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Information on EC 1.17.7.4 - 4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase
for references in articles please use BRENDA:EC1.17.7.4
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EC Tree 1 Oxidoreductases
1.17 Acting on CH or CH2 groups
1.17.7 With an iron-sulfur protein as acceptor
1.17.7.4 4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase
IUBMB Comments
An iron-sulfur protein that contains an unusual [4Fe-4S] cluster [5,6]. This enzyme forms a system with a ferredoxin or a flavodoxin and an NAD(P)H-dependent reductase. This is the last enzyme in the non-mevalonate pathway for isoprenoid biosynthesis. This pathway, also known as the 1-deoxy-D-xylulose 5-phosphate (DOXP) or as the 2-C-methyl-D-erythritol-4-phosphate (MEP) pathway, is found in most bacteria and in plant chloroplasts. The enzyme acts in the reverse direction, producing a 5:1 mixture of 3-methylbut-3-en-1-yl diphosphate and prenyl diphosphate.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 1.17.7.4
-
isoprenoids
-
dimethylallyl
- 4-phosphate
- methylerythritol
-
1-hydroxy-2-methyl-2-e-butenyl
-
2-c-methyl-d-erythritol
-
dmapp
- 1-deoxy-d-xylulose
- reductoisomerase
- 1-deoxy-d-xylulose-5-phosphate
-
e-4-hydroxy-3-methylbut-2-enyl
- isoprene
- bertoni
- rebaudiana
- steviol
-
methyl-jasmonate
- synthesis
Reaction Schemes
show+
2
+
=
+
2
+
2
+
2
oxidized ferredoxin [iron-sulfur] cluster
+
=
+
2
reduced ferredoxin [iron-sulfur] cluster
+
2
+
2
+
=
+
2
+
2
+
2
oxidized ferredoxin [iron-sulfur] cluster
+
=
+
2
reduced ferredoxin [iron-sulfur] cluster
+
2
Synonyms
4-hydroxy-3-methylbut-2-enyl diphosphate reductase, 1-hydroxy-2-methyl-2-(e)-butenyl 4-diphosphate reductase, 1-hydroxy-2-methyl-2-(e)-butenyl-4-diphosphate reductase, hshdr1, hshdr2, srhdr, (e)-4-hydroxy-3-methylbut-2-enyl diphosphate reductase, isoprenoid synthesis h, dshdr, lysis-tolerant b, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(E)-4-hydroxy-3-methylbut-2-enyl diphosphate reductase
1-hydroxy-2-methyl-2-(E)-butenyl-4-diphosphate reductase
4-hydroxy-3-methylbut-2-enyl diphosphate reductase
BbHDR
DsHDR
EC 1.17.1.2
-
-
formerly
-
HDR
HDR1
HMBPP reductase
isoprenoid synthesis H
ispH
lysis-tolerant B
LytB
reductase, (E)-4-hydroxy-3-methylbut-2-enyl diphosphate
-
-
-
-
1-hydroxy-2-methyl-2-(E)-butenyl-4-diphosphate reductase
-
1-hydroxy-2-methyl-2-(E)-butenyl-4-diphosphate reductase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
dimethylallyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
isopentenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
dimethylallyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
reaction mechanism, role of protein residues in the IspH mechanism, detailed overview
-
dimethylallyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
reaction mechanism, detailed overview
-
dimethylallyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
results show a bioorganometallic mechanism of IspH catalysis. There are two paramagnetic reaction intermediates proposed in this mechanism. The intermediate trapped with IspH E126Q mutants represents the 3-CH2OH-rotated weak pi-complex, intermediate II. Following a formally two-electron reduction and dehydration of the substrate, intermediate II is converted into an eta3-allyl complex with an oxidized HiPIP-like cluster [4Fe-4S]3+, intermediate III, which is observed with wild type IspH
-
dimethylallyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
-
-
-
isopentenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
reaction mechanism
isopentenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
Forms part of an alternative, nonmevalonate pathway for terpenoid biosynthesis. The enzyme acts in the reverse direction producing a 5:1 mixture of isopentenyl diphosphate and dimethyallyl diphosphate
-
-
-
isopentenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
reaction mechanism, role of protein residues in the IspH mechanism, detailed overview
-
isopentenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
reaction mechanism, detailed overview
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
methylerythritol phosphate pathway I, methylerythritol phosphate pathway II
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SYSTEMATIC NAME
IUBMB Comments
isopentenyl-diphosphate:ferredoxin oxidoreductase
An iron-sulfur protein that contains an unusual [4Fe-4S] cluster [5,6]. This enzyme forms a system with a ferredoxin or a flavodoxin and an NAD(P)H-dependent reductase. This is the last enzyme in the non-mevalonate pathway for isoprenoid biosynthesis. This pathway, also known as the 1-deoxy-D-xylulose 5-phosphate (DOXP) or as the 2-C-methyl-D-erythritol-4-phosphate (MEP) pathway, is found in most bacteria and in plant chloroplasts. The enzyme acts in the reverse direction, producing a 5:1 mixture of 3-methylbut-3-en-1-yl diphosphate and prenyl diphosphate.
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CAS REGISTRY NUMBER
COMMENTARY
512789-14-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
3-methylbut-3-en-1-yl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
dimethylallyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
isopentenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
prenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H + H+
dimethylallyl diphosphate + NAD(P)+ + H2O
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H + H+
isopentenyl diphosphate + NAD(P)+ + H2O
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NADPH
dimethylallyl diphosphate + isopentenyl diphosphate + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + reduced ferredoxin [iron-sulfur] cluster + H+
dimethylallyl diphosphate + oxidized ferredoxin [iron-sulfur] cluster + H2O
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + reduced ferredoxin [iron-sulfur] cluster + H+
isopentenyl diphosphate + oxidized ferredoxin [iron-sulfur] cluster + H2O
2 (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+
dimethylallyl diphosphate + isopentenyl diphosphate + 4 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
isopentenyl diphosphate + NAD(P)+ + H2O
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
3-methylbut-3-en-1-yl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
3-methylbut-3-en-1-yl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
3-methylbut-3-en-1-yl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
3-methylbut-3-en-1-yl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
3-methylbut-3-en-1-yl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
3-methylbut-3-en-1-yl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
3-methylbut-3-en-1-yl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
dimethylallyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: producing a 5:1 mixture of isopentenyl diphosphate and dimethyallyl diphosphate
Products: producing a 5:1 mixture of isopentenyl diphosphate and dimethyallyl diphosphate
r
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
dimethylallyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
r
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
dimethylallyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
dimethylallyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
Substrates: -
Products: dimethylallyl diphosphate is convertable into isopentenyl diphosphate and vice versa
Products: dimethylallyl diphosphate is convertable into isopentenyl diphosphate and vice versa
r
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
dimethylallyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
Substrates: -
Products: -
Products: -
r
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
dimethylallyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
r
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
dimethylallyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
dimethylallyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
Substrates: -
Products: dimethylallyl diphosphate is convertable into isopentenyl diphosphate and vice versa
Products: dimethylallyl diphosphate is convertable into isopentenyl diphosphate and vice versa
r
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
dimethylallyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
Substrates: -
Products: -
Products: -
r
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
isopentenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: producing a 5:1 mixture of isopentenyl diphosphate and dimethyallyl diphosphate
Products: producing a 5:1 mixture of isopentenyl diphosphate and dimethyallyl diphosphate
r
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
isopentenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
isopentenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
Substrates: -
Products: -
Products: -
r
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
isopentenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
r
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
isopentenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
Substrates: -
Products: Co2+ and Mn2+ lower the content of isopentenyl diphosphate in the mixture of both products, isopentenyl diphosphate and dimethylallyl diphosphate
