Information on EC 4.1.1.33 - Diphosphomevalonate decarboxylase

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The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria

EC NUMBER
COMMENTARY
4.1.1.33
-
RECOMMENDED NAME
GeneOntology No.
Diphosphomevalonate decarboxylase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + (R)-5-diphosphomevalonate = ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
-
ATP + (R)-5-diphosphomevalonate = ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
mechanism
-
ATP + (R)-5-diphosphomevalonate = ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
sequential mechanism
-
ATP + (R)-5-diphosphomevalonate = ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
thiophosphoryl group transfer proceeds with inversion of configuration at phosphorus
-
ATP + (R)-5-diphosphomevalonate = ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
ordered sequential mechanism with mevalonate 5-diphosphate as the first substrate to bind to the enzyme
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
isoprene biosynthesis II (engineered)
-
-
mevalonate pathway I
-
-
mevalonate metabolism
-
-
Terpenoid backbone biosynthesis
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
Biosynthesis of antibiotics
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:(R)-5-diphosphomevalonate carboxy-lyase (adding ATP; isopentenyl-diphosphate-forming)
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5-Pyrophosphomevalonate decarboxylase
-
-
-
-
Decarboxylase, pyrophosphomevalonate
-
-
-
-
diphosphomevalonate decarboxylase
-
diphosphomevalonate decarboxylase
-
-
Mevalonate (diphospho)decarboxylase
-
-
-
-
mevalonate 5'-diphosphate decarboxylase
-
-
Mevalonate 5-diphosphate decarboxylase
-
-
-
-
Mevalonate 5-diphosphate decarboxylase
-
Mevalonate 5-diphosphate decarboxylase
-
-
Mevalonate 5-diphosphate decarboxylase
-
mevalonate diphosphate decarboxylase
-
mevalonate diphosphate decarboxylase
-
mevalonate diphosphate decarboxylase
-
-
mevalonate diphosphate decarboxylase
-
-
mevalonate diphosphate decarboxylase
-
mevalonate diphosphate decarboxylase
-
-
mevalonate diphosphate decarboxylase
-
-
mevalonate diphospho decarboxylase
-
-
Mevalonate pyrophosphate decarboxylase
-
-
-
-
Mevalonate pyrophosphate decarboxylase
-
-
Mevalonate pyrophosphate decarboxylase
-
Mevalonate pyrophosphate decarboxylase
Ganoderma lucidum HG
-
-
Mevalonate pyrophosphate decarboxylase
-
-
Mevalonate pyrophosphate decarboxylase
-
mevalonate pyrophosphate decraboxylase
-
-
Mevalonate-5-pyrophosphate decarboxylase
-
-
-
-
Mevalonate-5-pyrophosphate decarboxylase
-
-
Mevalonate-5-pyrophosphate decarboxylase
Ganoderma lucidum HG
-
-
-
Mevalonate-5-pyrophosphate decarboxylase
-
-
MVD
Ganoderma lucidum HG
gene name
-
phosphomevalonate decarboxylase
-
-
Pyrophosphomevalonate decarboxylase
-
-
-
-
Pyrophosphomevalonic acid decarboxylase
-
-
-
-
ScMDD1
improved mutant I145F
ScMDD2
improved mutant R74H
SSO2989
locus name
-
CAS REGISTRY NUMBER
COMMENTARY
9024-66-2
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
the enzyme catalyzes a reaction of the classical mevalonate pathway
metabolism
-
the enzyme catalyzes a reaction of the classical mevalonate pathway
-
physiological function
-
investigation of the role of mevalonate diphospho decarboxylase in viral replication
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(3R)-3-cyclopropyl-3-hydroxy-5-[[hydroxy(phosphonooxy)phosphoryl]oxy]pentanoic acid + ATP
?
show the reaction diagram
-
-
-
-
?
(3R)-3-ethyl-3-hydroxy-5-[[hydroxy(phosphonooxy)phosphoryl]oxy]pentanoic acid + ATP
?
show the reaction diagram
-
-
-
-
?
(3R)-3-hydroxy-3-(2-[[hydroxy(phosphonooxy)phosphoryl]oxy]ethyl)-4-methylpent-4-enoic acid + ATP
?
show the reaction diagram
-
-
-
-
?
(3R)-3-hydroxy-3-(2-[[hydroxy(phosphonooxy)phosphoryl]oxy]ethyl)-4-methylpentanoic acid + ATP
?
show the reaction diagram
-
-
-
-
?
(3R)-3-hydroxy-3-(2-[[hydroxy(phosphonooxy)phosphoryl]oxy]ethyl)-5-methylhexanoic acid + ATP
?
show the reaction diagram
-
-
-
-
?
