Saltar al contenido
Merck

A stereoselective vanadium-dependent chloroperoxidase in bacterial antibiotic biosynthesis.

Journal of the American Chemical Society (2011-03-10)
Peter Bernhardt, Tatsufumi Okino, Jaclyn M Winter, Akimasa Miyanaga, Bradley S Moore
RESUMEN

Halogenases catalyze reactions that introduce halogen atoms into electron-rich organic molecules. Vanadium-dependent haloperoxidases are generally considered to be promiscuous halogenating enzymes that have thus far been derived exclusively from eukaryotes, where their cellular function is often disputed. We now report the first biochemical characterization of a bacterial vanadium-dependent chloroperoxidase, NapH1 from Streptomyces sp. CNQ-525, which catalyzes a highly stereoselective chlorination-cyclization reaction in napyradiomycin antibiotic biosynthesis. This finding biochemically links a vanadium chloroperoxidase to microbial natural product biosynthesis.

MATERIALES
Referencia del producto
Marca
Descripción del producto

Sigma-Aldrich
Chloroperoxidase from Caldariomyces fumago, buffered aqueous suspension, ≥3,000 units/mL
Sigma-Aldrich
Chloroperoxidase from Caldariomyces fumago, aqueous suspension, brown, >10,000 U/mL
Sigma-Aldrich
Chloroperoxidase from Caldariomyces fumago, buffered aqueous suspension, 1,000-2,000 units/mg protein (E1%/280)