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(4S)-ectoine + 2-oxoglutarate + O2
(4S,5S)-5-hydroxyectoine + succinate + CO2
-
-
-
?
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
L-homoectoine + 2-oxoglutarate + O2
trans-5-hydroxy-L-homoectoine + succinate + CO2
L-proline + 2-oxoglutarate + O2
trans-3-hydroxyproline + succinate + CO2
additional information
?
-
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
JN019030
-
-
-
ir
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
JN019031
-
-
-
ir
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
-
-
-
?
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
-
-
-
ir
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
-
-
-
ir
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
-
-
-
?
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
-
-
-
-
?
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
-
-
-
ir
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
-
-
-
-
ir
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
-
-
-
-
ir
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
-
-
-
?
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
-
-
-
-
?
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
-
-
-
ir
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
-
-
-
?
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
-
-
-
ir
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
-
-
-
?
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
-
-
-
?
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
-
-
-
?
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
-
-
-
?
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
-
-
-
-
?
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
-
-
-
-
?
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
Stutzerimonas stutzeri
-
-
-
?
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
Stutzerimonas stutzeri A1501
-
-
-
?
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
-
-
-
ir
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
-
-
-
ir
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
-
-
-
?
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
-
-
-
ir
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
-
reaction is dependent on iron(II), molecular oxygen, and 2-oxoglutarate
-
?
L-homoectoine + 2-oxoglutarate + O2
trans-5-hydroxy-L-homoectoine + succinate + CO2
-
-
-
?
L-homoectoine + 2-oxoglutarate + O2
trans-5-hydroxy-L-homoectoine + succinate + CO2
-
-
-
?
L-homoectoine + 2-oxoglutarate + O2
trans-5-hydroxy-L-homoectoine + succinate + CO2
Stutzerimonas stutzeri
-
-
-
?
L-homoectoine + 2-oxoglutarate + O2
trans-5-hydroxy-L-homoectoine + succinate + CO2
Stutzerimonas stutzeri A1501
-
-
-
?
L-proline + 2-oxoglutarate + O2
trans-3-hydroxyproline + succinate + CO2
-
-
-
?
L-proline + 2-oxoglutarate + O2
trans-3-hydroxyproline + succinate + CO2
-
-
-
?
L-proline + 2-oxoglutarate + O2
trans-3-hydroxyproline + succinate + CO2
-
-
-
?
L-proline + 2-oxoglutarate + O2
trans-3-hydroxyproline + succinate + CO2
-
-
-
?
additional information
?
-
JN019030
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
-
-
?
additional information
?
-
JN019031
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
-
-
?
additional information
?
-
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
-
-
?
additional information
?
-
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
-
-
?
additional information
?
-
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
-
-
?
additional information
?
-
-
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
-
-
?
additional information
?
-
-
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
-
-
?
additional information
?
-
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
-
-
?
additional information
?
-
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
-
-
?
additional information
?
-
-
no substrate: L-proline
-
-
?
additional information
?
-
-
no substrate: L-proline
-
-
?
additional information
?
-
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
-
-
?
additional information
?
-
-
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
-
-
?
additional information
?
-
the cosubstrate 2-oxoglutarate is stoichiometrically decarboxylated during the hydroxylation of the substrate ectoine. CO2 is thereby liberated from 2-oxoglutarate to form succinate. During the hydroxylation reaction, one atom of the atmospheric oxygen molecule is incorporated into succinate, whereas the other atom is incorporated into the hydroxy group formed on ectoine
-
-
?
additional information
?
-
-
the cosubstrate 2-oxoglutarate is stoichiometrically decarboxylated during the hydroxylation of the substrate ectoine. CO2 is thereby liberated from 2-oxoglutarate to form succinate. During the hydroxylation reaction, one atom of the atmospheric oxygen molecule is incorporated into succinate, whereas the other atom is incorporated into the hydroxy group formed on ectoine
-
-
?
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(4S)-ectoine + 2-oxoglutarate + O2
(4S,5S)-5-hydroxyectoine + succinate + CO2
-
-
-
?
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
additional information
?
-
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
JN019030
-
-
-
ir
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
JN019031
-
-
-
ir
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
-
-
-
ir
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
-
-
-
ir
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
-
-
-
-
?