Products: Co2+ and Mn2+ lower the content of isopentenyl diphosphate in the mixture of both products, isopentenyl diphosphate and dimethylallyl diphosphate
r
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
isopentenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
isopentenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
isopentenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
isopentenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
Substrates: -
Products: -
Products: -
r
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
prenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
prenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
prenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
prenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
prenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
prenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
prenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H + H+
dimethylallyl diphosphate + NAD(P)+ + H2O
-
Substrates: HMBPP reductase catalyzes the 2H+/2e- reduction of (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate to form an approximately 5:1 mixture of isopentenyl diphosphate and dimethylallyl diphosphate, insights into IspH catalysis and inhibition, involving organometallic species. Residue E126 is essential for catalytic activity. Residue H124 is not a major contributor to substrate binding, but is essential for catalysis, it is involved in delivering H+ to E126 and the bound (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate. Residue H42 forms hydrogen bonds to the bound diphosphate ligand. Ligand binding structure spectral analysis and modelling, overview
Products: -
Products: -
r
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H + H+
dimethylallyl diphosphate + NAD(P)+ + H2O
-
Substrates: formation of a mixture of isopentenyl diphosphate and dimethylallyl diphosphate in a ratio 1:5
Products: -
Products: -
r
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H + H+
dimethylallyl diphosphate + NAD(P)+ + H2O
-
Substrates: HMBPP reductase catalyzes the 2H+/2e- reduction of (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate to form an approximately 5:1 mixture of isopentenyl diphosphate and dimethylallyl diphosphate, insights into IspH catalysis and inhibition, involving organometallic species, overview
Products: -
Products: -
r
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H + H+
dimethylallyl diphosphate + NAD(P)+ + H2O
-
Substrates: in the nonmevalonate pathway, the terminal intermediate, 1-hydroxy-2-methyl-2-butenyl 4-diphosphate, i.e. HMBPP, is reductively converted into a mixture of isopentenyl diphosphate and dimethylallyl diphosphate
Products: -
Products: -
r
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H + H+
dimethylallyl diphosphate + NAD(P)+ + H2O
-
Substrates: formation of a mixture of isopentenyl diphosphate and dimethylallyl diphosphate
Products: -
Products: -
r
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H + H+
isopentenyl diphosphate + NAD(P)+ + H2O
-
Substrates: HMBPP reductase catalyzes the 2H+/2e- reduction of (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate to form an approximately 5:1 mixture of isopentenyl diphosphate and dimethylallyl diphosphate, insights into IspH catalysis and inhibition, involving organometallic species. Residue E126 is essential for catalytic activity. Residue H124 is not a major contributor to substrate binding, but is essential for catalysis, it is involved in delivering H+ to E126 and the bound (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate. Residue H42 forms hydrogen bonds to the bound diphosphate ligand. Ligand binding structure spectral analysis and modelling, overview
Products: -
Products: -
r
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H + H+
isopentenyl diphosphate + NAD(P)+ + H2O
-
Substrates: formation of a mixture of isopentenyl diphosphate and dimethylallyl diphosphate in a ratio 1:5
Products: -
Products: -
r
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H + H+
isopentenyl diphosphate + NAD(P)+ + H2O
-
Substrates: HMBPP reductase catalyzes the 2H+/2e- reduction of (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate to form an approximately 5:1 mixture of isopentenyl diphosphate and dimethylallyl diphosphate, insights into IspH catalysis and inhibition, involving organometallic species, overview
Products: -
Products: -
r
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H + H+
isopentenyl diphosphate + NAD(P)+ + H2O
-
Substrates: in the nonmevalonate pathway, the terminal intermediate, 1-hydroxy-2-methyl-2-butenyl 4-diphosphate, i.e. HMBPP, is reductively converted into a mixture of isopentenyl diphosphate and dimethylallyl diphosphate
Products: -
Products: -
r
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H + H+
isopentenyl diphosphate + NAD(P)+ + H2O
-
Substrates: formation of a mixture of isopentenyl diphosphate and dimethylallyl diphosphate
Products: -
Products: -
r
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + reduced ferredoxin [iron-sulfur] cluster + H+
dimethylallyl diphosphate + oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + reduced ferredoxin [iron-sulfur] cluster + H+
dimethylallyl diphosphate + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + reduced ferredoxin [iron-sulfur] cluster + H+
dimethylallyl diphosphate + oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + reduced ferredoxin [iron-sulfur] cluster + H+
dimethylallyl diphosphate + oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + reduced ferredoxin [iron-sulfur] cluster + H+
isopentenyl diphosphate + oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + reduced ferredoxin [iron-sulfur] cluster + H+
isopentenyl diphosphate + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + reduced ferredoxin [iron-sulfur] cluster + H+
isopentenyl diphosphate + oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + reduced ferredoxin [iron-sulfur] cluster + H+
isopentenyl diphosphate + oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
2 (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+
dimethylallyl diphosphate + isopentenyl diphosphate + 4 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
Substrates: -
Products: ratio of dimethylallyl diphosphate to isopentenyl diphosphate produced is 1 to 6.3
Products: ratio of dimethylallyl diphosphate to isopentenyl diphosphate produced is 1 to 6.3
?
2 (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+
dimethylallyl diphosphate + isopentenyl diphosphate + 4 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
Substrates: -
Products: mixture of products
Products: mixture of products
?
isopentenyl diphosphate + NAD(P)+ + H2O
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H
Substrates: part of isoprenoid biosynthesis
Products: -
Products: -
r
isopentenyl diphosphate + NAD(P)+ + H2O
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H
Substrates: 2-C-methyl-D-erithritol-4-phosphate pathway
Products: -
Products: -
r
isopentenyl diphosphate + NAD(P)+ + H2O
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H
-
Substrates: part of isoprenoid biosynthesis
Products: -
Products: -
r
isopentenyl diphosphate + NAD(P)+ + H2O
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H
-
Substrates: biosynthesis of terpenes
Products: -
Products: -
r
isopentenyl diphosphate + NAD(P)+ + H2O
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H
Substrates: biosynthesis of terpenes
Products: -
Products: -
r
isopentenyl diphosphate + NAD(P)+ + H2O
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H
-
Substrates: 2-C-methyl-D-erithritol-4-phosphate pathway
Products: -
Products: -
r
isopentenyl diphosphate + NAD(P)+ + H2O
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H
Substrates: investigation of biosynthetic coupling and pattern by expression of involved genes from synthetic operon
Products: -
Products: -
r
isopentenyl diphosphate + NAD(P)+ + H2O
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H
-
Substrates: 2-C-methyl-D-erithritol-4-phosphate pathway
Products: -
Products: -
r
additional information
?
-
Substrates: the affinity of Fe-S cluster binding to the cleft is similar to substrate HMBPP
Products: -
Products: -
?
additional information
?
-
-
Substrates: the IspH-catalyzed reaction involves formation of organometallic species, containing Fe-C bonds
Products: -
Products: -
?
additional information
?
-
-
Substrates: active site structure analysis of the IspH protein in complex with the substrate and the reaction products, or with diphosphate, overview. IspH is more stable in its closed conformation with a substrate molecule bound to the cluster, compared to its open conformation in solution
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme produces a 5:1 mixture of 3-methylbut-3-en-1-yl diphosphate and prenyl diphosphate
Products: -
Products: -
?
additional information
?
-
Substrates: turnover numbers of IspH are measured using artificial reducing agents
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme produces a 5:1 mixture of 3-methylbut-3-en-1-yl diphosphate and prenyl diphosphate
Products: -
Products: -
?
additional information
?
