Information on EC 1.17.7.3 - (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase (flavodoxin)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.17.7.3
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RECOMMENDED NAME
GeneOntology No.
(E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase (flavodoxin)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H2O + oxidized flavodoxin = 2-C-methyl-D-erythritol 2,4-cyclodiphosphate + reduced flavodoxin
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
methylerythritol phosphate pathway I
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Terpenoid backbone biosynthesis
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
(E)-4-hydroxy-3-methylbut-2-en-1-yl-diphosphate:oxidized flavodoxin oxidoreductase
A bacterial iron-sulfur protein that contains a [4Fe-4S] cluster. Forms part of an alternative non-mevalonate pathway for isoprenoid biosynthesis that is found in most bacteria [2]. Plants and cyanobacteria have a similar enzyme that utilizes ferredoxin rather than flavodoxin (cf. EC 1.17.7.1).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H2O + oxidized flavodoxin
2-C-methyl-D-erythritol 2,4-cyclodiphosphate + reduced flavodoxin
show the reaction diagram
2-C-methyl-D-erythritol 2,4-cyclodiphosphate + reduced 10-methyl-5-deazaisoalloxazine
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H2O + oxidized 10-methyl-5-deazaisoalloxazine
show the reaction diagram
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-
?
2-C-methyl-D-erythritol 2,4-cyclodiphosphate + reduced deazaflavin
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H2O + oxidized deazaflavin
show the reaction diagram
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low activity with photoreduced deazaflavin as an artifactual electron donor
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?
2-C-methyl-D-erythritol 2,4-cyclodiphosphate + reduced flavodoxin
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H2O + oxidized flavodoxin
show the reaction diagram
[(2R,3R)-3-(hydroxymethyl)-3-methyloxiran-2-yl]methyl trihydrogen diphosphate + O2
[(2R,3R)-3-(hydroxymethyl)-3-methyloxiran-2-yl]methyl trihydrogen diphosphate + H2O
show the reaction diagram
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?
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
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H2O + oxidized flavodoxin
2-C-methyl-D-erythritol 2,4-cyclodiphosphate + reduced flavodoxin
show the reaction diagram
2-C-methyl-D-erythritol 2,4-cyclodiphosphate + reduced flavodoxin
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H2O + oxidized flavodoxin
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
[4Fe-4S]-center
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
iron-sulfur centre
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the protein contained 2.4 iron ions and 4.4 sulfide ions per subunit
Mn2+
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reactivates EDTA-inactivated enzyme
[4Fe-4S]2+ cluster
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the purified protein is inactive. It is activated after reconstitution of its Fe/S cluster
additional information
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the enzyme is active in absence of added metal ions
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2Z)-3-methyl-4-sulfanylbut-2-en-1-yl trihydrogen diphosphate
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(2Z)-4-amino-3-methylbut-2-en-1-yl trihydrogen diphosphate
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aminosulfonylcarbamate
weak inhibitor
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but-3-yn-1-yl trihydrogen diphosphate
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Ca2+
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1 mM, 43% inhibition
Co2+
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1 mM, 29% inhibition
EDTA
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10 mM, complete inhibition, reactivated by Mn2+ to a level of 25%
Fe2+
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1 mM, 11% inhibition
Mg2+
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1 mM, 25% inhibition
N-acyl-N'-oxysulfamate
weak inhibitor
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Ni2+
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1 mM, 30% inhibition
prop-2-yn-1-yl trihydrogen diphosphate
Zn2+
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1 mM, 98% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.7
2-C-methyl-D-erythritol 2,4-cyclodiphosphate
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pH 8.0, 37°C, photometric assay
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0067
prop-2-yn-1-yl trihydrogen diphosphate
Thermus thermophilus;
Q72H18
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.045
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activity with 2-C-methyl-D-erythritol 2,4-cyclodiphosphate and reduced deazaflavin, pH 8.0, 37°C
0.099
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activity with 2-C-methyl-D-erythritol 2,4-cyclodiphosphate and reduced flavodoxin, pH 8.0, 37°C, photometric assay
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 9.5
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pH 8.0: about 65% of maximal activity, pH 9.5: about 75% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
PDB
SCOP
CATH
UNIPROT
ORGANISM
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039);
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579);
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
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x * 43000, SDS-PAGE
84000
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x * 84000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
His6-tagged enzyme. The purified protein is inactive. It is activated after reconstitution of its Fe/S cluster
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recombinant fusion protein comprising maltose binding protein and IspG protein domains
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the recombinant MalE/IspG fusion protein (expression level of about 40% with respect to the total soluble cell protein) is purified by affinity chromatography on an amylose resin FF column that is developed with a gradient of 0-10 mM maltose under anaerobic conditions, whereby the enzyme is enriched by a factor of 2.4
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant fusion protein comprising maltose binding protein and IspG protein domains is expressed in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C270S
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the replacement of any of the three conserved cysteine residues affords mutant proteins which are devoid of catalytic activity and contain less than 6% of Fe2+ and less than 23% of S2- as compared to the wild-type protein
C273S
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the replacement of any of the three conserved cysteine residues affords mutant proteins which are devoid of catalytic activity and contain less than 6% of Fe2+ and less than 23% of S2- as compared to the wild-type protein
C306S
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the replacement of any of the three conserved cysteine residues affords mutant proteins which are devoid of catalytic activity and contain less than 6% of Fe2+ and less than 23% of S2- as compared to the wild-type protein
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