| Entry |
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| Name |
L-arginine hydroxylase;
VioC (ambiguous);
L-arginine,2-oxoglutarate:O2 oxidoreductase (3-hydroxylating)
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| Class |
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
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| Sysname |
L-arginine,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
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| Reaction(IUBMB) |
L-arginine + 2-oxoglutarate + O2 = (3S)-3-hydroxy-L-arginine + succinate + CO2 [RN: R09363]
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| Reaction(KEGG) |
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| Substrate |
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| Product |
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| Comment |
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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| History |
EC 1.14.11.41 created 2013
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| Orthology |
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| Reference |
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| Authors |
Ju J, Ozanick SG, Shen B, Thomas MG. |
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| Title |
Conversion of (2S)-arginine to (2S,3R)-capreomycidine by VioC and VioD from the viomycin biosynthetic pathway of Streptomyces sp. strain ATCC11861. |
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| Journal |
Chembiochem. 5 (2004) 1281-5. |
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| Sequence |
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| Reference |
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| Authors |
Helmetag V, Samel SA, Thomas MG, Marahiel MA, Essen LO. |
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| Title |
Structural basis for the erythro-stereospecificity of the L-arginine oxygenase VioC in viomycin biosynthesis. |
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| Journal |
FEBS. J. 276 (2009) 3669-82. |
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| Sequence |
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| Other DBs |
ExplorEnz - The Enzyme Database: IUBMB Enzyme Nomenclature: ExPASy - ENZYME nomenclature database: BRENDA, the Enzyme Database: |
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| LinkDB |
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