-
Substrates: turnover numbers of IspH are measured using artificial reducing agents
Products: -
Products: -
?
additional information
?
-
-
Substrates: production of isopentenyl diphosphate and dimethylallyl diphosphate is key step in controlling the production of plastidial isoprenoid precursors and carotenoid biosynthesis in plant cells
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
3-methylbut-3-en-1-yl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
dimethylallyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
isopentenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
prenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H + H+
dimethylallyl diphosphate + NAD(P)+ + H2O
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H + H+
isopentenyl diphosphate + NAD(P)+ + H2O
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + reduced ferredoxin [iron-sulfur] cluster + H+
dimethylallyl diphosphate + oxidized ferredoxin [iron-sulfur] cluster + H2O
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + reduced ferredoxin [iron-sulfur] cluster + H+
isopentenyl diphosphate + oxidized ferredoxin [iron-sulfur] cluster + H2O
isopentenyl diphosphate + NAD(P)+ + H2O
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
3-methylbut-3-en-1-yl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
3-methylbut-3-en-1-yl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
3-methylbut-3-en-1-yl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
3-methylbut-3-en-1-yl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
3-methylbut-3-en-1-yl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
3-methylbut-3-en-1-yl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
3-methylbut-3-en-1-yl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
dimethylallyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
r
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
dimethylallyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
dimethylallyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
Substrates: -
Products: -
Products: -
r
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
dimethylallyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
r
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
dimethylallyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
dimethylallyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
Substrates: -
Products: -
Products: -
r
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
isopentenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
isopentenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
prenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
prenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
prenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
prenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
prenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
prenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
prenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H + H+
dimethylallyl diphosphate + NAD(P)+ + H2O
-
Substrates: HMBPP reductase catalyzes the 2H+/2e- reduction of (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate to form an approximately 5:1 mixture of isopentenyl diphosphate and dimethylallyl diphosphate, insights into IspH catalysis and inhibition, involving organometallic species. Residue E126 is essential for catalytic activity. Residue H124 is not a major contributor to substrate binding, but is essential for catalysis, it is involved in delivering H+ to E126 and the bound (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate. Residue H42 forms hydrogen bonds to the bound diphosphate ligand. Ligand binding structure spectral analysis and modelling, overview
Products: -
Products: -
r
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H + H+
dimethylallyl diphosphate + NAD(P)+ + H2O
-
Substrates: formation of a mixture of isopentenyl diphosphate and dimethylallyl diphosphate in a ratio 1:5
Products: -
Products: -
r
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H + H+
dimethylallyl diphosphate + NAD(P)+ + H2O
-
Substrates: in the nonmevalonate pathway, the terminal intermediate, 1-hydroxy-2-methyl-2-butenyl 4-diphosphate, i.e. HMBPP, is reductively converted into a mixture of isopentenyl diphosphate and dimethylallyl diphosphate
Products: -
Products: -
r
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H + H+
isopentenyl diphosphate + NAD(P)+ + H2O
-
Substrates: HMBPP reductase catalyzes the 2H+/2e- reduction of (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate to form an approximately 5:1 mixture of isopentenyl diphosphate and dimethylallyl diphosphate, insights into IspH catalysis and inhibition, involving organometallic species. Residue E126 is essential for catalytic activity. Residue H124 is not a major contributor to substrate binding, but is essential for catalysis, it is involved in delivering H+ to E126 and the bound (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate. Residue H42 forms hydrogen bonds to the bound diphosphate ligand. Ligand binding structure spectral analysis and modelling, overview
Products: -
Products: -
r
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H + H+
isopentenyl diphosphate + NAD(P)+ + H2O
-
Substrates: formation of a mixture of isopentenyl diphosphate and dimethylallyl diphosphate in a ratio 1:5
Products: -
Products: -
r
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H + H+
isopentenyl diphosphate + NAD(P)+ + H2O
-
Substrates: in the nonmevalonate pathway, the terminal intermediate, 1-hydroxy-2-methyl-2-butenyl 4-diphosphate, i.e. HMBPP, is reductively converted into a mixture of isopentenyl diphosphate and dimethylallyl diphosphate
Products: -
Products: -
r
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + reduced ferredoxin [iron-sulfur] cluster + H+
dimethylallyl diphosphate + oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + reduced ferredoxin [iron-sulfur] cluster + H+
dimethylallyl diphosphate + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + reduced ferredoxin [iron-sulfur] cluster + H+
dimethylallyl diphosphate + oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + reduced ferredoxin [iron-sulfur] cluster + H+
dimethylallyl diphosphate + oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + reduced ferredoxin [iron-sulfur] cluster + H+
isopentenyl diphosphate + oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + reduced ferredoxin [iron-sulfur] cluster + H+
isopentenyl diphosphate + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + reduced ferredoxin [iron-sulfur] cluster + H+
isopentenyl diphosphate + oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + reduced ferredoxin [iron-sulfur] cluster + H+
isopentenyl diphosphate + oxidized ferredoxin [iron-sulfur] cluster + H2O
Substrates: -
Products: -
Products: -
?
isopentenyl diphosphate + NAD(P)+ + H2O
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H
Substrates: part of isoprenoid biosynthesis
Products: -
Products: -
r
isopentenyl diphosphate + NAD(P)+ + H2O
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H
Substrates: 2-C-methyl-D-erithritol-4-phosphate pathway
Products: -
Products: -
r
isopentenyl diphosphate + NAD(P)+ + H2O
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H
-
Substrates: part of isoprenoid biosynthesis
Products: -
Products: -
r
isopentenyl diphosphate + NAD(P)+ + H2O
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H
-
Substrates: biosynthesis of terpenes
Products: -
Products: -
r
isopentenyl diphosphate + NAD(P)+ + H2O
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H
Substrates: biosynthesis of terpenes
Products: -
Products: -
r
isopentenyl diphosphate + NAD(P)+ + H2O
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H
-
Substrates: 2-C-methyl-D-erithritol-4-phosphate pathway
Products: -
Products: -
r
isopentenyl diphosphate + NAD(P)+ + H2O
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H
Substrates: investigation of biosynthetic coupling and pattern by expression of involved genes from synthetic operon
Products: -
Products: -
r
isopentenyl diphosphate + NAD(P)+ + H2O
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H
-
Substrates: 2-C-methyl-D-erithritol-4-phosphate pathway
Products: -
Products: -
r
additional information
?