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
-
-
-
ir
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
-
-
-
-
ir
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
-
-
-
-
ir
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
-
-
-
ir
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
-
-
-
ir
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
-
-
-
ir
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
-
-
-
ir
ectoine + 2-oxoglutarate + O2
5-hydroxyectoine + succinate + CO2
-
-
-
ir
additional information
?
-
JN019030
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
-
-
?
additional information
?
-
JN019031
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
-
-
?
additional information
?
-
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
-
-
?
additional information
?
-
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
-
-
?
additional information
?
-
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
-
-
?
additional information
?
-
-
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
-
-
?
additional information
?
-
-
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
-
-
?
additional information
?
-
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
-
-
?
additional information
?
-
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
-
-
?
additional information
?
-
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
-
-
?
additional information
?
-
-
ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Fe2+
-
stimulation at 1 mM, inhibitory above
Fe2+
presence of Fe2+ is required
Iron
JN019030
the iron ligand is bound via interaction with histidine side-chains His146 and His248, and the side-chain of Asp-148. These residues form a conserved H6D/E
H motif, the so-called 2-His-1-carboxylate facial triad
Iron
JN019031
the iron ligand is bound via interaction with histidine side-chains His146 and His248, and the side-chain of Asp-148. These residues form a conserved H6D/E
H motif, the so-called 2-His-1-carboxylate facial triad
Iron
the iron ligand is bound via interaction with histidine side-chains His146 and His248, and the side-chain of Asp-148. These residues form a conserved H6D/E
H motif, the so-called 2-His-1-carboxylate facial triad
Iron
the iron ligand is bound via interaction with histidine side-chains His146 and His248, and the side-chain of Asp-148. These residues form a conserved H6D/E
H motif, the so-called 2-His-1-carboxylate facial triad
Iron
-
the iron ligand is bound via interaction with histidine side-chains His146 and His248, and the side-chain of Asp-148. These residues form a conserved H6D/E
H motif, the so-called 2-His-1-carboxylate facial triad
Iron
0.12-0.14 mol per mol of enzyme
Iron
the iron ligand is bound via interaction with histidine side-chains His146 and His248, and the side-chain of Asp-148. These residues form a conserved H6D/E
H motif, the so-called 2-His-1-carboxylate facial triad
Iron
the iron ligand is bound via interaction with histidine side-chains His146 and His248, and the side-chain of Asp-148. These residues form a conserved H6D/E
H motif, the so-called 2-His-1-carboxylate facial triad
KCl
JN019030
maximum activity in presence of 100 mM KCl
KCl
JN019031
maximum activity in presence of 150 mM KCl
KCl
maximum activity in presence of 150 mM KCl
KCl
maximum activity in presence of 200 mM KCl
KCl
-
maximum activity in presence of 150 mM KCl
KCl
maximum activity in presence of 100 mM KCl
KCl
maximum activity in presence of 150 mM KCl
NaCl
JN019030
maximum activity in presence of 50 mM KCl. High concentrations of NaCl are inhibitory
NaCl
JN019031
maximum activity in presence of 150 mM KCl. High concentrations of NaCl are inhibitory
NaCl
maximum activity in presence of 100 mM KCl. High concentrations of NaCl are inhibitory
NaCl
maximum activity in presence of 150 mM KCl. High concentrations of NaCl are inhibitory
NaCl
-
maximum activity in presence of 100 mM KCl. High concentrations of NaCl are inhibitory
NaCl
maximum activity in presence of 100 mM KCl. High concentrations of NaCl are inhibitory
NaCl
maximum activity in presence of 100 mM KCl. High concentrations of NaCl are inhibitory
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E140A
residue involved in dimerization, activity similar to wild-type
Q127A
residue involved in ectoine binding, about 1% of wild-type activity
R139A
residue involved in dimerization, activity similar to wild-type
