Identification of bacterial carotenoid cleavage dioxygenase homologues that cleave the interphenyl alpha,beta double bond of stilbene derivatives via a monooxygenase reaction.

ABSTRACT: Carotenoid cleavage oxygenases (CCOs), which are also referred to as carotenoid cleavage dioxygenases (CCDs) are a new class of nonheme iron-type enzymes that oxidatively cleave double bonds in the conjugated carbon chain of carotenoids. The oxidative cleavage mechanism of these enzymes is not clear, and both monooxygenase and dioxygenase mechanisms have been proposed for different carotenoid cleavage enzymes. CCOs have been described from plants, animals, fungi, and cyanobacteria, but little is known about their distribution and activities in bacteria other than cyanobacteria. We surveyed bacterial genome sequences for CCO homologues and report the characterization of CCO homologues that were identified in Novosphingobium aromaticivorans DSM 12444 (NOV1 and NOV2) and in Bradyrhizobium sp.

SUBMITTER: Marasco EK 

PROVIDER: S-EPMC3988535 | biostudies-literature | 2008 Jun

REPOSITORIES: biostudies-literature