-
Substrates: the enzyme produces a 5:1 mixture of 3-methylbut-3-en-1-yl diphosphate and prenyl diphosphate
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme produces a 5:1 mixture of 3-methylbut-3-en-1-yl diphosphate and prenyl diphosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: production of isopentenyl diphosphate and dimethylallyl diphosphate is key step in controlling the production of plastidial isoprenoid precursors and carotenoid biosynthesis in plant cells
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
deazaflavin
-
requires a reducing system, e.g. flavodoxin/flavodoxin reductase or NADPH or the photoreduced deazaflavin radical
FAD
-
requires a reducing system, e.g. flavodoxin/flavodoxin reductase or NADPH or the photoreduced deazaflavin radical
[4Fe-4S] cluster
the Fe-S cluster binding site is formed with three conserved residues of cysteine at positions C123, C214, C251 of ApHDR. The affinity of Fe-S cluster binding to the cleft is similar to substrate HMBPP
additional information
-
enzyme possesses a dioxygen-sensitive [4Fe-4S] cluster as prosthetic group
-
NADPH
-
requires a reducing system, e.g. flavodoxin/flavodoxin reductase or NADPH or the photoreduced deazaflavin radical
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
-
Co2+ and Mn2+, at 0.5 mM, lower the content of isopentenyl diphosphate in the mixture of both products, isopentenyl diphosphate and dimethylallyl diphosphate
Fe2+
Iron
-
(3FE-4S)+ cluster, 2.6 mol of iron per mol of subunit, wild-type, 0.6 mol per mol of subunit, mutant C12S, 0.9 mol per mol of subunit, mutant C92S, 1.4 mol, mutant C197S
Iron-sulfur cluster
Mn2+
Iron-sulfur cluster
the iron-sulfur bridge is involved in catalysis
Mn2+
-
Co2+ and Mn2+, at 0.5 mM, lower the content of isopentenyl diphosphate in the mixture of both products, isopentenyl diphosphate and dimethylallyl diphosphate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
inhibitor molecular docking analysis
-
additional information
-
analysis of alkynyl diphosphate inhibitors, inhibition model based on an electrostatic interaction with the active site E126, model for alkyne inhibition involving pi (or pi/sigma) metallacycle complex formation with the unique 4th Fe in the Fe4S4 cluster, computational docking and quantum chemical calculations, overview
-
additional information
-
pyridine inhibitors of IspH directly bind to the unique fourth Fe in the 4Fe-4S cluster, spectral binding structure analysis and inhibitor design, overview
-
additional information
-
alkyne diphosphates are potent IspH inhibitors that form metallacycle complexes. Identification of inhibitors using the metallacycle model
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.006
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate
-
pH 8, temperature not specified in the publication
0.0212
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate
-
pH 8, temperature not specified in the publication
0.59
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate
recombinant enzyme, pH 7.5, 60°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.11
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate
-
pH 8, temperature not specified in the publication
3.11
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate
-
pH 8, temperature not specified in the publication
3.7
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate
recombinant enzyme, pH 7.5, 60°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
52.35
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate
-
pH 8, temperature not specified in the publication
518.3
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate
-
pH 8, temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10
propargyl alcohol
-
above, pH not specified in the publication, temperature not specified in the publication
0.97
propargyl diphosphate
-
pH not specified in the publication, temperature not specified in the publication
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0091
2-(pyridin-3-yl)ethyl diphosphate
Aquifex aeolicus
-
pH not specified in the publication, temperature not specified in the publication
0.00045
but-3-ynyl diphosphate
Aquifex aeolicus
-
pH not specified in the publication, temperature not specified in the publication
1.2
pyridin-2-ylmethyl diphosphate
Aquifex aeolicus
-
pH not specified in the publication, temperature not specified in the publication
0.149
pyridin-4-ylmethyl trihydrogen diphosphate
Aquifex aeolicus
-
pH not specified in the publication, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.011
-
purified apoenzyme, with photoreduced deazaflavin as reducing cofactor
0.03
-
reconstituted purified enzyme, with photoreduced deazaflavin as reducing cofactor
0.044
-
reconstituted purified enzyme, with FAD and NADPH as reducing cofactors
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.6
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
induced in correlation with carotinoid production during fruit ripening and, in recombinant Arabidopsis thaliana, in correlation with deetiolation of seedlings
-
-
brenda
plants are sampled in Bawangling Nature Reserve of Hainan province (at the altitude of 1320m, 109°10'E, 19°7'N), gene HsHDR1
UniProt
brenda
plants are sampled in Bawangling Nature Reserve of Hainan province (at the altitude of 1320m, 109°10'E, 19°7'N), gene HsHDR2
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
especially in young leaves followed by mature leaves
brenda
-
highest enzyme protein levels are detected in young leaves
brenda
additional information
ApHDR is expressed in all tissues. The expression profile of ApHDR suggests a significant variation in the expression pattern among different tissues such as mature leaves, young leaves, stem and roots, with a 16fold higher expression of ApHDR observed in the mature leaves compared to roots
brenda
additional information
-
enzyme is detected in all tissues analyzed
brenda
additional information
gene expression analysis during a culture period, overview
brenda
additional information
-
gene expression analysis during a culture period, overview
-
brenda
additional information
spatial transcript levels indicated that isozyme OsIspH1 is highly expressed in all tissues at different developmental stages, whereas isozyme OsIspH2 is barely expressed due to an early stop in exon 1 caused by splicing error, expression patterns
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
N-terminal bipartite sequence is required for targeting proteins to the apicoplast lumen
brenda
additional information
no transmembrane regions in the SmHDR1 polypeptide
-
brenda
a chloroplast transit peptide with 33 amino acids is found at the N-terminus of ApHDR
brenda
the enzyme has a chloroplast transit peptide, the cleavage site of the putative N-terminal cTP of SmHDR1 is predicted to be located between Arg33 and Cys34, comprising 33 amino acid residues
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
compared with the bacterial IspH, cyanobacterial and plant HDRs all contain an extra N-terminal conserved domain (NCD) that is essential for their function. Tyr72 in the NCD and several plant-specific residues around the central active site are critical for Arabidopsis HDR function
evolution
the structure and reaction mechanism of HDR evolution have become specific for oxygen-evolving photosynthesis organisms and that enzyme HDR probably evolved independently in cyanobacteria versus other prokaryotes
evolution
phylogenetic analysis, evolutionary relationship of the rice IspH family with predicted amino acid sequences of 79 IspHs
malfunction
-
HDR1 is able to complement an Escherichia coli hdr deletion mutant (DYTL1)
malfunction
-
HDR2 is able to complement an Escherichia coli hdr deletion mutant (DYTL1)
malfunction
construction of genomic HDR transgene-induced gene-silencing lines showing an albino, variegated, or pale green phenotype, confirming that HDR is essential for plants
malfunction
a T-DNA inserted knockout mutant, osisph1, shows an albino phenotype, indicating that OsIspH1 is the only functional gene. The albinism phenotype of osisph1 might also be mediated by the defective chloroplast biogenesis. When overexpressed in rice plants, the H145P/K407R double-mutated gene, OsIspH1MUT, reduces chlorophyll and carotenoid biosynthesis in the leaves and seeds