(3R)-3-hydroxy-3-(2-[[hydroxy(phosphonooxy)phosphoryl]oxy]ethyl)heptanoic acid + ATP
?
show the reaction diagram
-
-
-
-
?
(3R)-3-hydroxy-3-(2-[[hydroxy(phosphonooxy)phosphoryl]oxy]ethyl)hex-4-ynoic acid + ATP
?
show the reaction diagram
-
-
-
-
?
(3R)-3-hydroxy-3-(2-[[hydroxy(phosphonooxy)phosphoryl]oxy]ethyl)hex-5-enoic acid + ATP
?
show the reaction diagram
-
-
-
-
?
(3R)-3-hydroxy-3-(2-[[hydroxy(phosphonooxy)phosphoryl]oxy]ethyl)pent-4-enoic acid + ATP
?
show the reaction diagram
-
-
-
-
?
(3R)-3-hydroxy-3-(2-[[hydroxy(phosphonooxy)phosphoryl]oxy]ethyl)pent-4-ynoic acid + ATP
?
show the reaction diagram
-
-
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
ir
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
the enzyme catalyzes a reaction of the classical mevalonate pathway
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
Ganoderma lucidum HG
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
the enzyme catalyzes a reaction of the classical mevalonate pathway
-
?
ATP + (R,S)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
ir
ATP + 3-hydroxy-3-methylbutyrate
ADP + isobutene + CO2
show the reaction diagram
-
-
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
show the reaction diagram
-
-
-
-
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
-
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
-
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
-
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
-
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
-
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
-
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
-
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
Q2FJ52
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
-
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
-
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
-
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
-
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
-
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
-
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
-
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
-
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
-
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
-
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
-
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
high specificity for ATP
-
-
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
high specificity for ATP
-
-
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
high specificity for ATP
-
-
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
the enzyme is responsible for regulation of cholesterogenesis. Response to lipoprotein content of culture medium
-
-
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
enzyme catalyzes one of the early steps in the biosynthesis of cholesterol from mevalonic acid
-
-
CTP + 5-diphosphomevalonate
CDP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
no activity
-
-
CTP + 5-diphosphomevalonate
CDP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
about 10% of the activity with ATP
-
-
CTP + 5-diphosphomevalonate
CDP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
12% of the activity with ATP
-
?
dATP + 5-diphosphomevalonate
dADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
about 59% of the activity with ATP
-
-
diphosphomevalonate + ATP
isopentenyl diphosphate + ADP
show the reaction diagram
-
-
-
?
GTP + 5-diphosphomevalonate
GDP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
about 15% of the activity with ATP
-
-
GTP + 5-diphosphomevalonate
GDP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
about 10% of the activity with ATP
-
-
GTP + 5-diphosphomevalonate
GDP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
25% of the activity with ATP
-
?
UTP + 5-diphosphomevalonate
UDP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
13% of the activity with ATP
-
?
ITP + 5-diphosphomevalonate
IDP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
about 6% 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
?
-
-
