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Information on EC 1.14.11.41 - L-arginine 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
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L-arginine + 2-oxoglutarate + O2 = (3S)-3-hydroxy-L-arginine + succinate + CO2
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ethylene biosynthesis II (microbes)
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L-arginine,2-oxoglutarate:O2 oxidoreductase (3-hydroxylating)
Fe2+-dependent enzyme. The enzyme is involved in the biosynthesis of the cyclic pentapeptide antibiotic viomycin. It differs from EC 1.14.11.34, 2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming), because it does not form guanidine and (S)-1-pyrroline-5-carboxylate from 3-hydroxy-L-arginine.
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VioC
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brenda
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UniProt
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physiological function
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the enzyme is involved in the biosynthesis of viomycin (an antibiotic of the tuberactinomycin family)
physiological function
the enzyme is involved in the biosynthesis of the tuberactinomycin antibiotic viomycin
physiological function
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the enzyme is involved in the biosynthesis of viomycin (an antibiotic of the tuberactinomycin family)
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L-arginine + 2-oxoglutarate + O2
(3S)-3-hydroxy-L-arginine + succinate + CO2
L-canavanine + 2-oxoglutarate + O2
? + succinate + CO2
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L-homoarginine + 2-oxoglutarate + O2
(3S)-N6-(diaminomethylidene)-3-hydroxy-L-lysine + succinate + CO2
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additional information
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no activity with D-arginine, NG-methyl-L-arginine, NG-hydroxynor-L-arginine
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L-arginine + 2-oxoglutarate + O2
(3S)-3-hydroxy-L-arginine + succinate + CO2
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?
L-arginine + 2-oxoglutarate + O2
(3S)-3-hydroxy-L-arginine + succinate + CO2
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L-arginine + 2-oxoglutarate + O2
(3S)-3-hydroxy-L-arginine + succinate + CO2
L-arginine is the preferred substrate
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?
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Fe2+
Fe2+-dependent enzyme
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3.4
L-arginine
pH 8.0, 30°C
1.16
L-canavanine
pH 8.0, 30°C
7.05
L-homoarginine
pH 8.0, 30°C
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43.5
L-arginine
pH 8.0, 30°C
1.22
L-canavanine
pH 8.0, 30°C
13.85
L-homoarginine
pH 8.0, 30°C
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12.8
L-arginine
pH 8.0, 30°C
1.05
L-canavanine
pH 8.0, 30°C
1.96
L-homoarginine
pH 8.0, 30°C
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41600
x * 41600, SDS-PAGE
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sitting drop vapor-diffusion method. The crystal structures of VioC are determined in complexes with the cofactor Fe(II), the substrate L-arginine, the product (2S,3S)-hydroxyarginine and the coproduct succinate at 1.1–1.3 A resolution
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expressed as a fusion protein with an N-terminal hexahistidine tag in Escherichia coli BL21(DE3)
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expression in Escherichia coli BL21
overexpression in Escherichia coli with an N-terminal hexahistidine affinity tag
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ARGHX_STRVI
358
39427
Swiss-Prot
ORR3O_CATAD
Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897)
343
39116
Swiss-Prot
A0A1D8G7S3_9ACTN
358
39456
TrEMBL
A0A0U5HI29_STRRE
358
38290
TrEMBL
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Ju, J.; Ozanick, S.G.; Shen, B.; Thomas, M.,G.
Conversion of (2S)-arginine to (2S,3R)-capreomycidine by VioC and VioD from the viomycin biosynthetic pathway of Streptomyces sp. strain ATCC11861
Chembiochem
5
1281-1285
2004
Streptomyces sp., Streptomyces sp. ATCC 11861
brenda
Helmetag, V.; Samel, S.A.; Thomas, M.G.; Marahiel, M.A.; Essen, L.O.
Structural basis for the erythro-stereospecificity of the L-arginine oxygenase VioC in viomycin biosynthesis
FEBS J.
276
3669-3682
2009
Streptomyces vinaceus (Q6WZB0)
brenda
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