malfunction
overexpresson of HMBPP reductase slightly reduces flavuxanthin formation in recombinant Escherichia coli
malfunction
-
overexpresson of HMBPP reductase slightly reduces flavuxanthin formation in recombinant Escherichia coli
-
metabolism
function of HsHDR1 and HsHDR2 in terpenoid and sterol biosynthesis in Huperziaceae plants
metabolism
the enzyme catalyzes the last step of the methylerythritol phosphate pathway to synthesize isopentenyl diphosphate and dimethylallyl diphosphate
metabolism
enzyme overexpression leads to the increase of artemisinin production
metabolism
-
the terminal enzyme of the methylerythritol phosphate pathway regulates chlorophyll and carotenoid biosynthesis
metabolism
differential regulation of an OsIspH1, the functional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase, for photosynthetic pigment biosynthesis in rice leaves and seeds. Crucial role of OsIspH1 in plastidic terpenoid biosynthesis with organ-specific differential regulation of OsIspH1 in rice plants
metabolism
terpenoids are of high interest as chemical building blocks and pharmaceuticals. In microbes, terpenoids can be synthesized via the methylerythritol phosphate (MEP) or mevalonate (MVA) pathways. In the MEP pathway of Escherichia coli recombinantly expressing isoprene synthase (ispS) from Populus alba, the endogenous expression of 1-deoxyxylulose 5-phosphate synthase (Dxs) controls the flux through the MEP pathway increasing the 2-C-methyl-d-erythritol-2,4-cyclopyrophosphate (MEcPP) concentration to a higher amount compared to the other MEP pathway intermediates. Thus, 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (IspG), which consumes MEcPP, becomes saturated and therefore limits the flux towards isoprene. The higher intracellular concentrations of MEcPP lead to the efflux of this intermediate into the growth medium. Proteomic and metabolomic analysis of the MEP pathway, overview
metabolism
-
the content of total polysaccharide and total saponin is positively correlated with the expression patterns of several enzymes including 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (ispF, EC 4.6.1.12), (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase (ispG, EC 1.17.7.1), and 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (ispH), transcriptome analysis and determination of a link between polysaccharides and saponin biosynthesis and gene expression, detailed overview. For saponin biosynthesis pathway, the genes encoding HMGS, MVK, ispF, ispG, ispH and FPPS enzymes are high expressed in three-year rhizomes, and these gene expression pattern is consistent with the accumulation pattern of total saponin with the rhizome development. It seems that MEP and MVA pathway all participate in the saponin biosynthesis
metabolism
the two pathways namely cytosolic MVA and plastidial, methyl erythritol diphosphate pathway (MEP) are involved in biosynthesis of isopentyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). The IPP and DMAPP subsequently lead to the production of diterpenes. Both the MVA and MEP pathways are involved in the synthesis of precursors (IPP and DMAPP) and there exists the cross talk between cytoplasm and plastids. The MEP pathway is a seven step multi-enzyme pathway wherein the ultimate step is catalyzed by the enzyme 4-hydroxy 3-methyl 2-butenyl 4-diphosphate reductase (HDR). The HDR is also known as LytB or IspH and has been proved as key regulatory enzyme which converts HMBDB into IPP and DMAPP
metabolism
in the B race of the algal species Botryococcus braunii, precursors of triterpene hydrocarbons are provided from the 2-C-methyl-d-erythritol 4-phosphate (MEP) pathway. The terminal enzyme of this pathway, 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HDR), is regarded as one of the key enzymes that affect yields of products in terpene biosynthesis
metabolism
-
terpenoids are of high interest as chemical building blocks and pharmaceuticals. In microbes, terpenoids can be synthesized via the methylerythritol phosphate (MEP) or mevalonate (MVA) pathways. In the MEP pathway of Escherichia coli recombinantly expressing isoprene synthase (ispS) from Populus alba, the endogenous expression of 1-deoxyxylulose 5-phosphate synthase (Dxs) controls the flux through the MEP pathway increasing the 2-C-methyl-d-erythritol-2,4-cyclopyrophosphate (MEcPP) concentration to a higher amount compared to the other MEP pathway intermediates. Thus, 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (IspG), which consumes MEcPP, becomes saturated and therefore limits the flux towards isoprene. The higher intracellular concentrations of MEcPP lead to the efflux of this intermediate into the growth medium. Proteomic and metabolomic analysis of the MEP pathway, overview
-
metabolism
-
in the B race of the algal species Botryococcus braunii, precursors of triterpene hydrocarbons are provided from the 2-C-methyl-d-erythritol 4-phosphate (MEP) pathway. The terminal enzyme of this pathway, 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HDR), is regarded as one of the key enzymes that affect yields of products in terpene biosynthesis
-
physiological function
-
IspH is a 4Fe-4S protein that carries out an essential reduction step in isoprenoid biosynthesis
physiological function
-
SrHDR rescues Escherichia coli HDR mutant strain MG1655
physiological function
enzyme SmHDR1 is HDR is involved in the plastid nonmevalonate pathway of isoprenoid biosynthesis, it is an important enzyme involved in the biosynthesis of diterpenoid tanshinones in Salvia miltiorrhiza Bge. f. alba, HDR is key enzyme in the biosynthesis of precursors of isoprenoids
physiological function
the methylerythritol 4-phosphate (MEP) pathway is responsible for providing common precursors for the biosynthesis of diverse plastidial terpenoids, including chlorophylls, carotenoids, and phytohormones, in plants. In Oryza sativa, the last-step genes encoding 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HDR/isoprenoid synthesis H (IspH)) have been annotated in two genes (OsIspH1 and OsIspH2) in the rice genome. Crucial role of OsIspH1 in plastidic terpenoid biosynthesis with organ-specific differential regulation of OsIspH1 in rice plants
additional information
the enzyme contains an extra N-terminal conserved domain (NCD) that is essential for its function. Tyr72 in the NCD and several plant-specific residues around the central active site are critical for Arabidopsis HDR function, homology modeling and substrate docking of the IspH domain of the Arabidopsis enzyme HDR, sequence comparisons, overview
additional information
homology modeling using Escherichia coli isoprenoid synthesis H, PDB ID 3F7T, as a template. Residues Cys122, Cys213, and Cys350 are involved in iron-sulfur cluster formation and His152, His241, Glu242, Glu243, Thr244, Thr312, Ser379, and Asp381 are related to substrate binding or catalysis
additional information
Oryza sativa IspH1 three-dimensional modeling based on the structure of Aquifex aeolicus IspH, PDB ID 3DNF
additional information
simple overexpression of IspG (EC 1.17.7.3) and IspH does not increase the flux towards terpenoids via the MEP pathway
additional information
enzyme three-dimensional structure homology modeling using the crystal structure of Escherichia coli (PDB ID 3ke8.1A) as a template, structural comparisons of enzyme ApHDR, overview
additional information
three-dimensional structure modeling using a crystal structure of HDR from Escherichia coli (PDB ID 3F7T) as a template, overview
additional information
-
simple overexpression of IspG (EC 1.17.7.3) and IspH does not increase the flux towards terpenoids via the MEP pathway
-
additional information
-
three-dimensional structure modeling using a crystal structure of HDR from Escherichia coli (PDB ID 3F7T) as a template, overview
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36591
-
2 * 36591, recombinant His-tagged enzyme, amino acid sequence determination
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
2 * 36591, recombinant His-tagged enzyme, amino acid sequence determination
additional information
?
