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EC Tree
The taxonomic range for the selected organisms is: Homo sapiens The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
mevalonate diphosphate decarboxylase, mevalonate pyrophosphate decarboxylase, diphosphomevalonate decarboxylase, mevalonate-5-pyrophosphate decarboxylase, mevalonate 5-diphosphate decarboxylase, pyrophosphomevalonate decarboxylase, scmdd, 5-pyrophosphomevalonate decarboxylase, scmdd1, scmdd2,
more
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mevalonate diphosphate decarboxylase
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5-Pyrophosphomevalonate decarboxylase
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Decarboxylase, pyrophosphomevalonate
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Mevalonate (diphospho)decarboxylase
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Mevalonate 5-diphosphate decarboxylase
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mevalonate diphospho decarboxylase
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Mevalonate pyrophosphate decarboxylase
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mevalonate pyrophosphate decraboxylase
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Mevalonate-5-pyrophosphate decarboxylase
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Pyrophosphomevalonate decarboxylase
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Pyrophosphomevalonic acid decarboxylase
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ATP:(R)-5-diphosphomevalonate carboxy-lyase (adding ATP; isopentenyl-diphosphate-forming)
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ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
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?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
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?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
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?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
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the enzyme is responsible for regulation of cholesterogenesis. Response to lipoprotein content of culture medium
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?
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ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
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?
ATP + 5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
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the enzyme is responsible for regulation of cholesterogenesis. Response to lipoprotein content of culture medium
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?
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Mg2+
20 mM, required for activity
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6-fluoromevalonate 5-diphosphate
competitive inhibitor with respect to 5-diphosphomevalonate
diphosphoglycolyl proline
competitive inhibitor with respect to 5-diphosphomevalonate
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Dehydration
Fermentative production of isobutene.
Hypercholesterolemia
Molecular cloning and expression of the cDNAs encoding human and yeast mevalonate pyrophosphate decarboxylase.
Melanoma
Apolipoprotein A-I anti-tumor activity targets cancer cell metabolism.
Neoplasms
Apolipoprotein A-I anti-tumor activity targets cancer cell metabolism.
Neoplasms
Multisite inhibition by phenylacetate of PC-3 cell growth.
Pancreatic Neoplasms
d-Dlta-tocotrienol-mediated suppression of the proliferation of human PANC-1, MIA PaCa-2, and BxPC-3 pancreatic carcinoma cells.
Porokeratosis
Disorder of the mevalonate pathway inhibits calcium-induced differentiation of keratinocytes.
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0.0289 - 0.425
5-diphosphomevalonate
0.0289
5-diphosphomevalonate
wild type enzyme, at 30°C
0.1257
5-diphosphomevalonate
mutant enzyme S162A, at 30°C
0.425
5-diphosphomevalonate
mutant enzyme N17A, at 30°C
0.69
ATP
wild type enzyme, at 30°C
4.9
ATP
mutant enzyme S162A, at 30°C
7.7
ATP
mutant enzyme N17A, at 30°C
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0.0022 - 4.5
5-diphosphomevalonate
0.0022
5-diphosphomevalonate
mutant enzyme R161Q, at 30°C
0.2
5-diphosphomevalonate
mutant enzyme N17A, at 30°C
2.1
5-diphosphomevalonate
mutant enzyme S162A, at 30°C
4.5
5-diphosphomevalonate
wild type enzyme, at 30°C
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0.000062
6-fluoromevalonate 5-diphosphate
wild type enzyme
0.0023
diphosphoglycolyl proline
wild type enzyme
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UniProt
brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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physiological function
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investigation of the role of mevalonate diphospho decarboxylase in viral replication
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MVD1_HUMAN
400
0
43405
Swiss-Prot
other Location (Reliability: 2 )
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dimer
x-ray crystallography
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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
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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
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Ni-Sepharose resin chromatography
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expressed in Escherichia coli BL21(DE3) cells
expressed in CV-1 cells
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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
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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
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
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
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