molecular dynamics simulation to characterize the active site of mevalonate 5-diphosphate decarboxylase to predict a probable mechanism in the transition state
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
ir
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
G9BIY1
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
F6K7K1
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
Q97UL5
the enzyme catalyzes a reaction of the classical mevalonate pathway
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
Ganoderma lucidum HG
G9BIY1
-
-
?
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
Q97UL5
the enzyme catalyzes a reaction of the classical mevalonate pathway
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
-
-
?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
the enzyme is responsible for regulation of cholesterogenesis. Response to lipoprotein content of culture medium
-
-
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
enzyme catalyzes one of the early steps in the biosynthesis of cholesterol from mevalonic acid
-
-
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
1 mM ATP4- above that complexed at the substrate. MgATP2- decreases the Km from 0.45 mM to 0.15 mM
ATP
-
activates
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
-
4 mM, activates at 17% of the activity of Mg2+
Ca2+
-
4 mM, activates at 44% of the activity of Mg2+
Cd2+
-
MgCd2, activates at 37% of the activity of Mn2+
Co2+
-
4 mM, activates at 13% of the activity of Mg2+
Co2+
-
divalent metal ion required, Mg2+, Mn2+ or Co2+; Mn2+ and Co2+ are the best activators for the 45000 MW enzyme form
Co2+
-
divalent metal ion required, Mg2+ can be substituted by Mn2+ or Co2+
Mg2+
-
divalent cation required, Mg2+ is most effective, maximal activity at 1 mM
Mg2+
-
divalent cation required, Mg2+ and Mn2+ being most effective
Mg2+
-
required
Mg2+
-
4 mM, activates
Mg2+
-
MgATP2-, activates at 14% of the activity with Mn2+
Mg2+
-
divalent metal ion required, Mg2+, Mn2+ or Co2+
Mg2+
-
divalent metal ion required, Mg2+ can be substituted by Mn2+ or Co2+
Mg2+
20 mM, required for activity
Mg2+
-
required, bound to ATP
Mn2+
-
divalent cation required, Mg2+ and Mn2+ being most effective
Mn2+
-
can partially replace Mg2+
Mn2+
-
4 mM, activates at 37% of the activity of Mg2+
Mn2+
-
MnATP2-, best activator
Mn2+
-
divalent metal ion required, Mg2+, Mn2+ or Co2+; Mn2+ and Co2+ are the best activators for the 45000 MW enzyme form; Mn2+ is the best activator for the 37000 MW enzyme form
Mn2+
-
divalent metal ion required, Mg2+ can be substituted by Mn2+ or Co2+
Ni2+
-
4 mM, activates at 20% of the activity of Mg2+
Sr2+
-
4 mM, activates at 22% of the activity of Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2E)-3,7-dimethylocta-2,6-dien-1-yl 2-(4-hydroxy-4-methyl-6-oxotetrahydro-2H-pyran-2-yl)ethyl diphosphate
-
-
(2E)-3,7-dimethylocta-2,6-dien-1-yl 4-(4-hydroxy-4-methyl-6-oxotetrahydro-2H-pyran-2-yl)butyl diphosphate
-
-
(R)-6-fluoromevalonate diphosphate
-
-
(R,S)-diphosphoglycolyl proline
-
competitive inhibitor
1-(diphosphenyloxy)-3,4-dimethylpentan-3-ol
-
-
1-(diphosphenyloxy)-3-methylpentan-3-ol
-
-
1-(diphosphenyloxy)-5-fluoro-3-methylpentan-3-ol
-
-
2,2-difluoromevalonate 5-diphosphate
-
-
2-fluoromevalonate 5-diphosphate
-
irreversible inhibitor
24S-hydroxycholesterol
-
down-regulates the expression
3-ethyl-2-fluoro-3,5-dihydroxy-pentanate 5-diphosphate
-
-
4-(diphosphenyloxy)-2-methylbutan-2-ol
-
-
4-(diphosphenyloxy)-2-phenylbutan-2-ol
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
presence of substrate ATP or mevalonate 5-diphosphate protects effectively against inactivation
6-fluoromevalonate 5-diphosphate
competitive inhibitor with respect to 5-diphosphomevalonate
6-fluoromevalonate diphosphate
-
competitive
-
6-fluoromevalonate diphosphate
-
negligible inhibition
-
6-fluoromevalonate monophosphate
-
strong inhibition
-
adenosine 5'-O-(3-thiotriphosphate)
-
-
arsenite-2,3-dimercapto-1-propanol
-
-
citrate
-
inhibits below pH 4.8
citrate
-
-
Diamide
-
-
diphosphoglycolyl proline
competitive inhibitor with respect to 5-diphosphomevalonate
diphosphoglycolyl-L-proline
-
competitive
-
diphosphoglycolylproline
