Streptomyces venezuelae rox is a class A flavoprotein monooxygenase that confers resistance to rifamycin antibiotics. It acts by oxygenating the naphthyl group of the antibiotic, leading to a ring opening event and linearization of the molecule.
This is a thioredoxin-like domain found at the C-terminal of aromatic-ring hydroxylases [1-5], such as PgaE from Bacillus subtilis and Rifampicin monooxygenase from Streptomyces venezuelae. The function of this domain is not clear. It may be involved ...
This is a thioredoxin-like domain found at the C-terminal of aromatic-ring hydroxylases [1-5], such as PgaE from Bacillus subtilis and Rifampicin monooxygenase from Streptomyces venezuelae. The function of this domain is not clear. It may be involved in folding and stability [6] as it lacks the catalytic cysteine residues of thioredoxin, therefore, is not likely to have a redox function [1].