x * 36161-36173, recombinant enzyme, DNA sequence determination and electrospray mass spectroscopy
additional information
the enzyme contains the conserved domain of 1-hydroxy-2-methyl-2-(E)-butenyl-4-diphosphate reductase (PF02401), but no transmembrane region and signal peptide, secondary structure and structural domains, overview
additional information
the enzyme contains the conserved domain of 1-hydroxy-2-methyl-2-(E)-butenyl-4-diphosphate reductase (PF02401), but no transmembrane region and signal peptide, secondary structure and structural domains, overview
additional information
-
the enzyme contains the conserved domain of 1-hydroxy-2-methyl-2-(E)-butenyl-4-diphosphate reductase (PF02401), but no transmembrane region and signal peptide, secondary structure and structural domains, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant IspH, sitting drop vapour diffusion method at 20°C, 0.004 ml of 35 /ml protein in 50 mM Tris-HCl, pH 8.0, is mixed with 0.004 ml of reservoir solution containing 100 mM Bis-Tris-HCl, pH 6.5, 200 mM lithium sulfate and 25% PEG 3350, final pH is 6.8, crystal soaking in 2 M lithium sulfate, pH 6.5, before freezing, X-ray diffraction structure determination and analysis at 1.4 A resolution, molecular replacement, modelling
-
crystallized under anaerobic conditions. Its structure is determined by the multiple anomalous dispersion method and refined to final R/Rfree factors of 17.5/19.5% at 2.2 A resolution. LytB is a momoner which is essentially composed of three related alpha/beta-domains arranged in a cloverleaf form with the Fe/S-cluster in its center
Q9BJX6
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E126A
-
site-directed mutagenesis, the mutant is almost inactive, formation of an organometallic species with HMBPP, a pi/sigma metallacycle or nu2-alkenyl complex, overview
H124A
-
site-directed mutagenesis, the mutant shows an increased Km and a 5fold decreased Vmax compared to the wild-type enzyme
H42A
-
site-directed mutagenesis, the mutant shows a decreased Vmax but unaltered Km compared to the wild-type enzyme
E126Q
-
inactive mutant used to trap a paramagnetic reaction intermediate representing the 3-CH2OH-rotated weak pi-complex, intermediate II
H145P
site-directed mutagenesis, the mutant retains activity, complementation of two hdr mutants, including Escherichia coli DLYT1 strains and osisph1 rice plants
H145P/K407R
site-directed mutagenesis, inactive mutant, no complementation of two hdr mutants, including Escherichia coli DLYT1 strains and osisph1 rice plants
K407R
site-directed mutagenesis, the mutant retains activity, complementation of two hdr mutants, including Escherichia coli DLYT1 strains and osisph1 rice plants
additional information
additional information
-
albino mutant clb6-1 contains a null mutant allele of the enzyme
additional information
construction of genomic HDR transgene-induced gene-silencing lines showing an albino, variegated, or pale green phenotype, overview. The cotyledons of T4 seedlings are pale green, light yellow, or albino, indicating that the bleaching phenotype of these lines occurs earlier and is more severe than in previous generations
additional information
-
using different expression cassettes it is shown that the N-terminal bipartite sequence is required for targeting proteins to the apicoplast lumen
additional information
simple overexpression of IspG (EC 1.17.7.3) and IspH does not increase the flux towards terpenoids via the MEP pathway
additional information
elucidation of the prenyl donor substrate of lycopene elongase from Corynebacterium glutamicum, by constructing a flavuxanthin-producing Escherichia coli strain that also possesses the exogenous mevalonate (MVA) pathway, which enables the inhibition of the endogenous MEP pathway. In addition, the effect of the overexpression of HMBPP reductase on carotenogenesis is investigated and the ability of HMBPP to act as a substrate for (all-E)-prenyl diphosphate synthases is evaluated. (all-E)-Prenyl diphosphate synthases utilize DMAPP as a proper substrate and are known to catalyze the carbocation-involving prenyltransfer reaction (e.g. Geobacillus stearothermophilus FPS, Sulfolobus acidocaldarius GGPS, and Aeropyrus pernix (all-E)-geranylfarnesyl diphosphate synthase (GFPS)), detailed overview. HMBPP, which is depleted by the inhibition of the MEP pathway, is utilized as the prenyl donor substrate by Corynebacterium glutamicum lycopene elongase
additional information
-
simple overexpression of IspG (EC 1.17.7.3) and IspH does not increase the flux towards terpenoids via the MEP pathway
-
additional information
-
elucidation of the prenyl donor substrate of lycopene elongase from Corynebacterium glutamicum, by constructing a flavuxanthin-producing Escherichia coli strain that also possesses the exogenous mevalonate (MVA) pathway, which enables the inhibition of the endogenous MEP pathway. In addition, the effect of the overexpression of HMBPP reductase on carotenogenesis is investigated and the ability of HMBPP to act as a substrate for (all-E)-prenyl diphosphate synthases is evaluated. (all-E)-Prenyl diphosphate synthases utilize DMAPP as a proper substrate and are known to catalyze the carbocation-involving prenyltransfer reaction (e.g. Geobacillus stearothermophilus FPS, Sulfolobus acidocaldarius GGPS, and Aeropyrus pernix (all-E)-geranylfarnesyl diphosphate synthase (GFPS)), detailed overview. HMBPP, which is depleted by the inhibition of the MEP pathway, is utilized as the prenyl donor substrate by Corynebacterium glutamicum lycopene elongase
-
additional information
a T-DNA inserted knockout mutant, osisph1, shows an albino phenotype, indicating that OsIspH1 is the only functional gene, genotyping and mutant phenotypes in the different tissues, overview
additional information
recombinant overexpression of the enzyme leads to increased tanshinone content in SmHDR1 transgenic hairy roots, overview. The total levels of all three tanshinones are 0.70 to 1.04fold higher in the H lines than in the wild-type
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
IspH is more stable in its closed conformation with a substrate molecule bound to the cluster, compared to its open conformation in solution
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
highly sensitive to O2, 21% remaining activity after incubation in air for 10 min
639340
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, purified enzyme, 20 mM Tris-HCl, pH 8.0, 95% remaining activity after 2 weeks
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged apoprotein from Escherichia coli strain M15, to homogeneity
-
recombinant His-tagged IspH from strain XL-1 Blue by nickel affinity and anion exchange chromatography followed by dialysis, over 99% purity
-
recombinant His-tagged protein from Escherichia coli strain Xl1-Blue, to 95% homogeneity
recombinant His-tagged protein from Escherichia coli strain XL1-Blue, to homogeneity
using Ni-NTA chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning from genomic DNA and expression as His-tagged protein in Escherichia coli strain XL-1 Blue
-
expressed in Escherichia coli as a His-tagged fusion protein
gene HDR, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, functional complementation by SmHDR1 of the Escherichia coli HDR mutant MG1655 ara/ispH, overexpression of SmHDR1 accelerates the biosynthesis of beta-carotene and enhances the production of tanshinones in cultured hairy roots of Salvia miltiorrhiza Bge. f. alba, transformation using Agrobacterium rhizogenes strain ACCC10060
gene HDR, single copy gene, cloning from cDNA and genomic DNA, DNA and amino acid sequence determination and analysis, genetic structure, quantitative RT-PCR enzyme expression analysis. Phylogenetic analysis revealing that exon-intron structure of BbHDR genes does not show clear relation to phylogeny, while its amino acid sequence reflects phyla and classes well, phylogenetic tree. Introduction of BbHDR cDNA into an Escherichia coli HDR-deficient mutant results in recovery of its auxotrophy, recombinant enzyme expression in HDR-null Escherichia coli strain MG1655
gene HsHDR1, DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene HsHDR2, DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene ispH, cloning from leaves cDNA, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, recombinant expression in Escherichia coli strain BL21
gene ispH, expression as His-tagged protein in Escherichia coli strain XL1-Blue, construction of a synthetic operon containing ispH, ispG and gepE
gene ispH, overexpression of HMBPP reductase in an engineered flavuxanthin-producing Escherichia coli strain
gene ispH, quantitative real-time PCR enzyme expression analysis, transcriptome analysis
-
gene ispH, the IspH domain of the Arabidopsis thaliana enzyme HDR corresponding to the full-length IspH of Escherichia coli fails to complement the Escherichia coli ispH mutant
gene ispH1, sequence comparisons and phylogenetic analysis and tree, genetic structures of isozyme genes, isozyme expression analysis, recombinant expression of wild-type and mutant isozyme OsIspH1 in Escherichia coli strain DLYT1 and in Oryza sativa mutant osisph1 plants via Agrobacterium tumefaciens strain LBA4404 transformation method
gene lytB, expression as His-tagged enzyme in Escherichia coli strain XL1-Blue
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is induced by methyl jasmonate reaching the highest level after 1 h
expression of gene SmHDR1 is induced by 0.1 mM methyl-jasmonate and salicylic acid, but not by 0.1 mM abscisic acid, in hairy roots
GATA box is involved in light mediated gene regulation of SrHDR in stevia
-
hydrocarbon content is positively correlated with BbHDR expression. Upregulation of BbHDR expression remains within a smaller amplitude
Salinity up-shift (9-18% NaCl) and/or nitrate depletion resulted in an increase of DsHDR steady-state mRNA, 36 h upon the stress onset
up-regulated preceding and during the increase in monoterpenol precursor volatile organic compounds (PVOCs)
-
hydrocarbon content is positively correlated with BbHDR expression. Upregulation of BbHDR expression remains within a smaller amplitude
hydrocarbon content is positively correlated with BbHDR expression. Upregulation of BbHDR expression remains within a smaller amplitude
-
-
Salinity up-shift (9-18% NaCl) and/or nitrate depletion resulted in an increase of DsHDR steady-state mRNA, 36 h upon the stress onset
Salinity up-shift (9-18% NaCl) and/or nitrate depletion resulted in an increase of DsHDR steady-state mRNA, 36 h upon the stress onset
-
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
reconstitution of purified apoenzyme with prosthetic group [Fe4-S4] cluster
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biofuel production
synthesis
-
recombinant expression of enzyme can be greatly enhanced by coexpression of genes from the isc operon which are required for the assembly of iron-sulfur clusters
biofuel production
the B race of a green microalga Botryococcus braunii Kützing produces triterpene hydrocarbons that is a promising source for biofuel. In this algal race, precursors of triterpene hydrocarbons are provided from the 2-C-methyl-d-erythritol 4-phosphate (MEP) pathway
biofuel production
-
the B race of a green microalga Botryococcus braunii Kützing produces triterpene hydrocarbons that is a promising source for biofuel. In this algal race, precursors of triterpene hydrocarbons are provided from the 2-C-methyl-d-erythritol 4-phosphate (MEP) pathway
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rohdich, F.; Hecht, S.; Grtner, K.; Adam, P.; Krieger, C.; Amslinger, S.; Arigoni, D.; Bacher, A.; Eisenreich, W.
