Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With oxidation of a pair of donors resulting in the reduction of O2 to two molecules of water
The enzyme, characterized from marine bacteria of the Pseudoalteromonas genus, belongs to a family of FAD-dependent halogenases that act on acyl-carrier protein-tethered substrates. It catalyses three successive rounds of bromination. While the order has not been verified, it is believed to resemble that of EC 1.14.19.56, S-(1H-pyrrole-2-carbonyl)-[peptidyl-carrier protein] chlorinase, due to significant sequence homology. Reduced FAD is provided in situ by a dedicated reductase and diffuses into the active site, where it reacts with the oxygen and bromide ion, resulting in formation of a bromoamine intermediate on a catalytic lysine side chain, and the eventual transfer of the bromide to the substrate. The enzyme from Pseudoalteromonas luteoviolacea 2ta16 is specific for bromide and does not accept chloride.
