KEGG   ENZYME: 1.14.11.41Help
Entry
EC 1.14.11.41               Enzyme                                 

Name
L-arginine hydroxylase;
VioC (ambiguous);
L-arginine,2-oxoglutarate:O2 oxidoreductase (3-hydroxylating)
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
BRITE hierarchy
Sysname
L-arginine,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Reaction(IUBMB)
L-arginine + 2-oxoglutarate + O2 = (3S)-3-hydroxy-L-arginine + succinate + CO2 [RN:R09363]
Reaction(KEGG)
Substrate
L-arginine [CPD:C00062];
2-oxoglutarate [CPD:C00026];
O2 [CPD:C00007]
Product
(3S)-3-hydroxy-L-arginine [CPD:C18473];
succinate [CPD:C00042];
CO2 [CPD:C00011]
Comment
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.
History
EC 1.14.11.41 created 2013
Orthology
K20612  L-arginine hydroxylase
Reference
1  [PMID:15368582]
  Authors
Ju J, Ozanick SG, Shen B, Thomas MG.
  Title
Conversion of (2S)-arginine to (2S,3R)-capreomycidine by VioC and VioD from the viomycin biosynthetic pathway of Streptomyces sp. strain ATCC11861.
  Journal
Chembiochem 5:1281-5 (2004)
DOI:10.1002/cbic.200400136
  Sequence
Reference
2  [PMID:19490124]
  Authors
Helmetag V, Samel SA, Thomas MG, Marahiel MA, Essen LO.
  Title
Structural basis for the erythro-stereospecificity of the L-arginine oxygenase VioC in viomycin biosynthesis.
  Journal
FEBS J 276:3669-82 (2009)
DOI:10.1111/j.1742-4658.2009.07085.x
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.14.11.41
IUBMB Enzyme Nomenclature: 1.14.11.41
ExPASy - ENZYME nomenclature database: 1.14.11.41
BRENDA, the Enzyme Database: 1.14.11.41

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