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Journal of Bacteriology, October 1999, p. 6184-6187, Vol. 181, No. 19
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

4,4'-Diapophytoene Desaturase: Catalytic Properties of an Enzyme from the C30 Carotenoid Pathway of Staphylococcus aureus

Axel Raisig and Gerhard Sandmann*

Biosynthesis Group, Botanisches Institut, J. W. Goethe Universität Frankfurt, 60054 Frankfurt, Germany

Received 9 April 1999/Accepted 21 July 1999

Staphylococcus aureus synthesizes C30 carotenoids. Their formation involves the introduction of three double bonds, which is catalyzed by a single enzyme. This enzyme, 4,4'-diapophytoene desaturase from S. aureus, was overexpressed in Escherichia coli and purified in one step by affinity chromatography, and then the protein was characterized with respect to substrate specificity, cofactor requirement, and oligomerization.

* Corresponding author. Mailing address: Biosynthesis Group, Botanical Institute, J. W. Goethe Universität, P.O. Box 111932, 60054 Frankfurt, Germany. Phone: 49 69 798 24746. Fax: 49 69 798 24822. E-mail: Sandmann{at}em.uni-frankfurt.d400.de.

Journal of Bacteriology, October 1999, p. 6184-6187, Vol. 181, No. 19
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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