Biophys. Res. Commun.
181
1449-1455
1991
Rattus norvegicus
brenda
Sawamura, M.; Nara, Y.; Yamori, Y.
Liver mevalonate 5-pyrophosphate decarboxylase is responsible for reduced serum cholesterol in stroke-prone spontaneously hypertensive rat
J. Biol. Chem.
267
6051-6055
1992
Rattus norvegicus
brenda
Iglesias, J.; Gonzalez-Pacanowska, D.; Marco, C.; Garcia-Peregrin, E.
Regulation of mevalonate 5-pyrophosphate decarboxylase in isolated cells from chick intestinal epithelium
Biochem. J.
260
333-337
1989
Gallus gallus
brenda
Michihara, A.; Akasaki, K.; Yamori, Y.; Tsuji, H.
Tissue distribution of a major mevalonate pyrophosphate decarboxylase in rats
Biol. Pharm. Bull.
24
1231-1234
2001
Rattus norvegicus
brenda
Michihara, A.; Sawamura, M.; Yamori, Y.; Akasaki, K.; Tsuji, H.
Mevalonate pyrophosphate decarboxylase is predominantly located in the cytosol of rat hepatocytes
Biol. Pharm. Bull.
24
1235-1240
2001
Rattus norvegicus
brenda
Michihara, A.; Sawamura, M.; Yamori, Y.; Akasaki, K.; Tsuji, H.
Difference in subcellular distribution between 45- and 37-kDa mevalonate pyrophosphate decarboxylase in rat liver
Biol. Pharm. Bull.
24
1347-1350
2001
Rattus norvegicus
brenda
Michihara, A.; Akasaki, K.; Yamori, Y.; Tsuji, H.
Purification and characterization of mouse mevalonate pyrophosphate decarboxylase
Biol. Pharm. Bull.
25
302-306
2002
Mus musculus
brenda
Michihara, A.; Akasaki, K.; Yamori, Y.; Tsuji, H.
Change in the protein level of mevalonate pyrophosphate decarboxylase in tissues of mouse by pravastatin
Biol. Pharm. Bull.
26
1082-1085
2003
Mus musculus
brenda
Michihara, A.; Sawamura, M.; Yamori, Y.; Akasaki, K.; Tsuji, H.
Probucol decreases mevalonate pyrophosphate decarboxylase in the rat liver
Biol. Pharm. Bull.
26
1484-1486
2003
Rattus norvegicus
brenda
Michihara, A.; Akasaki, K.; Yamori, Y.; Tsuji, H.
Subcellular distribution of mouse mevalonate pyrophosphate decarboxylase
Biol. Pharm. Bull.
26
579-584
2003
Mus musculus
brenda
Cordier, H.; Lacombe, C.; Karst, F.; Berges, T.
The Saccharomyces cerevisiae mevalonate diphosphate decarboxylase (erg19p) forms homodimers in vivo, and a single substitution in a structurally conserved region impairs dimerization
Curr. Microbiol.
38
290-294
1999
Saccharomyces cerevisiae
brenda
Hogenboom, S.; Tuyp, J.J.M.; Espeel, M.; Koster, J.; Wanders, R.J.A.; Waterham, H.R.
Human mevalonate pyrophosphate decarboxylase is localized in the cytosol
Mol. Genet. Metab.
81
216-224
2004
Homo sapiens
brenda
Cordier, H.; Karst, F.; Berges, T.
Heterologous expression in Saccharomyces cerevisiae of an Arabidopsis thaliana cDNA encoding mevalonate diphosphate decarboxylase
Plant Mol. Biol.
39
953-967
1999
Arabidopsis thaliana (O23722), Arabidopsis thaliana
brenda
Byres, E.; Martin, D.M.A.; Hunter, W.N.
A preliminary crystallographic analysis of the putative mevalonate diphosphate decarboxylase from Trypanosoma brucei
Acta Crystallogr. Sect. F
F61
581-584
2005
Trypanosoma brucei
brenda
Krepkiy, D.V.; Miziorko, H.M.
Investigation of the functional contributions of invariant serine residues in yeast mevalonate diphosphate decarboxylase
Biochemistry
44
2671-2677
2005
Saccharomyces cerevisiae (P32377), Saccharomyces cerevisiae
brenda
Krepkiy, D.; Miziorko, H.M.