R139A/E140A
residues involved in dimerization, activity similar to wild-type
R280A
residue involved in ectoine binding, about 8% of wild-type activity
T149A
residue involved in ectoine binding, about 4% of wild-type activity
W150A
residue involved in ectoine binding, about 2% of wild-type activity
E140A
-
residue involved in dimerization, activity similar to wild-type
-
Q127A
-
residue involved in ectoine binding, about 1% of wild-type activity
-
R139A
-
residue involved in dimerization, activity similar to wild-type
-
R280A
-
residue involved in ectoine binding, about 8% of wild-type activity
-
T149A
-
residue involved in ectoine binding, about 4% of wild-type activity
-
A163C
the mutant shows reduced activity compared to the wild type enzyme
A163C
residue is not involved in ligand binding
A163C/S244C
the mutant shows increased activity compared to the wild type enzyme
A163C/S244C
residues are not involved in ligand binding
D148A
inactive
D148A
loss of activity. Residue is involved in binding of Fe2+
D148E
inactive
D148E
loss of activity. Residue is involved in binding of Fe2+
F143A
inactive
F143A
loss of activity. Residue is involved in binding of 2-oxoglutarate
F143W
inactive
F143W
loss of activity. Residue is involved in binding of 2-oxoglutarate
F143Y
inactive
F143Y
loss of activity. Residue is involved in binding of 2-oxoglutarate
F242A
inactive
F242A
loss of activity. Residue is involved in binding of ectoine
F242W
inactive
F242W
loss of activity. Residue is involved in binding of ectoine
F242Y
3fold increase in Km value
F242Y
the mutant shows reduced activity compared to the wild type enzyme
F263A
inactive
F263A
loss of activity. Residue is involved in binding of ectoine
F263W
inactive
F263W
loss of activity. Residue is involved in binding of ectoine
F263Y
the mutant shows reduced activity compared to the wild type enzyme
F263Y
30% increase in Km value
F95A
inactive
F95A
loss of activity. Residue is involved in binding of 2-oxoglutarate
H146A
inactive
H146A
loss of activity. Residue is involved in binding of Fe2+
H248A
inactive
H248A
loss of activity. Residue is involved in binding of Fe2+
N133A
inactive
N133A
loss of activity. Residue is involved in binding of 2-oxoglutarate
N261A
the mutant shows reduced activity compared to the wild type enzyme
N261A
residue is not involved in ligand binding
P198A
the mutant shows reduced activity compared to the wild type enzyme
P198A
activity similar to wild-type, residue of loop region
Q129A
inactive
Q129A
loss of activity. Residue is involved in binding of ectoine
R131A
inactive
R131A
loss of activity. Residue is involved in binding of 2-oxoglutarate
R259A
inactive
R259A
loss of activity. Residue is involved in binding of 2-oxoglutarate
R259H
inactive
R259H
loss of activity. Residue is involved in binding of 2-oxoglutarate
R259K
inactive
R259K
loss of activity. Residue is involved in binding of 2-oxoglutarate
R259Q
inactive
R259Q
loss of activity. Residue is involved in binding of 2-oxoglutarate
S165A
3fold increase in Km value
S165A
the mutant shows reduced activity compared to the wild type enzyme
S167A
the mutant shows about wild type activity
S167A
residue is not involved in ligand binding
S205A
the mutant shows reduced activity compared to the wild type enzyme
S205A
activity similar to wild-type, residue of loop region
S244C
the mutant shows reduced activity compared to the wild type enzyme
S244C
residue is not involved in ligand binding
S250A
inactive
S250A
loss of activity. Residue is involved in binding of 2-oxoglutarate
V265A
the mutant shows reduced activity compared to the wild type enzyme
V265A
residue is not involved in ligand binding
V265L
the mutant shows reduced activity compared to the wild type enzyme
V265L
residue is not involved in ligand binding
V265T
the mutant shows reduced activity compared to the wild type enzyme
V265T
residue is not involved in ligand binding
W152A
inactive
W152A
loss of activity. Residue is involved in binding of ectoine
W152F
inactive
W152F
loss of activity. Residue is involved in binding of ectoine
W152Y
inactive
W152Y
loss of activity. Residue is involved in binding of ectoine
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synthesis
efficient conversion of ectoine to hydroxyectoine in Halomonas elongata by heterologous expression of the ectoine hydroxylase gene, thpD, from Streptomyces anulatus under cotrol of the Hansenula elongata ectA promoter
