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Information on EC 1.17.7.3 - (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase (flavodoxin)
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1.17.7.3 (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase (flavodoxin)IUBMB Comments
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 . Plants and cyanobacteria have a similar enzyme that utilizes ferredoxin rather than flavodoxin (cf. EC 1.17.7.1).
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Word Map
- 1.17.7.3
-
e-4-hydroxy-3-methylbut-2-enyl
-
isoprenoids
-
mecpp
- mevalonate
-
plastids
-
prosthetic
- epr
-
paramagnetic
-
iron-sulfur
-
isopentenyl
-
dimethylallyl
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
(e)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase, hmbpp synthase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(E)-4-hydroxy-3-methylbut-2-en-1-yl-diphosphate:protein-disulfide oxidoreductase (hydrating)
-
-
incorrect
-
(E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase
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-
ambiguous
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4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
GcpE
IspG
4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
-
-
ambiguous
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IspG
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
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
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-
-
-
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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).
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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
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H2O + oxidized flavodoxin
2-C-methyl-D-erythritol 2,4-cyclodiphosphate + reduced flavodoxin
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
-
-
-
?
2-C-methyl-D-erythritol 2,4-cyclodiphosphate + reduced deazaflavin
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H2O + oxidized deazaflavin
low activity with photoreduced deazaflavin as an artifactual electron donor
-
-
?
2-C-methyl-D-erythritol 2,4-cyclodiphosphate + reduced flavodoxin
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H2O + oxidized flavodoxin
[(2R,3R)-3-(hydroxymethyl)-3-methyloxiran-2-yl]methyl trihydrogen diphosphate + O2
[(2R,3R)-3-(hydroxymethyl)-3-methyloxiran-2-yl]methyl trihydrogen diphosphate + H2O
-
-
-
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H2O + oxidized flavodoxin
2-C-methyl-D-erythritol 2,4-cyclodiphosphate + reduced flavodoxin
-
-
-
-
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H2O + oxidized flavodoxin
2-C-methyl-D-erythritol 2,4-cyclodiphosphate + reduced flavodoxin
-
-
-
?
2-C-methyl-D-erythritol 2,4-cyclodiphosphate + reduced flavodoxin
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H2O + oxidized flavodoxin
-
-
-
-
?
2-C-methyl-D-erythritol 2,4-cyclodiphosphate + reduced flavodoxin
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H2O + oxidized flavodoxin
-
-
-
?
2-C-methyl-D-erythritol 2,4-cyclodiphosphate + reduced flavodoxin
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H2O + oxidized flavodoxin
the enzyme is involved in the deoxyxylulose phosphate pathway of isoprenoid biosynthesis
-
-
?
2-C-methyl-D-erythritol 2,4-cyclodiphosphate + reduced flavodoxin
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H2O + oxidized flavodoxin
the enzyme is involved in the nonmevalonate pathway of isoprenoid biosynthesis
-
-
?
2-C-methyl-D-erythritol 2,4-cyclodiphosphate + reduced flavodoxin
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H2O + oxidized flavodoxin
flavodoxin is essential for activity
-
-
?
2-C-methyl-D-erythritol 2,4-cyclodiphosphate + reduced flavodoxin
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H2O + oxidized flavodoxin
lower apparent activities are found using photoreduced deazaflavin as an artifactual electron donor, whereas dithionite is unable to serve as an artificial electron donor
-
-
?
2-C-methyl-D-erythritol 2,4-cyclodiphosphate + reduced flavodoxin
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H2O + oxidized flavodoxin
Escherichia coli CAR005
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-
-
-
?
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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
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H2O + oxidized flavodoxin
2-C-methyl-D-erythritol 2,4-cyclodiphosphate + reduced flavodoxin
2-C-methyl-D-erythritol 2,4-cyclodiphosphate + reduced flavodoxin
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H2O + oxidized flavodoxin
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H2O + oxidized flavodoxin
2-C-methyl-D-erythritol 2,4-cyclodiphosphate + reduced flavodoxin
-
-
-
-
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H2O + oxidized flavodoxin
2-C-methyl-D-erythritol 2,4-cyclodiphosphate + reduced flavodoxin
-
-
-
?
2-C-methyl-D-erythritol 2,4-cyclodiphosphate + reduced flavodoxin
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H2O + oxidized flavodoxin
-
-
-
-
?
2-C-methyl-D-erythritol 2,4-cyclodiphosphate + reduced flavodoxin
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H2O + oxidized flavodoxin
-
-
-
?
2-C-methyl-D-erythritol 2,4-cyclodiphosphate + reduced flavodoxin
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H2O + oxidized flavodoxin
the enzyme is involved in the deoxyxylulose phosphate pathway of isoprenoid biosynthesis
-
-
?
2-C-methyl-D-erythritol 2,4-cyclodiphosphate + reduced flavodoxin
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H2O + oxidized flavodoxin
the enzyme is involved in the nonmevalonate pathway of isoprenoid biosynthesis
-
-
?
