Unknown

Dataset Information

0

A stereoselective vanadium-dependent chloroperoxidase in bacterial antibiotic biosynthesis.


ABSTRACT: 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.

SUBMITTER: Bernhardt P 

PROVIDER: S-EPMC3065929 | biostudies-literature | 2011 Mar

REPOSITORIES: biostudies-literature

altmetric image

Publications

A stereoselective vanadium-dependent chloroperoxidase in bacterial antibiotic biosynthesis.

Bernhardt Peter P   Okino Tatsufumi T   Winter Jaclyn M JM   Miyanaga Akimasa A   Moore Bradley S BS  

Journal of the American Chemical Society 20110308 12


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 chlorinati  ...[more]

Similar Datasets

| S-EPMC7377962 | biostudies-literature
| S-EPMC4270103 | biostudies-literature
| S-EPMC5930311 | biostudies-literature
| S-EPMC6536003 | biostudies-literature
| S-EPMC2711183 | biostudies-literature
| S-EPMC4343137 | biostudies-literature
| S-EPMC2707250 | biostudies-literature