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Information on EC 1.14.11.55 - ectoine hydroxylase
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1.14.11.55 ectoine hydroxylaseIUBMB Comments
Requires Fe2+ and ascorbate. The enzyme, found in bacteria, is specific for ectoine.
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Word Map
- 1.14.11.55
-
2-oxoglutarate-dependent
-
halophil
- 5-hydroxyectoine
-
halomonas
- salexigens
-
ironii
-
non-heme-containing
- hydroxylases
- alaskensis
-
sphingopyxis
- elongata
-
stereo-specific
-
osmostress
-
mechanosensitive
-
tetrahydropyrimidine
-
ectabc
- stutzeri
-
osmolarity
-
virgibacillus
-
co-substrate
-
halotolerant
- maritimus
-
chassis
- salina
-
region-selective
-
thermoregulated
- nitrosopumilus
-
chromohalobacter
-
thermoprotection
-
alkaliphilic
- hydrothermalis
-
sitting-drop
- synthesis
-
extremophiles
-
prop
-
apo-form
-
monosodium
The enzyme appears in viruses and cellular organisms
Synonyms
ectoine hydroxylase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Csal_3003
ectD
EctE
ectoine dioxygenase
-
-
-
-
HELO_4008
REctD
Sala_2952
SCATT_10620
ectD
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ectoine + 2-oxoglutarate + O2 = 5-hydroxyectoine + succinate + CO2
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
ectoine,2-oxoglutarate:oxygen oxidoreductase (5-hydroxylating)
Requires Fe2+ and ascorbate. The enzyme, found in bacteria, is specific for ectoine.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(4S)-ectoine + 2-oxoglutarate + O2
(4S,5S)-5-hydroxyectoine + succinate + CO2
-
-
-
?
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
?
-
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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(4S)-ectoine + 2-oxoglutarate + O2
(4S,5S)-5-hydroxyectoine + succinate + CO2
-
-
-
?
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.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Iron
KCl
NaCl
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
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
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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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.2
2-oxoglutarate
-
pH not specified in the publication, temperature not specified in the publication
2.6
ectoine
-
pH not specified in the publication, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
-
pH not specified in the publication, temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE