NDLI: Conversion of the lycopene monocyclase of Myxococcus xanthus into a bicyclase

Content Provider	Springer Nature Link
Author	Iniesta, Antonio A. Cervantes, María Murillo, Francisco J.
Copyright Year	2008
Abstract	Depending on the cyclized hydrocarbon backbone ends, carotenoids can be acyclic, monocyclic, or bicyclic. Lycopene cyclases are the enzymes responsible for catalyzing the formation of cyclic carotenoids from acyclic lycopene. Myxococcus xanthus is a bacterium that accumulates monocyclic carotenoids such as a glycoside ester of myxobacton. We show here that this bacterium possesses a cyclase belonging to the group of the heterodimeric cyclases CrtYc and CrtYd. These two individual proteins are encoded by crtYc and crtYd, which are located in the carotenogenic carA operon of the carB–carA gene cluster, and the presence of both is essential for the cyclization of lycopene. CrtYc and CrtYd from M. xanthus form a heterodimeric cyclase with β-monocyclic activity, which converts lycopene into monocyclic γ-carotene, but not into bicyclic β-carotene like most β-cyclases. This is an unusual case where two different proteins constitute a lycopene cyclase enzyme with monocyclic activity. We were able to convert this lycopene monocyclase into a lycopene bicyclase enzyme producing β-carotene, by fusing both proteins with an extra transmembrane domain. The chimeric protein appears to allow a proper membranal disposition of both CrtYc and CrtYd, to perform two cyclization reactions, while a hybrid without the extra transmembrane helix performs only one cyclization.
Starting Page	793
Ending Page	802
Page Count	10
File Format	PDF
ISSN	01757598
Journal	Applied Microbiology and Biotechnology
Volume Number	79
Issue Number	5
e-ISSN	14320614
Language	English
Publisher	Springer-Verlag
Publisher Date	2008-04-24
Publisher Place	Berlin, Heidelberg
Access Restriction	Subscribed
Subject Keyword	Carotenes Cyclization Beta-carotene Gamma-carotene Heterodimeric Microbial Genetics and Genomics Microbiology Biotechnology
Content Type	Text
Resource Type	Article
Subject	Medicine Applied Microbiology and Biotechnology Biotechnology

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