Information on EC 1.14.11.B11 - L-asparagine hydroxylase

for references in articles please use BRENDA:EC1.14.11.B11
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The expected taxonomic range for this enzyme is: Streptomyces coelicolor

EC NUMBER
COMMENTARY hide
1.14.11.B11
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
L-asparagine hydroxylase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-asparagine + 2-oxoglutarate + O2 = (2S,3S)-3-hydroxyasparagine + succinate + CO2
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
L-asparagine,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
synonym Streptomyces violaceoruber NBRC 15146
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-asparagine + 2-oxoglutarate + O2
(2S,3S)-3-hydroxyasparagine + succinate + CO2
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-asparagine + 2-oxoglutarate + O2
(2S,3S)-3-hydroxyasparagine + succinate + CO2
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.479
L-asparagine
pH 7.5, 25C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.98
L-asparagine
pH 7.5, 25C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10.3
L-asparagine
pH 7.5, 25C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystals of AsnO are grown at 18C 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
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni affinity column chromatography, and Superdex 200 gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Rosetta2(DE3) cells
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expression in Escherichia coli BL21
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D241N
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the mutant shows low activity compared to the wild type enzyme
D246N
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the mutant shows low activity compared to the wild type enzyme
D241N
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the mutant shows low activity compared to the wild type enzyme
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D246N
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the mutant shows low activity compared to the wild type enzyme
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