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VioC is a Non‐Heme Iron, α‐Ketoglutarate‐Dependent Oxygenase that Catalyzes the Formation of 3 S ‐Hydroxy‐ L ‐Arginine during Viomycin Biosynthesis
Author(s) -
Yin Xihou,
Zabriskie T. Mark
Publication year - 2004
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200400082
Subject(s) - viomycin , biosynthesis , arginine , biochemistry , amino acid , chemistry , heme , stereochemistry , enzyme , antibiotics , streptomycin
TB or no TB? Viomycin is a peptide antibiotic possessing several nonproteinogenic amino acids and is an effective agent in the treatment of multidrug resistant tuberculosis. The vioC gene from the recently cloned viomycin biosynthesis gene cluster was expressed in E. coli , and the corresponding protein was shown to catalyze the conversion of L ‐arginine to 3 S ‐hydroxy‐ L ‐arginine in the presence of Fe 2+ and α‐ketoglutarate. VioC is the first example of an arginine β‐hydroxylase, and the product is a putative precursor to the unusual amino acid capreomycidine.