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The Lycopene Cyclase CrtY from Pantoea ananatis (Formerly Erwinia uredovora) Catalyzes an FAD<sub>red</sub>-dependent Non-redox Reaction

The Lycopene Cyclase CrtY from Pantoea ananatis (Formerly Erwinia uredovora) Catalyzes an FADred-dependent Non-redox Reaction

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YU, Qiuju, Patrick SCHAUB, Sandro GHISLA, Salim AL-BABILI, Anja KRIEGER-LISZKAY, Peter BEYER, 2010. The Lycopene Cyclase CrtY from Pantoea ananatis (Formerly Erwinia uredovora) Catalyzes an FADred-dependent Non-redox Reaction. In: The Journal of Biological Chemistry. American Society for Biochemistry and Molecular Biology. 285(16), pp. 12109-12120. ISSN 0021-9258. eISSN 1083-351X. Available under: doi: 10.1074/jbc.M109.091843

@article{Yu2010-04-16Lycop-52089, title={The Lycopene Cyclase CrtY from Pantoea ananatis (Formerly Erwinia uredovora) Catalyzes an FADred-dependent Non-redox Reaction}, year={2010}, doi={10.1074/jbc.M109.091843}, number={16}, volume={285}, issn={0021-9258}, journal={The Journal of Biological Chemistry}, pages={12109--12120}, author={Yu, Qiuju and Schaub, Patrick and Ghisla, Sandro and Al-Babili, Salim and Krieger-Liszkay, Anja and Beyer, Peter} }

The cyclization of lycopene generates provitamin A carotenoids such as β-carotene and paves the way toward the formation ofcyclic xanthophylls playing distinct roles in photosynthesis and as precursors for regulatory molecules in plants and animals.The biochemistry of lycopene cyclization has been enigmatic, as the previously proposed acid-base catalysis conflicted withthe possibility of redox catalysis as predicted by the presence of a dinucleotide binding site. We show that reduced FAD isthe essential lycopene cyclase (CrtY) cofactor. Using flavin analogs, mass spectrometry, and mutagenesis, evidence was obtainedbased on which a catalytic mechanism relying on cryptic (net) electron transfer can be refuted. The role of reduced FAD isproposed to reside in the stabilization of a transition state carrying a (partial) positive charge or of a positively chargedintermediate via a charge transfer interaction, acid-base catalysis serving as the underlying catalytic principle. Lycopenecyclase, thus, ranks among the novel class of non-redox flavoproteins, such as isopentenyl diphosphate:dimethylallyl diphosphateisomerase type 2 (IDI-2) that requires the reduced form of the cofactor. Yu, Qiuju Krieger-Liszkay, Anja Krieger-Liszkay, Anja eng 2020-12-11T09:27:28Z Beyer, Peter Al-Babili, Salim Schaub, Patrick Ghisla, Sandro Schaub, Patrick Beyer, Peter 2010-04-16 Ghisla, Sandro Yu, Qiuju 2020-12-11T09:27:28Z The Lycopene Cyclase CrtY from Pantoea ananatis (Formerly Erwinia uredovora) Catalyzes an FAD<sub>red</sub>-dependent Non-redox Reaction Al-Babili, Salim

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