Acyclic carotenoid and cyclic apocarotenoid cleavage by an orthologue of lignostilbene-α,β-dioxygenase in Rhodopseudomonas palustris

Carotenoid cleavage oxygenases catalyse formation of apocarotenoids and the precursors of phytohormones, abscisic acid and strigolactones through oxidative cleavage at specific double bonds of carotenoids. A gene encoding a presumed bacterial oxygenase homologous to lignostilbene-α,β-dioxygenases has been found in the genome of Rhodopseudomonas palustris. By analysing apocarotenoids in recombinant Escherichia coli strains, it was found that the presumed oxygenase catalyses the 15,15′ double bond cleavage of lycopene and neurosporene. Cell lysate containing the recombinant protein cleaved all-trans-β-apo-8′-carotenal at the 15,15′ double bond into retinal and apo-8′,15′-apocarotene-dial. These data demonstrate for the first time that the orthologue of lignostilbene-α,β-dioxygenase found in the carotenogenic phototrophic bacterium has the 15,15′ double bond cleavage activity towards both the acyclic carotenoids and cyclic apocarotenoid.