Identification of active site residues in mevalonate diphosphate decarboxylase: implications for a family of phosphotransferases
Protein Sci.
13
1875-1881
2004
Saccharomyces cerevisiae (P32377)
brenda
Qiu, Y.; Li, D.
Bifunctional inhibitors of mevalonate kinase and mevalonate 5-diphosphate decarboxylase
Org. Lett.
8
1013-1016
2006
Rattus norvegicus
brenda
Qiu, Y.; Li, D.
Inhibition of mevalonate 5-diphosphate decarboxylase by fluorinated substrate analogs
Biochim. Biophys. Acta
1760
1080-1087
2006
Rattus norvegicus
brenda
Qiu, Y.; Gao, J.; Guo, F.; Qiao, Y.; Li, D.
Mutation and inhibition studies of mevalonate 5-diphosphate decarboxylase
Bioorg. Med. Chem. Lett.
17
6164-6168
2007
Rattus norvegicus
brenda
Byres, E.; Alphey, M.S.; Smith, T.K.; Hunter, W.N.
Crystal structures of Trypanosoma brucei and Staphylococcus aureus mevalonate diphosphate decarboxylase inform on the determinants of specificity and reactivity
J. Mol. Biol.
371
540-553
2007
Staphylococcus aureus (A0A0H2XIV6), Staphylococcus aureus, Saccharomyces cerevisiae (P32377), Saccharomyces cerevisiae, Trypanosoma brucei (Q388P2), Trypanosoma brucei
brenda
Pang, Y.; Shen, G.; Berges, T.; Cardier, H.; Wu, W.; Sun, X.; Tang, K.
Molecular cloning, characterization and heterologous expression in Saccharomyces cerevisiae of a mevalonate diphosphate decarboxylase cDNA from Ginkgo biloba
Physiol. Plant.
127
19-27
2006
Ginkgo biloba (Q5UCT8)
brenda
Wang, Y.; Muneton, S.; Sjoevall, J.; Jovanovic, J.N.; Griffiths, W.J.
The effect of 24S-hydroxycholesterol on cholesterol homeostasis in neurons: quantitative changes to the cortical neuron proteome
J. Proteome Res.
7
1606-1614
2008
Rattus norvegicus
brenda
Voynova, N.E.; Fu, Z.; Battaile, K.P.; Herdendorf, T.J.; Kim, J.J.; Miziorko, H.M.
Human mevalonate diphosphate decarboxylase: characterization, investigation of the mevalonate diphosphate binding site, and crystal structure
Arch. Biochem. Biophys.
480
58-67
2008
Homo sapiens (P53602), Homo sapiens
brenda
Michihara, A.; Morita, S.; Toda, K.; Akasaki, K.; Tsuji, H.
Mevalonate pyrophosphate decarboxylase is predominantly located in the cytosol of both B16 and B16F10 cells in mouse melanoma treated with lovastatin
J. Health Sci.
54
216-223
2008
Mus musculus
-
brenda
Shimatani, M.; Michihara, A.; Akasaki, K.
Tissue distribution of mevalonate pyrophosphate decarboxylase in guinea pig
Biol. Pharm. Bull.
32
1476-1479
2009
Cavia porcellus
brenda
Ren, A.; Qin, L.; Shi, L.; Dong, X.; Mu, D.S.; Li, Y.X.; Zhao, M.W.
Methyl jasmonate induces ganoderic acid biosynthesis in the basidiomycetous fungus Ganoderma lucidum
Biores. Technol.
101
6785-6790
2010
Ganoderma lucidum, Ganoderma lucidum HG
brenda
Lefurgy, S.T.; Rodriguez, S.B.; Park, C.S.; Cahill, S.; Silverman, R.B.; Leyh, T.S.
Probing ligand-binding pockets of the mevalonate pathway enzymes from Streptococcus pneumoniae
J. Biol. Chem.
285
20654-20663
2010
Streptococcus pneumoniae
brenda
Weerasinghe, S.; Samantha Dassanayake, R.
Simulation of structural and functional properties of mevalonate diphosphate decarboxylase (MVD)
J. Mol. Model.
16
489-498
2010
Saccharomyces cerevisiae (P32377), Saccharomyces cerevisiae
brenda
Rothwell, C.; Lebreton, A.; Young Ng, C.; Lim, J.Y.; Liu, W.; Vasudevan, S.; Labow, M.; Gu, F.; Gaither, L.A.