-
-
DTNB
-
10 mM, 60% inhibition
ferulate
-
-
geranyl diphosphate
-
-
iodoacetic acid
-
10 mM, 15% inhibition
methylmethanethiosulfonate
-
presence of substrate ATP or mevalonate 5-diphosphate protects effectively against inactivation
mevalonate
-
mixed inhibition
mevalonate 5-phosphate
-
mixed inhibition
MgADP-
-
-
NEM
-
10 mM, 40% inhibition
P'-geranyl 2-fluoromevalonate 5-diphosphate
-
irreversible inhibitor
P'-geranyl 3,5,8-trihydroxy-3-methyloctanate 8-diphosphate
-
-
p-chloromercuribenzene sulfonic acid
-
10 mM, 50% inhibition
p-coumarate
-
-
Phenylarsine oxide
-
-
Phenylglyoxal
-
inactivation follows pseudo-first-order kinetics
Phloroglucinol carboxylic acid
-
-
phosphate
-
-
Phthalate
-
-
protocatechuate
-
-
Resorcyclic acid
-
-
-
triflouromevalonate diposphate
-
molecular dynamics simulation for the inhibitor bound complex
Zn2+
-
-
Mn2+
-
-
additional information
-
probucol decreases mevalonate pyrophosphate decarboxylase in the rat liver
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
required
additional information
-
no requirement for SH-containing reagents for activity
-
additional information
-
the enzyme posseses a functional dithiol that is important for substrate binding
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.001
(3R)-3-cyclopropyl-3-hydroxy-5-[[hydroxy(phosphonooxy)phosphoryl]oxy]pentanoic acid
-
-
0.0015
(3R)-3-ethyl-3-hydroxy-5-[[hydroxy(phosphonooxy)phosphoryl]oxy]pentanoic acid
-
-
0.016
(3R)-3-hydroxy-3-(2-[[hydroxy(phosphonooxy)phosphoryl]oxy]ethyl)-4-methylpentanoic acid
-
-
0.029
(3R)-3-hydroxy-3-(2-[[hydroxy(phosphonooxy)phosphoryl]oxy]ethyl)-5-methylhexanoic acid
-
-
0.0063
(3R)-3-hydroxy-3-(2-[[hydroxy(phosphonooxy)phosphoryl]oxy]ethyl)hex-4-ynoic acid
-
-
0.0028
(3R)-3-hydroxy-3-(2-[[hydroxy(phosphonooxy)phosphoryl]oxy]ethyl)hex-5-enoic acid
-
-
0.0017
(3R)-3-hydroxy-3-(2-[[hydroxy(phosphonooxy)phosphoryl]oxy]ethyl)pent-4-enoic acid
-
-
0.0029
(3R)-3-hydroxy-3-(2-[[hydroxy(phosphonooxy)phosphoryl]oxy]ethyl)pent-4-ynoic acid
-
-
0.005
(R,S)-5-diphosphomevalonate
-
mutant enzyme S192A, at 30C in 100 mM HEPES-NaOH (pH 7.0)
0.0091
(R,S)-5-diphosphomevalonate
-
wild type enzyme, at 30C in 100 mM HEPES-NaOH (pH 7.0)
0.01
5-diphosphomevalonate
-
-
0.0141
5-diphosphomevalonate
-
-
0.02
5-diphosphomevalonate
-
-
0.02
5-diphosphomevalonate
-
37000 MW enzyme form
0.0227
5-diphosphomevalonate
-
45000 MW enzyme form
0.0289
5-diphosphomevalonate
wild type enzyme, at 30C
0.036
5-diphosphomevalonate
-
-
0.036
5-diphosphomevalonate
-
wild type enzyme
0.095
5-diphosphomevalonate
-
mutant S121A, pH 7.0, 30C
0.103
5-diphosphomevalonate
-
mutant D302N, pH 7.0, 30C
0.123
5-diphosphomevalonate
-
wild-type, pH 7.0, 30C
0.1257
5-diphosphomevalonate
mutant enzyme S162A, at 30C
0.177
5-diphosphomevalonate
-
mutant K18M, pH 7.0, 30C
0.267
5-diphosphomevalonate
-
mutant S120A, pH 7.0, 30C
0.307
5-diphosphomevalonate
-
mutant S36A, pH 7.0, 30C
0.397
5-diphosphomevalonate
-
mutant D302A, pH 7.0, 30C
0.425
5-diphosphomevalonate
mutant enzyme N17A, at 30C
0.71
5-diphosphomevalonate
-
45000 MW enzyme form
0.75
5-diphosphomevalonate
-
mutant enzyme K27A
0.92
5-diphosphomevalonate
-
mutant enzyme R154A
0.944
5-diphosphomevalonate
-
mutant S153A, pH 7.0, 30C
1.921
5-diphosphomevalonate
-
mutant S155A, pH 7.0, 30C
12.5
5-diphosphomevalonate
-
in presence of 4 mM MgCl2 and 3 mM ATP
0.00053
ATP
-
-
0.027
ATP
-
wild type enzyme, at 30C in 100 mM HEPES-NaOH (pH 7.0)
0.061
ATP
-
wild-type, pH 7.0, 30C
0.07
ATP
-
mutant enzyme S192A, at 30C in 100 mM HEPES-NaOH (pH 7.0)
0.504
ATP
-
-
0.53
ATP
-
wild type enzyme
0.69
ATP
wild type enzyme, at 30C
0.8
ATP
-
37000 MW enzyme form
1.066
ATP
-
mutant K18M, pH 7.0, 30C
1.4
ATP
-
mutant enzyme R154A
1.66
ATP
-
-
1.87
ATP
-
mutant enzyme K27A
4.9
ATP
mutant enzyme S162A, at 30C
7.7
ATP
mutant enzyme N17A, at 30C
0.048
CdATP2-
-
-
0.47
CTP
-
-
0.0012
diphosphomevalonate
-
-
0.01
mevalonate diphosphate
-
pH 7.2
0.061
MgATP2-
-
wild-type, pH 7.0, 30C
0.065
MgATP2-
-
mutant S36A, pH 7.0, 30C
0.202
MgATP2-
-
-
0.45
MgATP2-
-
1 mM ATP4- above that complexed at the substrate. MgATP2- deceases the Km from 0.45 mM to 0.15 mM
