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Expression and biochemical characterization of the 1-HO-carotenoid methylase CrtF from Rhodobacter capsulatus
Article first published online: 9 JAN 2006
DOI: 10.1016/S0378-1097(03)00302-1
1574-6968/asset/cover.gif?v=1&s=069bb2c224e243333d4486580fbd90d9ebeffa6b "FEMS Microbiology Letters")
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How to Cite
Badenhop, F., Steiger, S., Sandmann, M. and Sandmann, G. (2003), Expression and biochemical characterization of the 1-HO-carotenoid methylase CrtF from Rhodobacter capsulatus. FEMS Microbiology Letters, 222: 237–242. doi: 10.1016/S0378-1097(03)00302-1
Publication History
- Issue published online: 9 JAN 2006
- Article first published online: 9 JAN 2006
- Received 23 January 2003, Revised 1 April 2003, Accepted 1 April 2003
- Abstract
- Article
- References
- Cited By
Keywords:
- Acyclic 1-HO-carotenoid methylase;
- CrtF;
- Rhodobacter capsulatus;
- Spheroidene biosynthesis;
- Spirilloxanthin biosynthesis
Abstract
In purple bacteria, acyclic 1-methoxy carotenoids like spheroidene or spirilloxanthin are essential components of the photosynthetic apparatus. One of the last steps of their biosynthesis involves O-methylation of the 1-hydroxy group. The 1-HO-carotenoid methylase CrtF from Rhodobacter capsulatus catalyzing this type of reaction was expressed in Escherichia coli in an active form. It was then purified by affinity chromatography and biochemically characterized. The enzymatic reaction depends on S-adenosylmethionine as the only cofactor. By complementation in E. coli, the substrate specificity of the enzyme was determined. It could be shown that the enzyme converts not only all possible 1-hydroxy carotenoids in the spheroidene/1′-HO-spheroidene biosynthetic pathway of R. capsulatus but also carotenoid intermediates leading to the formation of spirilloxanthin in a pathway which is absent in R. capsulatus but present in related species.