Cholesterol biosynthesis modulation regulates dengue viral replication
Virology
389
8-19
2009
Homo sapiens
brenda
Gogerty, D.S.; Bobik, T.A.
Formation of isobutene from 3-hydroxy-3-methylbutyrate by diphosphomevalonate decarboxylase
Appl. Environ. Microbiol.
76
85004-8010
2010
Saccharomyces cerevisiae (P32377), Saccharomyces cerevisiae
brenda
Reuther, G.; Harris, R.; Girvin, M.; Leyh, T.S.
Backbone 1H, 13C, 15N NMR assignments of the unliganded and substrate ternary complex forms of mevalonate diphosphate decarboxylase from Streptococcus pneumoniae
Biomol. NMR Assign.
5
11-14
2011
Streptococcus pneumoniae
brenda
Barta, M.L.; Skaff, D.A.; McWhorter, W.J.; Herdendorf, T.J.; Miziorko, H.M.; Geisbrecht, B.V.
Crystal structures of Staphylococcus epidermidis mevalonate diphosphate decarboxylase bound to inhibitory analogs reveal new insight into substrate binding and catalysis
J. Biol. Chem.
286
23900-23910
2011
Staphylococcus epidermidis (Q9FD73), Staphylococcus epidermidis
brenda
Michihara, A.; Shimatani, M.; Akasaki, K.
Comparison of the gene expression levels of mevalonate pyrophosphate decarboxylase between stroke-prone spontaneously hypertensive and Wistar Kyoto rats
J. Health Sci.
56
733-737
2010
Rattus norvegicus (Q62967)
-
brenda
Nishimura, H.; Azami, Y.; Miyagawa, M.; Hashimoto, C.; Yoshimura, T.; Hemmi, H.
Biochemical evidence supporting the presence of the classical mevalonate pathway in the thermoacidophilic archaeon Sulfolobus solfataricus
J. Biochem.
153
415-420
2013
Saccharolobus solfataricus (Q97UL5), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q97UL5), Saccharolobus solfataricus DSM 1617 (Q97UL5)
brenda
Barta, M.L.; McWhorter, W.J.; Miziorko, H.M.; Geisbrecht, B.V.
Structural basis for nucleotide binding and reaction catalysis in mevalonate diphosphate decarboxylase
Biochemistry
51
5611-5621
2012
Staphylococcus epidermidis (Q9FD73), Staphylococcus epidermidis
brenda
Vannice, J.C.; Skaff, D.A.; Keightley, A.; Addo, J.K.; Wyckoff, G.J.; Miziorko, H.M.
Identification in Haloferax volcanii of phosphomevalonate decarboxylase and isopentenyl phosphate kinase as catalysts of the terminal enzyme reactions in an archaeal alternate mevalonate pathway
J. Bacteriol.
196
1055-1063
2014
Haloferax volcanii
brenda
Shi, L.; Qin, L.; Xu, Y.; Ren, A.; Fang, X.; Mu, D.; Tan, Q.; Zhao, M.
Molecular cloning, characterization, and function analysis of a mevalonate pyrophosphate decarboxylase gene from Ganoderma lucidum
Mol. Biol. Rep.
39
6149-6159
2012
Ganoderma lucidum (G9BIY1), Ganoderma lucidum, Ganoderma lucidum HG (G9BIY1)
brenda
Simkin, A.J.; Guirimand, G.; Papon, N.; Courdavault, V.; Thabet, I.; Ginis, O.; Bouzid, S.; Giglioli-Guivarch, N.; Clastre, M.
Peroxisomal localisation of the final steps of the mevalonic acid pathway in planta
Planta
234
903-914
2011
Catharanthus roseus (F6K7K1), Catharanthus roseus
brenda
Hattori, A.; Unno, H.; Goda, S.; Motoyama, K.; Yoshimura, T.; Hemmi, H.