0.525
MgATP2-
-
mutant S120A, pH 7.0, 30C
1.592
MgATP2-
-
mutant S155A, pH 7.0, 30C
2.172
MgATP2-
-
mutant S153A, pH 7.0, 30C
0.029
MnATP2-
-
-
0.888
ZnATP2-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.27
(3R)-3-cyclopropyl-3-hydroxy-5-[[hydroxy(phosphonooxy)phosphoryl]oxy]pentanoic acid
Streptococcus pneumoniae
-
-
1.3
(3R)-3-ethyl-3-hydroxy-5-[[hydroxy(phosphonooxy)phosphoryl]oxy]pentanoic acid
Streptococcus pneumoniae
-
-
0.018
(3R)-3-hydroxy-3-(2-[[hydroxy(phosphonooxy)phosphoryl]oxy]ethyl)-4-methylpentanoic acid
Streptococcus pneumoniae
-
-
0.024
(3R)-3-hydroxy-3-(2-[[hydroxy(phosphonooxy)phosphoryl]oxy]ethyl)-5-methylhexanoic acid
Streptococcus pneumoniae
-
-
0.21
(3R)-3-hydroxy-3-(2-[[hydroxy(phosphonooxy)phosphoryl]oxy]ethyl)hex-4-ynoic acid
Streptococcus pneumoniae
-
-
0.39
(3R)-3-hydroxy-3-(2-[[hydroxy(phosphonooxy)phosphoryl]oxy]ethyl)hex-5-enoic acid
Streptococcus pneumoniae
-
-
3.2
(3R)-3-hydroxy-3-(2-[[hydroxy(phosphonooxy)phosphoryl]oxy]ethyl)pent-4-enoic acid
Streptococcus pneumoniae
-
-
1.3
(3R)-3-hydroxy-3-(2-[[hydroxy(phosphonooxy)phosphoryl]oxy]ethyl)pent-4-ynoic acid
Streptococcus pneumoniae
-
-
0.0058
(R,S)-5-diphosphomevalonate
Staphylococcus epidermidis
-
mutant enzyme S192A, at 30C in 100 mM HEPES-NaOH (pH 7.0)
5.9
(R,S)-5-diphosphomevalonate
Staphylococcus epidermidis
-
wild type enzyme, at 30C in 100 mM HEPES-NaOH (pH 7.0)
0.000115
5-diphosphomevalonate
Saccharomyces cerevisiae
-
mutant S121A, pH 7.0, 30C
0.0022
5-diphosphomevalonate
Homo sapiens
P53602
mutant enzyme R161Q, at 30C
0.15
5-diphosphomevalonate
Saccharomyces cerevisiae
-
mutant K18M, pH 7.0, 30C
0.2
5-diphosphomevalonate
Homo sapiens
P53602
mutant enzyme N17A, at 30C
0.61
5-diphosphomevalonate
Saccharomyces cerevisiae
-
mutant S120A, pH 7.0, 30C
0.65
5-diphosphomevalonate
Saccharomyces cerevisiae
-
mutant S155A, pH 7.0, 30C
1.68
5-diphosphomevalonate
Saccharomyces cerevisiae
-
mutant S153A, pH 7.0, 30C
2.1
5-diphosphomevalonate
Homo sapiens
P53602
mutant enzyme S162A, at 30C
3.35
5-diphosphomevalonate
Saccharomyces cerevisiae
-
mutant S36A, pH 7.0, 30C
4.5
5-diphosphomevalonate
Homo sapiens
P53602
wild type enzyme, at 30C
4.9
5-diphosphomevalonate
Saccharomyces cerevisiae
-
wild-type, pH 7.0, 30C
5.6
diphosphomevalonate
Streptococcus pneumoniae
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
270
(3R)-3-cyclopropyl-3-hydroxy-5-[[hydroxy(phosphonooxy)phosphoryl]oxy]pentanoic acid
Streptococcus pneumoniae
-
-
40126
866
(3R)-3-ethyl-3-hydroxy-5-[[hydroxy(phosphonooxy)phosphoryl]oxy]pentanoic acid
Streptococcus pneumoniae
-
-
40119
0.54
(3R)-3-hydroxy-3-(2-[[hydroxy(phosphonooxy)phosphoryl]oxy]ethyl)-4-methylpent-4-enoic acid
Streptococcus pneumoniae
-
-
156573
1
(3R)-3-hydroxy-3-(2-[[hydroxy(phosphonooxy)phosphoryl]oxy]ethyl)-4-methylpentanoic acid
Streptococcus pneumoniae
-
-
40120
0.8
(3R)-3-hydroxy-3-(2-[[hydroxy(phosphonooxy)phosphoryl]oxy]ethyl)-5-methylhexanoic acid
Streptococcus pneumoniae
-
-
40122
12
(3R)-3-hydroxy-3-(2-[[hydroxy(phosphonooxy)phosphoryl]oxy]ethyl)heptanoic acid
Streptococcus pneumoniae
-
-
156572
33
(3R)-3-hydroxy-3-(2-[[hydroxy(phosphonooxy)phosphoryl]oxy]ethyl)hex-4-ynoic acid
Streptococcus pneumoniae
-
-
40125
139
(3R)-3-hydroxy-3-(2-[[hydroxy(phosphonooxy)phosphoryl]oxy]ethyl)hex-5-enoic acid
Streptococcus pneumoniae
-
-
40121
1882
(3R)-3-hydroxy-3-(2-[[hydroxy(phosphonooxy)phosphoryl]oxy]ethyl)pent-4-enoic acid
Streptococcus pneumoniae
-
-
40123
448
(3R)-3-hydroxy-3-(2-[[hydroxy(phosphonooxy)phosphoryl]oxy]ethyl)pent-4-ynoic acid
Streptococcus pneumoniae
-
-
40124
4666
diphosphomevalonate
Streptococcus pneumoniae
-
-
11295
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000049
(R)-6-fluoromevalonate diphosphate
-
wild type enzyme, at 30C in 100 mM HEPES-NaOH (pH 7.0)
0.0043
(R,S)-diphosphoglycolyl proline
-
wild type enzyme, at 30C in 100 mM HEPES-NaOH (pH 7.0)
0.00302
2-fluoromevalonate 5-diphosphate
-
in 100 mM Tris buffer, pH 7.5, at 25C
0.000062
6-fluoromevalonate 5-diphosphate
wild type enzyme
0.0043
6-fluoromevalonate diphosphate
-
pH and temperature not specified in the publication
-