2-C-methyl-D-erythritol 2,4-cyclodiphosphate + reduced flavodoxin
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H2O + oxidized flavodoxin
Escherichia coli CAR005
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
[4Fe-4S]-center
the protein contains 2.4 iron ions and 4.4 sulfide ions per subunit
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
iron-sulfur centre
the protein contained 2.4 iron ions and 4.4 sulfide ions per subunit
[4Fe-4S]2+ cluster
the purified protein is inactive. It is activated after reconstitution of its Fe/S cluster
additional information
the enzyme is active in absence of added metal ions
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
10 mM, complete inhibition, reactivated by Mn2+ to a level of 25%
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.7
2-C-methyl-D-erythritol 2,4-cyclodiphosphate
pH 8.0, 37°C, photometric assay
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.045
activity with 2-C-methyl-D-erythritol 2,4-cyclodiphosphate and reduced deazaflavin, pH 8.0, 37°C
0.099
activity with 2-C-methyl-D-erythritol 2,4-cyclodiphosphate and reduced flavodoxin, pH 8.0, 37°C, photometric assay
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8 - 9.5
pH 8.0: about 65% of maximal activity, pH 9.5: about 75% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
the enzyme is involved in the deoxyxylulose phosphate pathway of isoprenoid biosynthesis
metabolism
the enzyme is involved in the nonmevalonate pathway of isoprenoid biosynthesis
physiological function
-
enzyme activation leads to significant decrease of cell growth and beta-carotene production
physiological function
Escherichia coli CAR005
-
enzyme activation leads to significant decrease of cell growth and beta-carotene production
-
Show AA Sequence and Transmembrane Helices (30750 entries)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C270S
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
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
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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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
His6-tagged enzyme. The purified protein is inactive. It is activated after reconstitution of its Fe/S cluster
recombinant fusion protein comprising maltose binding protein and IspG protein domains
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hecht, S.; Eisenreich, W.; Adam, P.; Amslinger, S.; Kis, K.; Bacher, A.; Arigoni, D.; Rohdich, F.
Studies on the nonmevalonate pathway to terpenes: the role of the GcpE (IspG) protein
Proc. Natl. Acad. Sci. USA
98
14837-14842
2001
Escherichia coli (P62620)
brenda
Rohdich, F.; Zepeck, F.; Adam, P.; Hecht, S.; Kaiser, J.; Laupitz, R.; Grawert, T.; Amslinger, S.; Eisenreich, W.; Bacher, A.; Arigoni, D.
The deoxyxylulose phosphate pathway of isoprenoid biosynthesis: Studies on the mechanisms of the reactions catalyzed by IspG and isph protein
Proc. Natl. Acad. Sci. USA
100
1586-1591
2003
Escherichia coli (P62620)
brenda
Zepeck, F.; Graewert, T.; Kaiser, J.; Schramek, N.; Eisenreich, W.; Bacher, A.; Rohdich, F.
Biosynthesis of isoprenoids. Purification and properties of IspG protein from Escherichia coli
J. Org. Chem.
70
9168-9174
2005
Escherichia coli (P62620)
brenda
Seemann, M.; Tse Sum Bui, B.; Wolff, M.; Tritsch, D.; Campos, N.; Boronat, A.; Marquet, A.; Rohmer, M.
Isoprenoid biosynthesis through the methylerythritol phosphate pathway: the (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase (GcpE) is a [4Fe-4S] protein
Angew. Chem. Int. Ed. Engl.
41
4337-4339
2002
Escherichia coli (P62620)
brenda
Puan, K.; Wang, H.; Dairi, T.; Kuzuyama, T.; Morita, C.
fldA is an essential gene required in the 2-C-methyl-D-erythritol 4-phosphate pathway for isoprenoid biosynthesis
FEBS Lett.
579
3802-3806
2005
Escherichia coli (P62620)
brenda
Wang, W.; Oldfield, E.
Bioorganometallic chemistry with IspG and IspH Structure, function, and inhibition of the [Fe4S4] proteins involved in isoprenoid biosynthesis
Angew. Chem. Int. Ed. Engl.
53
4294-4310
2014
Thermus thermophilus (Q72H18)
brenda
Guerra, F.; Wang, K.; Li, J.; Wang, W.; Liu, Y.; Amin, S.; Oldfield, E.
Inhibition of the 4Fe-4S proteins IspG and IspH An EPR, ENDOR and HYSCORE investigation
Chem. Sci.
5
1642-1649
2014
Escherichia coli
brenda
Zhou, J.; Yang, L.; Wang, C.; Choi, E.; Kim, S.
Enhanced performance of the methylerythritol phosphate pathway by manipulation of redox reactions relevant to IspC, IspG, and IspH
J. Biotechnol.
248
1-8
2017
Escherichia coli (P62620)
brenda
Li, Q.; Fan, F.; Gao, X.; Yang, C.; Bi, C.; Tang, J.; Liu, T.; Zhang, X.
Balanced activation of IspG and IspH to eliminate MEP intermediate accumulation and improve isoprenoids production in Escherichia coli
Metab. Eng.
44
13-21
2017
Escherichia coli, Escherichia coli CAR005
brenda
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Release 2023.1 (January 2023)
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