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 hide
4.1.1.33
-
RECOMMENDED NAME
GeneOntology No.
diphosphomevalonate decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + (R)-5-diphosphomevalonate = ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
isoprene biosynthesis II (engineered)
-
-
Metabolic pathways
-
-
mevalonate metabolism
-
-
mevalonate pathway I
-
-
Terpenoid backbone biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:(R)-5-diphosphomevalonate carboxy-lyase (adding ATP; isopentenyl-diphosphate-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9024-66-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
TrEMBL
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
Q2FJ52
Uniprot
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(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,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
CTP + 5-diphosphomevalonate
CDP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
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
ITP + 5-diphosphomevalonate
IDP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
about 6% of the activity with ATP
-
-
-
UTP + 5-diphosphomevalonate
UDP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
-
13% of the activity with ATP
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
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+
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 hide
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
6-fluoromevalonate monophosphate
-
strong inhibition
-
adenosine 5'-O-(3-thiotriphosphate)
-
-
arsenite-2,3-dimercapto-1-propanol
-
-
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-
-
-
Mn2+
-
-
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+
-
-
additional information
-
probucol decreases mevalonate pyrophosphate decarboxylase in the rat liver
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
-
required
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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 - 0.0091
(R,S)-5-diphosphomevalonate
0.01 - 12.5
5-diphosphomevalonate
0.00053 - 7.7
ATP
0.048
CdATP2-
-
-
0.47
CTP
-
-
0.0012
diphosphomevalonate
-
-
0.01
mevalonate diphosphate
-
pH 7.2
0.061 - 2.172
MgATP2-
0.029
MnATP2-
-
-
0.888
ZnATP2-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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 - 5.9
(R,S)-5-diphosphomevalonate
0.000115 - 4.9
5-diphosphomevalonate
5.6
diphosphomevalonate
Streptococcus pneumoniae
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
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 - 1.576
diphosphoglycolylproline
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 hide
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 hide
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
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 6.5
-
-
4 - 7
-
-
4.5 - 7
-
-
7
-
37000 MW form and 45000 MW form
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
isoelectric focusing
5.83
calculated from sequence of cDNA
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
activity changes considerably under different dietary situations; epithelium
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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 hide
LITERATURE
42000
-
gel filtration, Tris-HCl buffer, presence of 2-mercaptoethanol
42200
-
gel filtration
44100
-
SDS-PAGE
44120
-
calculated from protein sequence
46000
-
SDS-PAGE
48000
calculated from sequence of cDNA
52000
-
gel filtration, sodium phosphate buffer
81500
-
sucrose density gradient centrifugation
87600
-
gel filtration
88000
-
gel filtration
90000
-
gel filtration
100000
107000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
-
2 * 36000, gel filtration
monomer
additional information
-
a diet containing 5% cholestyramine and 0.1% pravastatin induces a new enzyme species of 37000 Da
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
side-chain modification
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; wild-type and mutant S192A and D283A ternary complexes with inbhibitor 6-fluoromevalonate 5-diphosphate and ATPgammaS. During the catalytic mechanism, Asp283 correctly positions the mevalonate diphosphate acceptor substrate, while functioning as a catalytic base to abstract the acidic proton found on its C3-hydroxyl. This deprotonation facilitates an in-line transfer of the gamma-phosphoryl from the ATP donor. The Ser 107 side chain is appropriately positioned to hydrogen bond with both the beta- and gamma-phosphoryl groups of ATPgammaS within the ternary structure
-
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+
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
78
-
melting temperature, mutant C210S
80
-
1 h, complete loss of activity in presence of 2-mercaptoethanol
90
-
melting temperature, wild-type
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 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
-
-20C, Tris-HCl buffer, pH 7.0, 20% glycerol, 75 mM KCl, stable for 1 month
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 enzyme forms: MW 37000 and MW 45000. The MW 37000 enzyme form is induced by the diet containing cholestyramine and pravastin
-
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
-
Ni-Sepharose resin chromatography
Ni2+ chelating column chromatography and HiTrapQ Sepharose column chromatography
Ni2+-NTA-Sepharose column chromatography and Resource Q anion-exchange chromatography
-
nickel affinity column chromatography and glutathione-Sepharose column chromatography
-
nickel metal affinity column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; expressed in Saccharomyces cerevisiae
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 CV-1 cells
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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
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expressed in Saccharomyces cerevisiae
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
MPD mRNA expression in liver and MPD protein in brain of stroke-prone spontaneously hypertensive rats is significantly reduced
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; treatment with methyl jasmonate induces gene expression
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treatment with methyl jasmonate induces gene expression
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
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low activity
D306E
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low activity
D306N
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low activity
K208A
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low activity
K23A
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no activity
K27A
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low activity
R154A
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low activity
R162A
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low activity
D302A
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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
R74H
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mutant increases specific activity on non-native substrate (3-hydroxy-3-methylbutyrate) by 4.8fold
S120A
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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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10000fold decrease in kcat value; catalytically deficient enzyme with 100000fold decreased kcat value
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biofuel production
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enzyme establishes a possible route for biological production of petroleum based fuels and plastics by producing isobutene enzymatically
drug development
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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
pharmacology
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the enzyme is an antibiotic target, since inhibition prevents the production of isopentenyl diphosphate
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