0.0023
diphosphoglycolyl proline
wild type enzyme
0.00005
diphosphoglycolyl-L-proline
-
pH and temperature not specified in the publication
-
0.018
diphosphoglycolylproline
-
mutant S120A, pH 7.0, 30C
0.066
diphosphoglycolylproline
-
mutant S36A, pH 7.0, 30C
0.105
diphosphoglycolylproline
-
wild-type, pH 7.0, 30C
1.429
diphosphoglycolylproline
-
mutant S155A, pH 7.0, 30C
1.576
diphosphoglycolylproline
-
mutant S153A, pH 7.0, 30C
0.0046
P'-geranyl 2-fluoromevalonate 5-diphosphate
-
in 100 mM Tris buffer, pH 7.5, at 25C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0026
(2E)-3,7-dimethylocta-2,6-dien-1-yl 2-(4-hydroxy-4-methyl-6-oxotetrahydro-2H-pyran-2-yl)ethyl diphosphate
Rattus norvegicus
-
-
0.0065
(2E)-3,7-dimethylocta-2,6-dien-1-yl 4-(4-hydroxy-4-methyl-6-oxotetrahydro-2H-pyran-2-yl)butyl diphosphate
Rattus norvegicus
-
-
0.12
1-(diphosphenyloxy)-3,4-dimethylpentan-3-ol
Rattus norvegicus
-
-
0.08
1-(diphosphenyloxy)-3-methylpentan-3-ol
Rattus norvegicus
-
-
0.05
1-(diphosphenyloxy)-5-fluoro-3-methylpentan-3-ol
Rattus norvegicus
-
-
0.0075
2,2-difluoromevalonate 5-diphosphate
Rattus norvegicus
-
-
0.02
3-ethyl-2-fluoro-3,5-dihydroxy-pentanate 5-diphosphate
Rattus norvegicus
-
-
0.06
4-(diphosphenyloxy)-2-methylbutan-2-ol
Rattus norvegicus
-
-
0.14
4-(diphosphenyloxy)-2-phenylbutan-2-ol
Rattus norvegicus
-
-
0.002
P'-geranyl 3,5,8-trihydroxy-3-methyloctanate 8-diphosphate
Rattus norvegicus
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00000133
-
wild-type, 6xHis tagged, produced in Escherichia coli, 37C, pH 7.4
0.00015
-
mutant S121A, pH 7.0, 30C
0.2327
-
-
0.8
-
mutant S120A, pH 7.0, 30C
0.85
-
mutant S155A, pH 7.0, 30C
2.19
-
mutant S153A, pH 7.0, 30C
4.36
-
mutant S36A, pH 7.0, 30C
6.26
-
-
6.4
-
wild-type, pH 7.0, 30C
6.4
-
pH 7.0, 30C, recombinant enzyme
additional information
-
-
additional information
-
-
additional information
-
improved mutants ScMDD1 (I145F) and ScMDD2 (R74H) produce 3 and 5.888 nmol/h * g cells, respectively, which are 19- and 38fold increases compared to the wild type 6xHis ScMDD
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 6.5
-
-
4 - 7
-
-
4.5 - 7
-
-
7
-
37000 MW form and 45000 MW form
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 10
-
pH 3.0: about 5% of maximal activity, pH 4.0-7.0: maximal activity, pH 10.0: about 40% of maximal activity
4 - 9
-
about 35% of maximal activity at pH 4 and at pH 9, 37000 MW enzyme form
6 - 9
-
pH 6: about 35% of maximal activity, pH 9: about 30% of maximal activity, 45000 MW enzyme form
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5
-
isoelectric focusing
5.83
calculated from sequence of cDNA
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
low activity
Manually annotated by BRENDA team
-
activity changes considerably under different dietary situations; epithelium
Manually annotated by BRENDA team
-
in female rat the activity is lower than in male rat
Manually annotated by BRENDA team
-
high activity
Manually annotated by BRENDA team
-
the relative amount of mevalonate pyrophosphate decarboxylase in kidney is higher than in rats and similar to in mice
Manually annotated by BRENDA team
-
seasonal variations in activity, maximal activity in hot summer months, in the cold winter months the activity cannot be detected
Manually annotated by BRENDA team
-
decrease in activity when rats are fasted, fed with a diet containing 2% cholesterol or made diabetic, increase in activity when the animals are fed with a diet containing 3% cholestyramine; in female rats the activity is higher than in male animals
Manually annotated by BRENDA team
-
from animals fed a diet containing cholestyramine and pravastin
Manually annotated by BRENDA team
-
lower activity of mevalonate-diphosphate decarboxylase is responsible for the reduced cholesterol biosynthesis in the liver of stroke-prone spontaneously hypertensive rat
Manually annotated by BRENDA team
-
high activity, marked induction of MDP in liver by provastatin is responsible for the tissue-specific effect of pravastatin
Manually annotated by BRENDA team
-
mevalonate pyrophosphate decarboxylase in the liver is higher than in other tissues
