EC 1.14.11.41 - L-arginine hydroxylase

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IntEnz Enzyme Nomenclature
EC 1.14.11.41

Names

Accepted name:
L-arginine hydroxylase
Other name:
VioC [ambiguous]
Systematic name:
L-arginine,2-oxoglutarate:O2 oxidoreductase (3-hydroxylating)

Reaction

Cofactor

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0102525
UniProtKB/Swiss-Prot:

References

  1. 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). [PMID: 15368582]
  2. 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). [PMID: 19490124]

[EC 1.14.11.41 created 2013]