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Formation of the Nonproteinogenic Amino Acid 2 S ,3 R ‐Capreomycidine by VioD from the Viomycin Biosynthesis Pathway
Author(s) -
Yin Xihou,
McPhail Kerry L.,
Kim Kyungja,
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.200400187
Subject(s) - viomycin , biosynthesis , stereochemistry , chemistry , amino acid , biochemistry , arginine , gene cluster , residue (chemistry) , enzyme , gene , antibiotics , streptomycin
The tuberactinomycin peptide antibiotics possess several nonproteinogenic amino acids, including the signature capreomycidine residue arising from the oxidative cyclization of the L ‐arginine side chain. The vioD gene from the recently cloned viomycin biosynthesis gene cluster was expressed in E. coli , and the corresponding protein shown to catalyze the pyridoxal phosphate dependent conversion of 3 S ‐hydroxy‐ L ‐arginine to 2 S ,3 R ‐capreomycidine. VioD is the first example of a PLP‐dependent enzyme that promotes an intramolecular β‐replacement reaction.