Identification of carotenoid cleavage dioxygenases from Nostoc sp. PCC 7120 with different cleavage activities.
Carotenoid cleavage dioxygenases (CCDs) are a class of enzymes that oxidatively cleave carotenoids into apocarotenoids. Dioxygenases have been identified in plants and animals and produce a wide variety of cleavage products. Despite what is known about apocarotenoids in higher organisms, very little is known about apocarotenoids and CCDs in microorganisms. This study surveyed cleavage activities of ten putative carotenoid cleavage dioxygenases from five different cyanobacteria in recombinant Escherichia coli cells producing different carotenoid substrates. Three CCD homologs identified in Nostoc sp. PCC 7120 were purified, and their cleavage activities were investigated. Two of the three enzymes showed cleavage of beta,beta-carotene at the 9,10 and 15,15' positions, respectively. The third enzyme did not cleave full-length carotenoids but cleaved the apocarotenoid beta-apo-8'-carotenal at the 9,10 position. 9,10-Apocarotenoid cleavage specificity has previously not been described. The diversity of carotenoid cleavage activities identified in one cyanobacteria suggests that CCDs not only facilitate the degradation of photosynthetic pigments but generate apocarotenals with yet to be determined biological roles in microorganisms.
Marasco
Erin K
EK
Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, St. Paul, Minnesota 55108, USA.
Vay
Kimleng
K
Schmidt-Dannert
Claudia
C
D002338:Carotenoids / Q000737:chemistry*; D003001:Cloning, Molecular; D000458:Cyanobacteria / Q000201:enzymology; D049308:Dioxygenases / Q000737:chemistry*; D004926:Escherichia coli / Q000201:enzymology / Q000378:metabolism; D008956:Models, Chemical; D046937:Nostoc / Q000201:enzymology*; D010788:Photosynthesis; D011485:Protein Binding; D011994:Recombinant Proteins / Q000737:chemistry
D011994:Recombinant Proteins; C110652:beta-apo-8'-carotenal; D002338:Carotenoids; D049308:Dioxygenases