Manually annotated by BRENDA team
highest expression in liver
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
Ganoderma lucidum HG
-
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
predominantly located in
Manually annotated by BRENDA team
-
37000 Da and 45000 Da enzyme species
Manually annotated by BRENDA team
-
predominantly located in cytosol
Manually annotated by BRENDA team
-
contains a small amount of the 45000 Da enzyme species, but not the 37000 Da species. The 45000 Da enzyme species is localized in the matrix
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36800
Q2FJ52
SDS-PAGE
681448
36800
SDS-PAGE
681448
42200
-
gel filtration
663547
44000
SDS-PAGE
690629
44000
-
SDS-PAGE
707234
44100
-
SDS-PAGE
681448
44120
-
calculated from protein sequence
707234
46000
-
SDS-PAGE
702512
48000
calculated from sequence of cDNA
682276
81500
-
sucrose density gradient centrifugation
4370
87600
-
gel filtration
4370
88000
-
gel filtration
4377
90000
-
gel filtration
4383
100000
-
gel filtration
4382
100000
-
gel filtration
650496
107000
-
gel filtration
666848
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 45000, SDS-PAGE
?
x * 37028, calculated from sequence
?
x * 43270, calculated from amino acid sequence
?
x * 46600, calculated from amino acid sequence
?
Ganoderma lucidum HG
-
x * 43270, calculated from amino acid sequence
-
?
-
x * 37028, calculated from sequence
-
dimer
-
2 * 43500, SDS-PAGE
dimer
-
2 * 46000, SDS-PAGE
dimer
-
2 * 45000, SDS-PAGE
dimer
-
2 * 37000, enzyme form is induced by the diet containing cholestyramine and pravastin, SDS-PAGE; 2 * 45000, SDS-PAGE
dimer
-
2 * 46000, SDS-PAGE
dimer
-
wild-type enzyme exists as homodimer, mutation L79P drastically impairs the oligomerization of the protein
dimer
-
2 * 48000, SDS-PAGE
dimer
Q2FJ52
in solution, gel filtration
dimer
x-ray crystallography
homodimer
-
2 * 36000, gel filtration
monomer
-
1 * 42200, calculated and crystallization data
monomer
in solution, gel filtration
additional information
-
a diet containing 5% cholestyramine and 0.1% pravastatin induces a new enzyme species of 37000 Da
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
intracellular glycosylation does not contribute to the difference between the 45000 MW form and the 37000 MW form of the enzyme
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
vapour diffusion method, with 0.1 M MES buffer pH 6.5, 20% PEG 5000 MME, 0.1 M NaCl, 1 mM dithiothreitol, and 0.2 M ammonium sulfate
hanging drop vapour diffusion method using 0.1 M Tris-HCl (pH 8.0), 1.8 M sodium malonate
Q2FJ52
hanging drop vapor diffusion method, using 0.25 M sodium formate and 16% (w/v) PEG 3350
-
MDD bound to diphosphoglycolyl proline and 6-fluoromevalonate diphosphate, hanging drop vapor diffusion method, using 0.25 M sodium formate and 16% (w/v) PEG 3350, at 20C
-
in complex wih adenosine 5'-(beta,gamma-imido)-triphosphate and Mg2+
-
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
no requirement for SH-containing reagents for stability
-
stabilized by phenylmethylsulfonyl fluoride, aprotinin and leupeptin
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, Tris-HCl buffer, pH 7.0, 20% glycerol, 75 mM KCl, stable for 1 month
-
-20C or -73C, rat liver homogenate with 0.1 mM leupeptin, 0.75 mg/l aprotinin, 0.1 mM phenylmethylsulfonyl fluoride, 15 mM EDTA, 15 mM EGTA, stable for over 3 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-Sepharose resin chromatography
2 enzyme forms: MW 37000 and MW 45000. The MW 37000 enzyme form is induced by the diet containing cholestyramine and pravastin
-
nickel metal affinity column chromatography
-
both, the wild-type 6XHis tag ScMDD and the most active mutant R74H ScMDD2 purified by nickel affinity chromatography under anaerobic conditions, 90 to 95% homogenous
-
Ni2+ chelating column chromatography and HiTrapQ Sepharose column chromatography
Q2FJ52
Ni2+-NTA-Sepharose column chromatography and Resource Q anion-exchange chromatography
-
nickel affinity column chromatography and glutathione-Sepharose column chromatography
-
