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Information on EC 1.14.11.B11 - L-asparagine hydroxylase Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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The expected taxonomic range for this enzyme is: Streptomyces coelicolor
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1.14.11.B11
preliminary BRENDA-supplied EC number
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L-asparagine hydroxylase
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L-asparagine + 2-oxoglutarate + O2 = (2S,3S)-3-hydroxyasparagine + succinate + CO2
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L-asparagine,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
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AsnO
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SwissProt
brenda
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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
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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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L-asparagine + 2-oxoglutarate + O2
(2S,3S)-3-hydroxyasparagine + succinate + CO2
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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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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L-asparagine + 2-oxoglutarate + O2
(2S,3S)-3-hydroxyasparagine + succinate + CO2
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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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L-asparagine + 2-oxoglutarate + O2
(2S,3S)-3-hydroxyasparagine + succinate + CO2
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
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-
?
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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Fe2+
no activity without Fe2+
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0.479
L-asparagine
pH 7.5, 25°C
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4.98
L-asparagine
pH 7.5, 25°C
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10.3
L-asparagine
pH 7.5, 25°C
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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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expression in Escherichia coli BL21
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Strieker, M.; Kopp, F.; Mahlert, C.; Essen, L.O.; Marahiel, M.A.
Mechanistic and structural basis of stereospecific Cbeta-hydroxylation in calcium-dependent antibiotic, a daptomycin-type lipopeptide
ACS Chem. Biol.
2
187-196
2007
Streptomyces coelicolor (Q9Z4Z5)
brenda
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