The Enzyme Database

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EC 1.14.11.41     
Accepted name: L-arginine hydroxylase
Reaction: L-arginine + 2-oxoglutarate + O2 = (3S)-3-hydroxy-L-arginine + succinate + CO2
Other name(s): VioC (ambiguous); L-arginine,2-oxoglutarate:O2 oxidoreductase (3-hydroxylating)
Systematic name: L-arginine,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Comments: 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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ju, J., Ozanick, S.G., Shen, B. and 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 (2004) 1281–1285. [PMID: 15368582]
2.  Helmetag, V., Samel, S.A., Thomas, M.G., Marahiel, M.A. and Essen, L.O. Structural basis for the erythro-stereospecificity of the L-arginine oxygenase VioC in viomycin biosynthesis. FEBS J. 276 (2009) 3669–3682. [PMID: 19490124]
[EC 1.14.11.41 created 2013]
 
 


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