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 1.14.20.7, 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, PDB |
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. [DOI] [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. [DOI] [PMID: 19490124] |
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[EC 1.14.11.41 created 2013] |
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