Studies on the nonmevalonate terpene biosynthetic pathway: Metabolic role of IspH (LytB) protein
Proc. Natl. Acad. Sci. USA
99
1158-1163
2002
Escherichia coli (P62623)
brenda
Hintz, M.; Reichenberg, A.; Altincicek, B.; Bahr, U.; Gschwind, R.M.; Kollas, A.K.; Beck, E.; Wiesner, J.; Eberl, M.; Jomaa, H.
Identification of (E)-4-hydroxy-3-methyl-but-2-enyl pyrophosphate as a major activator for human gd T cells in Escherichia coli
FEBS Lett.
509
317-322
2001
Escherichia coli
brenda
Charon, L.; Pale-Grosdemange, C.; Rohmer, M.
On the reduction steps in the mevalonate independent 2-C-methyl-D-erythritol 4-phosphate (MEP) pathway for isoprenoid biosynthesis in the bacterium Zymomonas mobilis
Tetrahedron Lett.
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1999
Zymomonas mobilis
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Altincicek, B.; Duin, E.C.; Reichenberg, A.; Hedderich, R.; Kollas, A.K.; Hintz, M.; Wagner, S.; Wiesner, J.; Beck, E.; Jomaa, H.
LytB protein catalyzes the terminal step of the 2-C-methyl-D-erythritol-4-phosphate pathway of isoprenoid biosynthesis
FEBS Lett.
532
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2002
Aquifex aeolicus (O67625)
brenda
Wolff, M.; Seemann, M.; Tse Sum Bui, B.; Frapart, Y.; Tritsch, D.; Estrabot, A.G.; Rodriguez-Concepcion, M.; Boronat, A.; Marquet, A.; Rohmer, M.
Isoprenoid biosynthesis via the methylerythritol phosphate pathway: the (E)-4-hydroxy-3-methylbut-2-enyl diphosphate reductase (LytB/IspH) from Escherichia coli is a [4Fe-4S] protein
FEBS Lett.
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Escherichia coli
brenda
Graewert, T.; Kaiser, J.; Zepeck, F.; Laupitz, R.; Hecht, S.; Amslinger, S.; Schramek, N.; Schleicher, E.; Weber, S.; Haslbeck, M.; Buchner, J.; Rieder, C.; Arigoni, D.; Bacher, A.; Eisenreich, W.; Rohdich, F.
IspH protein of Escherichia coli: studies on iron-sulfur cluster implementation and catalysis
J. Am. Chem. Soc.
126
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2004
Escherichia coli
brenda
Botella-Pavia, P.; Besumbes, O.; Phillips, M.A.; Carretero-Paulet, L.; Boronat, A.; Rodriguez-Concepcion, M.
Regulation of carotenoid biosynthesis in plants: Evidence for a key role of hydroxymethylbutenyl diphosphate reductase in controlling the supply of plastidial isoprenoid precursors
Plant J.
40
188-199
2004
Solanum lycopersicum
brenda
Guevara-Garcia, A.; San Roman, C.; Arroyo, A.; Cortes, M.E.; De la Luz Gutierrez-Nava, M.; Leon, P.
Characterization of the Arabidopsis clb6 mutant illustrates the importance of posttranscriptional regulation of the methyl-D-erythritol 4-phosphate pathway
Plant Cell
17
628-643
2005
Arabidopsis thaliana
brenda
Tritsch, D.; Hemmerlin, A.; Bach, T.J.; Rohmer, M.
Plant isoprenoid biosynthesis via the MEP pathway: In vivo IPP/DMAPP ratio produced by (E)-4-hydroxy-3-methylbut-2-enyl diphosphate reductase in tobacco BY-2 cell cultures
FEBS Lett.
584
129-134
2010
Nicotiana tabacum
brenda
Ramos, A.A.; Marques, A.R.; Rodrigues, M.; Henriques, N.; Baumgartner, A.; Castilho, R.; Brenig, B.; Varela, J.C.
Molecular and functional characterization of a cDNA encoding 4-hydroxy-3-methylbut-2-enyl diphosphate reductase from Dunaliella salina
J. Plant Physiol.
166
968-977
2009
Dunaliella salina (C5H8E3), Dunaliella salina, Dunaliella salina CCAP 19/30 (C5H8E3)
brenda
Wang, K.; Wang, W.; No, J.H.; Zhang, Y.; Zhang, Y.; Oldfield, E.
Inhibition of the Fe(4)S(4)-cluster-containing protein IspH (LytB): electron paramagnetic resonance, metallacycles, and mechanisms
J. Am. Chem. Soc.
132
6719-6727
2010
Aquifex aeolicus
brenda
Wang, W.; Li, J.; Wang, K.; Smirnova, T.I.; Oldfield, E.
Pyridine inhibitor binding to the 4Fe-4S protein A. aeolicus IspH (LytB): a HYSCORE Investigation
J. Am. Chem. Soc.
133
6525-6528
2011
Aquifex aeolicus
brenda
Graewert, T.; Span, I.; Eisenreich, W.; Rohdich, F.; Eppinger, J.; Bacher, A.; Groll, M.
Probing the reaction mechanism of IspH protein by x-ray structure analysis
Proc. Natl. Acad. Sci. USA
107
1077-1081
2010
Escherichia coli
brenda
Wang, W.; Wang, K.; Liu, Y.; No, J.; Li, J.; Nilges, M.; Oldfield, E.
Bioorganometallic mechanism of action, and inhibition, of IspH
Proc. Natl. Acad. Sci. USA
107
4522-4527
2010
Aquifex aeolicus, no activity in Homo sapiens
brenda
Rekittke, I.; Olkhova, E.; Wiesner, J.; Demmer, U.; Warkentin, E.; Jomaa, H.; Ermler, U.
Structure of the (E)-4-hydroxy-3-methyl-but-2-enyl-diphosphate reductase from Plasmodium falciparum
FEBS Lett.
587
3968-3972
2013
Plasmodium falciparum (Q9BJX6)
brenda
Kumar, H.; Kumar, S.
