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Enzyme Nomenclature
Information on EC 1.14.11.B11 - L-asparagine hydroxylase
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The expected taxonomic range for this enzyme is: Streptomyces coelicolor
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EC NUMBER 
COMMENTARY 
1.14.11.B11
preliminary BRENDA-supplied EC number
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RECOMMENDED NAME
GeneOntology No.
L-asparagine hydroxylase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-asparagine + 2-oxoglutarate + O2 = (2S,3S)-3-hydroxyasparagine + succinate + CO2
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-
-
-
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SYSTEMATIC NAME
IUBMB Comments
L-asparagine,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
the enzyme is involved in the biosynthesis of (2S,3S)-3-hydroxyasparagine, a component of the lipopeptide lactone calcium-dependent antibiotic
physiological function
-
the enzyme is involved in the biosynthesis of (2S,3S)-3-hydroxyasparagine, a component of the lipopeptide lactone calcium-dependent antibiotic
-
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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
L-asparagine + 2-oxoglutarate + O2
(2S,3S)-3-hydroxyasparagine + succinate + CO2
the enzyme is involved in the biosynthesis of (2S,3S)-3-hydroxyasparagine, a component of the lipopeptide lactone calcium-dependent antibiotic
-
-
?
L-asparagine + 2-oxoglutarate + O2
(2S,3S)-3-hydroxyasparagine + succinate + CO2
in presence of Fe2+ and 2-oxoglutarate, hydroxylation activity is observed exclusively with the L-enantiomer of the free amino acid
-
-
?
L-asparagine + 2-oxoglutarate + O2
(2S,3S)-3-hydroxyasparagine + succinate + CO2
-
the enzyme is involved in the biosynthesis of (2S,3S)-3-hydroxyasparagine, a component of the lipopeptide lactone calcium-dependent antibiotic
-
-
?
L-asparagine + 2-oxoglutarate + O2
(2S,3S)-3-hydroxyasparagine + succinate + CO2
-
in presence of Fe2+ and 2-oxoglutarate, hydroxylation activity is observed exclusively with the L-enantiomer of the free amino acid
-
-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
L-asparagine + 2-oxoglutarate + O2
(2S,3S)-3-hydroxyasparagine + succinate + CO2
Q9Z4Z5
the enzyme is involved in the biosynthesis of (2S,3S)-3-hydroxyasparagine, a component of the lipopeptide lactone calcium-dependent antibiotic
-
-
?
L-asparagine + 2-oxoglutarate + O2
(2S,3S)-3-hydroxyasparagine + succinate + CO2
-
the enzyme is involved in the biosynthesis of (2S,3S)-3-hydroxyasparagine, a component of the lipopeptide lactone calcium-dependent antibiotic
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystals of AsnO are grown at 18°C by the sitting-drop vapor diffusion method. 1.45, 1.92, and 1.66 A crystal structures of AsnO as apoprotein, Fe2+ complex, and product complex, respectively, with (2S,3S)-3-hydroxyasparagine and succinate
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.11.B11)
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