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dc.contributor.authorTrautmann, Danika
dc.contributor.authorBeyer, Peter D.
dc.contributor.authorAl-Babili, Salim
dc.date.accessioned2015-08-03T11:12:59Z
dc.date.available2015-08-03T11:12:59Z
dc.date.issued2013-07-05
dc.identifier.citationTrautmann, D., Beyer, P., & Al-Babili, S. (2013). The ORFslr0091ofSynechocystis sp. PCC6803 encodes a high-light induced aldehyde dehydrogenase converting apocarotenals and alkanals. FEBS Journal, 280(15), 3685–3696. doi:10.1111/febs.12361
dc.identifier.issn1742464X
dc.identifier.pmid23734995
dc.identifier.doi10.1111/febs.12361
dc.identifier.urihttp://hdl.handle.net/10754/562857
dc.description.abstractOxidative cleavage of carotenoids and peroxidation of lipids lead to apocarotenals and aliphatic aldehydes called alkanals, which react with vitally important compounds, promoting cytotoxicity. Although many enzymes have been reported to deactivate alkanals by converting them into fatty acids, little is known about the mechanisms used to detoxify apocarotenals or the enzymes acting on them. Cyanobacteria and other photosynthetic organisms must cope with both classes of aldehydes. Here we report that the Synechocystis enzyme SynAlh1, encoded by the ORF slr0091, is an aldehyde dehydrogenase that mediates oxidation of both apocarotenals and alkanals into the corresponding acids. Using a crude lysate of SynAlh1-expressing Escherichia coli cells, we show that SynAlh1 converts a wide range of apocarotenals and alkanals, with a preference for apocarotenals with defined chain lengths. As suggested by in vitro incubations and using engineered retinal-forming E. coli cells, we found that retinal is not a substrate for SynAlh1, making involvement in Synechocystis retinoid metabolism unlikely. The transcript level of SynAlh1 is induced by high light and cold treatment, indicating a role in the stress response, and the corresponding gene is a constituent of a stress-related operon. The assumptions regarding the function of SynAlh are further supported by the surprisingly high homology to human and plant aldehyde dehydrogenase that have been assigned to aldehyde detoxification. SynAlh1 is the first aldehyde dehydrogenase that has been shown to form both apocarotenoic and fatty acids. This dual function suggests that its eukaryotic homologs may also be involved in apocarotenal metabolism, a function that has not been considered so far. Aldehyde dehydrogenases play an important role in detoxification of reactive aldehydes. Here, we report on a cyanbacterial enzyme capable in converting two classes of lipid-derived aldehydes, apocaotenals and alkanals. The corresponding gene is a constituent of a stress-related operon, and homology to eukaryotic enzymes points to a yet not considered possibility of their being involved in scavenging of apocarotenals. © 2013 FEBS.
dc.description.sponsorshipThis work was supported by Deutsche Forschungsgemeinschaft grant number AL 892/1-4 and the Deutsche Forschungsgemeinschaft Graduate School (GRK1305). We are indebted to Hansgeorg Ernst (BASF, Ludwigshafen, Germany) for providing synthetic apocarotenoids.
dc.publisherWiley
dc.subjectaldehyde dehydrogenase
dc.subjectalkanals
dc.subjectapocarotenoids
dc.subjectcarotenoid cleavage
dc.subjectcyanobacteria
dc.titleThe ORF slr0091 of Synechocystis sp. PCC6803 encodes a high-light induced aldehyde dehydrogenase converting apocarotenals and alkanals
dc.typeArticle
dc.contributor.departmentBiological and Environmental Science and Engineering (BESE) Division
dc.contributor.departmentBioscience Program
dc.contributor.departmentCenter for Desert Agriculture
dc.contributor.departmentPlant Science
dc.contributor.departmentPlant Science Program
dc.identifier.journalFEBS Journal
dc.contributor.institutionFaculty of Biology, Albert-Ludwigs University of Freiburg, Germany
kaust.personAl-Babili, Salim
dc.date.published-online2013-07-05
dc.date.published-print2013-08


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