A functional (E)-4-hydroxy-3-methylbut-2-enyl diphosphate reductase exhibits diurnal regulation of expression in Stevia rebaudiana (Bertoni)
Gene
527
332-338
2013
Stevia rebaudiana
brenda
Wang, W.; Wang, K.; Span, I.; Jauch, J.; Bacher, A.; Groll, M.; Oldfield, E.
Are free radicals involved in IspH catalysis? An EPR and crystallographic investigation
J. Am. Chem. Soc.
134
11225-11234
2012
Escherichia coli
brenda
Janthawornpong, K.; Krasutsky, S.; Chaignon, P.; Rohmer, M.; Poulter, C.D.; Seemann, M.
Inhibition of IspH, a [4Fe-4S]2+ enzyme involved in the biosynthesis of isoprenoids via the methylerythritol phosphate pathway
J. Am. Chem. Soc.
135
1816-1822
2013
Escherichia coli
brenda
Kwon, M.; Shin, B.; Lee, J.; Han, J.; Kim, S.
Characterization of Burkholderia glumae BGR1 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HDR), the terminal enzyme in 2-C-methyl-d-erythritol 4-phosphate (MEP) pathway
J. Korean Soc. Appl. Biol. Chem.
56
35-40
2013
Burkholderia glumae
-
brenda
Caballero, M.C.; Pedroni, M.J.; Palmer, G.H.; Suarez, C.E.; Davitt, C.; Lau, A.O.
Characterization of acyl carrier protein and LytB in Babesia bovis apicoplast
Mol. Biochem. Parasitol.
181
125-133
2012
Babesia bovis
brenda
Martin, D.M.; Chiang, A.; Lund, S.T.; Bohlmann, J.
Biosynthesis of wine aroma: transcript profiles of hydroxymethylbutenyl diphosphate reductase, geranyl diphosphate synthase, and linalool/nerolidol synthase parallel monoterpenol glycoside accumulation in Gewuerztraminer grapes
Planta
236
919-929
2012
Vitis vinifera
brenda
Lv, H.; Zhang, X.; Liao, B.; Liu, W.; He, L.; Song, J.; Sun, C.; Luo, H.; Chen, S.
Cloning and analysis of 1-hydroxy-2-methyl-2-(E)-butenyl-4-diphosphate reductase genes HsHDR1 and HsHDR2 in Huperzia serrate
Acta Pharm. Sin. B
5
583-589
2015
Huperzia serrata (A0A0G3EJZ3), Huperzia serrata (A0A0G3EHB0), Huperzia serrata
brenda
Hao, G.; Shi, R.; Tao, R.; Fang, Q.; Jiang, X.; Ji, H.; Feng, L.; Huang, L.
Cloning, molecular characterization and functional analysis of 1-hydroxy-2-methyl-2-(E)-butenyl-4-diphosphate reductase (HDR) gene for diterpenoid tanshinone biosynthesis in Salvia miltiorrhiza Bge. f. alba
Plant Physiol. Biochem.
70
21-32
2013
Salvia miltiorrhiza f. alba (T1RJ09)
brenda
Hsieh, W.Y.; Sung, T.Y.; Wang, H.T.; Hsieh, M.H.
Functional evidence for the critical amino-terminal conserved domain and key amino acids of Arabidopsis 4-hydroxy-3-methylbut-2-enyl diphosphate reductase
Plant Physiol.
166
57-69
2014
Arabidopsis thaliana (Q94B35)
brenda
Hsieh, W.Y.; Hsieh, M.H.
The amino-terminal conserved domain of 4-hydroxy-3-methylbut-2-enyl diphosphate reductase is critical for its function in oxygen-evolving photosynthetic organisms
Plant Signal. Behav.
10
e988072
2015
Arabidopsis thaliana (Q94B35)
brenda
Cheng, Q.; Tong, Y.; Wang, Z.; Su, P.; Gao, W.; Huang, L.
Molecular cloning and functional identification of a cDNA encoding 4-hydroxy-3-methylbut-2-enyl diphosphate reductase from Tripterygium wilfordii
Acta Pharm. Sin. B
7
208-214
2017
Tripterygium wilfordii (A0A088GJ08), Tripterygium wilfordii
brenda
Ma, D.; Li, G.; Zhu, Y.; Xie, D.
Overexpression and suppression of Artemisia annua 4-hydroxy-3-methylbut-2-enyl diphosphate reductase 1 gene (AaHDR1) differentially regulate artemisinin and terpenoid biosynthesis
Front. Plant Sci.
8
doi: 10.3389/fpls.2017.00077
2017
Artemisia annua (A0A1V0C086), Artemisia annua
brenda
Shin, B.; Jung, Y.; Kim, S.; Pan, C.
Transformation of the diatom Phaeodactylum tricornutum with its endogenous (E)-4-hydroxy-3-methylbut-2-enyl diphosphate reductase gene
J. Appl. Biol. Chem.
58
273-279
2015
Phaeodactylum tricornutum
-
brenda
Zhang, Z.; Lv, H.; Guo, X.; He, L.; Song, J.; Sun, C.; Luo, H.
Cloning and bioinformatics analysis of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase (PcHDR1) gene in Phlegmarirus carinatus
Zhongguo Zhong Yao Za Zhi
41
4169-4174
2016
Phlegmariurus carinatus (I6TT54), Phlegmariurus carinatus
brenda
Hayashi, Y.; Ito, T.; Yoshimura, T.; Hemmi, H.
Utilization of an intermediate of the methylerythritol phosphate pathway, (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate, as the prenyl donor substrate for various prenyltransferases
Biosci. Biotechnol. Biochem.
82
993-1002
2018
Escherichia coli (P62623), Escherichia coli K12 (P62623)
brenda
Li, D.; Wang, Q.; Chen, S.; Liu, H.; Pan, K.; Li, J.; Luo, C.; Wang, H.
De novo assembly and analysis of Polygonatum cyrtonema Hua and identification of genes involved in polysaccharide and saponin biosynthesis
BMC Genomics
23
195
2022
Polygonatum cyrtonema
brenda
Lee, Y.J.; Kim, J.K.; Baek, S.A.; Yu, J.S.; You, M.K.; Ha, S.H.
Differential regulation of an OsIspH1, the functional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase, for photosynthetic pigment biosynthesis in rice leaves and seeds
Front. Plant Sci.
13
861036
2022
Oryza sativa Japonica Group (Q6AVG6)
brenda
Uchida, H.; Sumimoto, K.; Oki, T.; Nishii, I.; Mizohata, E.; Matsunaga, S.; Okada, S.
Isolation and characterization of 4-hydroxy-3-methylbut-2-enyl diphosphate reductase gene from Botryococcus braunii, race B
J. Plant Res.
131
839-848
2018
Botryococcus braunii (A0A2Z5WA18), Botryococcus braunii Showa (A0A2Z5WA18)
brenda
Volke, D.C.; Rohwer, J.; Fischer, R.; Jennewein, S.
Investigation of the methylerythritol 4-phosphate pathway for microbial terpenoid production through metabolic control analysis
Microb. Cell Fact.
18
192
2019
Escherichia coli (P62623), Escherichia coli K12 (P62623)
brenda
Shailaja, A.; Srinath, M.; Bindu, B.V.B.; Giri, C.C.
Isolation of 4-hydroxy 3-methyl 2-butenyl 4-diphosphate reductase (ApHDR) gene of methyl erythritol diphosphate (MEP) pathway, in silico analysis and differential tissue specific ApHDR expression in Andrographis paniculata (Burm. f) Nees
Physiol. Mol. Biol. Plants
27
223-235
2021
Andrographis paniculata (A0A5C0PY82)
brenda
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