In vivo formation of the protein disulfide bond that enhances the thermostability of diphosphomevalonate decarboxylase, an intracellular enzyme from the hyperthermophilic archaeon Sulfolobus solfataricus
J. Bacteriol.
197
3463-3471
2015
Saccharolobus solfataricus (Q97UL5), Saccharolobus solfataricus, Saccharolobus solfataricus DSM 1617 (Q97UL5)
brenda
Kim, Y.K.; Kim, Y.B.; Uddin, M.R.; Lee, S.; Kim, S.U.; Park, S.U.
Enhanced triterpene accumulation in Panax ginseng hairy roots overexpressing mevalonate-5-pyrophosphate decarboxylase and farnesyl pyrophosphate synthase
ACS Synth. Biol.
3
773-779
2014
Panax ginseng (F8QQQ7), Panax ginseng
brenda
Skaff, D.A.; McWhorter, W.J.; Geisbrecht, B.V.; Wyckoff, G.J.; Miziorko, H.M.
Inhibition of bacterial (R)-5-diphosphomevalonate decarboxylase by eriochrome compounds
Arch. Biochem. Biophys.
566
1-6
2015
Staphylococcus epidermidis (Q9FD73), Staphylococcus epidermidis
brenda
Hayakawa, H.; Sobue, F.; Motoyama, K.; Yoshimura, T.; Hemmi, H.
Identification of enzymes involved in the mevalonate pathway of Flavobacterium johnsoniae
Biochem. Biophys. Res. Commun.
487
702-708
2017
Flavobacterium johnsoniae
brenda
Michihara, A.; Ide, N.; Mizutani, Y.; Okamoto, M.; Uchida, M.; Matsuoka, H.; Akasaki, K.
Involvement of microRNA214 and transcriptional regulation in reductions in mevalonate pyrophosphate decarboxylase mRNA levels in stroke-prone spontaneously hypertensive rat livers
Biosci. Biotechnol. Biochem.
79
1759-1770
2015
Rattus norvegicus (Q62967)
brenda
Chai, J.; Wang, D.; Peng, Y.; Zhao, X.; Zhang, Q.; Li, P.; Fang, X.; Wang, M.; Cai, X.
Molecular cloning, expression and immunolocalization analysis of diphosphomevalonate decarboxylase involved in terpenoid biosynthesis from Euphorbia helioscopia L.
Biotechnol. Biotechnol. Equip.
31
1106-1115
2017
Euphorbia helioscopia (A0A0M4FQ19)
-
brenda
Abbassi, S.J.; Vishwakarma, R.K.; Patel, P.; Kumari, U.; Khan, B.M.
Bacopa monniera recombinant mevalonate diphosphate decarboxylase Biochemical characterization
Int. J. Biol. Macromol.
79
661-668
2015
Bacopa monnieri (A0A0F6WBJ2), Bacopa monnieri
brenda
Abbassi, S.; Patel, K.; Khan, B.; Bhosale, S.; Gaikwad, S.
Functional and conformational transitions of mevalonate diphosphate decarboxylase from Bacopa monniera
Int. J. Biol. Macromol.
83
160-170
2016
Bacopa monnieri (A0A0F6WBJ2), Bacopa monnieri
brenda
Addo, J.; Skaff, D.; Miziorko, H.
Active site binding modes of inhibitors of Staphylococcus aureus mevalonate diphosphate decarboxylase from docking and molecular dynamics simulations
J. Mol. Model.
22
1-18
2016
Staphylococcus aureus
-
brenda
Wu, C.; Li, Y.; Nie, Z.; Dai, L.; Kang, G.; Zeng, R.
Molecular cloning and expression analysis of the mevalonate diphosphate decarboxylase gene from the latex of Hevea brasiliensis
Tree Genet. Genomes
13
22
2017
Hevea brasiliensis (A0A0H3WJ12)
-
brenda
Wu, C.; Lan, L.; Li, Y.; Nie, Z.; Zeng, R.
The relationship between latex metabolism gene expression with rubber yield and related traits in Hevea brasiliensis
BMC Genomics
19
897
2018
Hevea brasiliensis (A9ZN03), Hevea brasiliensis
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 (Q97UL5), Saccharolobus solfataricus, Saccharolobus solfataricus ATCC 35092 (Q97UL5), Saccharolobus solfataricus DSM 1617 (Q97UL5), Saccharolobus solfataricus JCM 11322 (Q97UL5), Saccharolobus solfataricus P2 (Q97UL5)
brenda