AI Article Synopsis
- Laurencia is a marine red alga known for producing unique brominated compounds.
- Researchers cloned and expressed two bromoperoxidase enzymes (LnVBPO1 and LnVBPO2) from Laurencia nipponica in E. coli, finding they were thermolabile with lower Km values for Br(-) compared to other red algae.
- The enzymes successfully converted a precursor (laurediol) to a brominated product (deacetyllaurencin), indicating they are functional in the alga and enhancing our understanding of the biosynthesis of Laurencia's brominated metabolites.
Article Abstract
The marine red alga genus Laurencia is one of the richest producers of unique brominated compounds in the marine environment. The cDNAs for two Laurencia nipponica vanadium-dependent bromoperoxidases (LnVBPO1 and LnVBPO2) were cloned and expressed in Escherichia coli. Enzyme assays of recombinant LnVBPO1 and LnVBPO2 using monochlorodimedone revealed that they were thermolabile but their Km values for Br(-) were significantly lower than other red algal VBPOs. The bromination reaction was also assessed using laurediol, the predicted natural precursor of the brominated ether laurencin. Laurediol, protected by trimethylsilyl at the enyne, was converted to deacetyllaurencin by the LnVBPOs, which was confirmed by tandem mass spectrometry. Native LnVBPO partially purified from algal bodies was active, suggesting that LnVBPO is functional in vivo. These results contributed to our knowledge of the biosynthesis of Laurencia brominated metabolites.
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| http://dx.doi.org/10.1080/09168451.2014.918482 | DOI Listing |
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