Ni2+ chelating column chromatography and HiTrapQ Sepharose column chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned under the control of the yeast PMA1 strong promoter, expression in Saccharomyces cerevisiae. Wild-type sterol content is not fully restored suggesting that the Arabidopsis thaliana enzyme activity may not be optimal in yeast
expressed in Saccharomyces cerevisiae
expressed in Saccharomyces cerevisiae
expressed in CV-1 cells
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells. Whole cells of Eschercihia coli produced ScMDD with an N-terminal 6xHis tag form isobutene from 3-hydroxy-3-methylbutyrate at a rate 0.154 nmol/h * g cells
-
expressed in Escherichia coli BL21(DE3) cells
Q2FJ52
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the transcriptional level for mevalonate-5-pyrophosphate decarboxylase is highest at 100 microM methyl jasmonate where it is approximately 2fold higher than the control sample
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the transcriptional level for mevalonate-5-pyrophosphate decarboxylase is highest at 100 microM methyl jasmonate where it is approximately 2fold higher than the control sample
Ganoderma lucidum HG
-
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MPD mRNA expression in liver and MPD protein in brain of stroke-prone spontaneously hypertensive rats is significantly reduced
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
D306A
-
low activity
D306E
-
low activity
D306N
-
low activity
K208A
-
low activity
K23A
-
no activity
K27A
-
low activity
R154A
-
low activity
R162A
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low activity
D302A
-
1000fold decrease in kcat value, still retains ability to stoichiometrically bind nucleotide triphosphates at the active site
D302N
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100000fold decrease in kcat value, still retains ability to stoichiometrically bind nucleotide triphosphates at the active site
K18M
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30fold decrease in kcat value, still retains ability to stoichiometrically bind nucleotide triphosphates at the active site
L79P
-
mutation drastically impairs the oligomerization of the protein
L79P
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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
R74H
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mutant increases specific activity on non-native substrate (3-hydroxy-3-methylbutyrate) by 4.8fold
S120A
-
8fold diminution in kcat-value
S121A
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42000fold diminution in kcat-value
S153A
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18fold inflation in Kd-value for Mg-ATP, 35fold inflation in Km-value for Mg-ATP
S155A
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26fold inflation in Km-value for Mg-ATP, 16fold inflation in Km-value for diphosphomevalonate
S36A
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limited solubility, impaired binding of fluorescent ATP analogue trinitrophenyl-ATP
D283A
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catalytically deficient enzyme with 100000fold decreased kcat value
S192A
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the mutation decreases kcat by about 1000fold
S192A
-
catalytically deficient enzyme with 1000fold decreased kcat value
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
-
siRNAs targeting mevalonate (diphospho) decarboxylase (MVD) are found to inhibit Dengue virus replication in a stable A549 subgenomic Renilla replicon cell line (Rluc-replicon) and in naive A549 cells after dengue type 2 (DEN-2) New Guinea C (NGC) live virus infection, knock down of mevalonate (diphospho) decarboxylase can inhibit dengue viral replication
biofuel production
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enzyme establishes a possible route for biological production of petroleum based fuels and plastics by producing isobutene enzymatically
pharmacology
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the enzyme is an antibiotic target, since inhibition prevents the production of isopentenyl diphosphate