synthesis
expression of 5-hydroxyectoine biosynthesis enzymes EctA, EctB, EctC, and EctD in Hansenula polymorpha. 5-Hydroxyectoine synthesis in gram per liter scale (2.8 g/l culture supernatant, 365 mol/g dry cell weight) can be achieved, with almost 100% conversion of ectoine to 5-hydroxyectoine without necessity of high salinity
synthesis
Stutzerimonas stutzeri
an Escherichia coli cell factory expressing the Pseudomonas stutzeri ectD gene from a synthetic promoter imports homoectoine via the ProU and ProP compatible solute transporters, hydroxylates it, and secretes the formed trans-5-hydroxyhomoectoine, independent from all currently known mechanosensitive channels, into the growth medium
synthesis
-
effect of medium formulation (i.e., yeast extract (YE) medium and high yeast extract (HYE) medium) on hydroxyectoine production. Hydroxyectoine production is elevated when the high yeast extract medium is utilized. Hydroxyectoine production increases to 2.9 g/l when 50 mM of 2-oxoglutarate and 1 mM of iron are added to the high yeast extract medium
synthesis
-
in an optimized medium containing 100 g/l NaCl in a 500-ml flask, the double mutant lacking EctD and ectoine hydrolaseDoeA synthesizes 3.13 g/l ectoine after 30 h cultivation. Mutants additionally lacking key Na+/H+ antiporter Mrp can synthesize around 7 g/l or 500 mg/(g DCW) in the medium containing lower concentration of NaCl. During a fed-batch fermentation process with 60 g/l NaCl stress, a maximum 10.5 g/l ectoine is accumulated by the Mrp-deficient strain,with a specific production of 765 mg/(g DCW) and a yield of 0.21 g/g monosodium glutamate
synthesis
Stutzerimonas stutzeri A1501
-
an Escherichia coli cell factory expressing the Pseudomonas stutzeri ectD gene from a synthetic promoter imports homoectoine via the ProU and ProP compatible solute transporters, hydroxylates it, and secretes the formed trans-5-hydroxyhomoectoine, independent from all currently known mechanosensitive channels, into the growth medium
-
synthesis
-
in an optimized medium containing 100 g/l NaCl in a 500-ml flask, the double mutant lacking EctD and ectoine hydrolaseDoeA synthesizes 3.13 g/l ectoine after 30 h cultivation. Mutants additionally lacking key Na+/H+ antiporter Mrp can synthesize around 7 g/l or 500 mg/(g DCW) in the medium containing lower concentration of NaCl. During a fed-batch fermentation process with 60 g/l NaCl stress, a maximum 10.5 g/l ectoine is accumulated by the Mrp-deficient strain,with a specific production of 765 mg/(g DCW) and a yield of 0.21 g/g monosodium glutamate
-
synthesis
-
effect of medium formulation (i.e., yeast extract (YE) medium and high yeast extract (HYE) medium) on hydroxyectoine production. Hydroxyectoine production is elevated when the high yeast extract medium is utilized. Hydroxyectoine production increases to 2.9 g/l when 50 mM of 2-oxoglutarate and 1 mM of iron are added to the high yeast extract medium
-
synthesis
-
expression of 5-hydroxyectoine biosynthesis enzymes EctA, EctB, EctC, and EctD in Hansenula polymorpha. 5-Hydroxyectoine synthesis in gram per liter scale (2.8 g/l culture supernatant, 365 mol/g dry cell weight) can be achieved, with almost 100% conversion of ectoine to 5-hydroxyectoine without necessity of high salinity
-
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Hoeppner, A.; Widderich, N.; Bremer, E.; Smits, S.
Overexpression, crystallization and preliminary X-ray crystallographic analysis of the ectoine hydroxylase from Sphingopyxis alaskensis
Acta Crystallogr. Sect. F
70
493-496
2014
Sphingopyxis alaskensis (Q1GNW5), Sphingopyxis alaskensis
brenda
Prabhu, J.; Schauwecker, F.; Grammel, N.; Keller, U.; Bernhard, M.
Functional expression of the ectoine hydroxylase gene (thpD) from Streptomyces chrysomallus in Halomonas elongata
Appl. Environ. Microbiol.
70
3130-3132
2004
Streptomyces anulatus (Q6QUY7), Streptomyces anulatus
brenda
Bursy, J.; Kuhlmann, A.U.; Pittelkow, M.; Hartmann, H.; Jebbar, M.; Pierik, A.J.; Bremer, E.
Synthesis and uptake of the compatible solutes ectoine and 5-hydroxyectoine by Streptomyces coelicolor A3(2) in response to salt and heat stresses
Appl. Environ. Microbiol.
74
7286-7296
2008
Streptomyces coelicolor, Streptomyces coelicolor A3(2)
brenda
Bursy, J.; Pierik, A.J.; Pica, N.; Bremer, E.
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