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Information on EC 4.1.1.33 - diphosphomevalonate decarboxylase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P32377
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4.1.1.33 diphosphomevalonate decarboxylaseSpecify your search results
Word Map
- 4.1.1.33
-
isoprenoids
- mevalonate-5-phosphate
-
cholesterogenesis
-
6-fluoromevalonate
- cholestyramine
-
polyisoprenoid
- 5-phosphomevalonate
- synthesis
- biofuel production
- pharmacology
- drug development
- medicine
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5-Pyrophosphomevalonate decarboxylase
-
-
-
-
Decarboxylase, pyrophosphomevalonate
-
-
-
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Mevalonate (diphospho)decarboxylase
-
-
-
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Mevalonate 5-diphosphate decarboxylase
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-
-
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Mevalonate pyrophosphate decarboxylase
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-
-
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Mevalonate-5-pyrophosphate decarboxylase
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-
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Pyrophosphomevalonate decarboxylase
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-
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Pyrophosphomevalonic acid decarboxylase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + (R)-5-diphosphomevalonate = ADP + phosphate + isopentenyl diphosphate + CO2
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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-, -
SYSTEMATIC NAME
IUBMB Comments
ATP:(R)-5-diphosphomevalonate carboxy-lyase (adding ATP; isopentenyl-diphosphate-forming)
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CAS REGISTRY NUMBER
COMMENTARY
9024-66-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + (R)-5-diphosphomevalonate
ADP + phosphate + isopentenyl diphosphate + CO2
-
-
-
?
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
-
-
-
?
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
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-
?
additional information
?
-
molecular dynamics simulation to characterize the active site of mevalonate 5-diphosphate decarboxylase to predict a probable mechanism in the transition state
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-
?
additional information
?
-
-
molecular dynamics simulation to characterize the active site of mevalonate 5-diphosphate decarboxylase to predict a probable mechanism in the transition state
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
triflouromevalonate diposphate
molecular dynamics simulation for the inhibitor bound complex
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00000133
wild-type, 6xHis tagged, produced in Escherichia coli, 37°C, pH 7.4
6.4
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
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
wild-type enzyme exists as homodimer, mutation L79P drastically impairs the oligomerization of the protein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
R74H
mutant increases specific activity on non-native substrate (3-hydroxy-3-methylbutyrate) by 4.8fold
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
L79P
-
mutation drastically impairs the oligomerization of the protein
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biofuel production
enzyme establishes a possible route for biological production of petroleum based fuels and plastics by producing isobutene enzymatically
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cardemil, E.; Jabalquinto, A.M.
The mechanism of action of mevalonate-5-pyrophosphate decarboxylase
Trends Biochem. Sci.
8
7
1983
Saccharomyces cerevisiae
-
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
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
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)
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
Saccharomyces cerevisiae (P32377), Saccharomyces cerevisiae, Staphylococcus aureus (A0A0H2XIV6), Staphylococcus aureus, Trypanosoma brucei (Q388P2), Trypanosoma brucei
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
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