The lycopene cyclase CrtY from Pantoea ananatis (formerly Erwinia uredovora) catalyzes an FADred-dependent non-redox reaction

Qiuju Yu, Patrick Schaub, Sandro Ghisla, Salim Al-Babili, Anja Krieger-Liszkay, Peter Beyer*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

42 Scopus citations


The cyclization of lycopene generates provitamin A carotenoids such as β-carotene and paves the way toward the formation of cyclic 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 with the possibility of redox catalysis as predicted by the presence of a dinucleotide binding site. We show that reduced FAD is the essential lycopene cyclase (CrtY) cofactor. Using flavin analogs, mass spectrometry, and mutagenesis, evidence was obtained based on which a catalytic mechanism relying on cryptic (net) electron transfer can be refuted. The role of reduced FAD is proposed to reside in the stabilization of a transition state carrying a (partial) positive charge or of a positively charged intermediate via a charge transfer interaction, acidbase catalysis serving as the underlying catalytic principle. Lycopene cyclase, thus, ranks among the novel class of non-redox flavoproteins, such as isopentenyl diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) that requires the reduced form of the cofactor.

Original languageEnglish (US)
Pages (from-to)12109-12120
Number of pages12
JournalJournal of Biological Chemistry
Issue number16
StatePublished - Apr 16 2010

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


Dive into the research topics of 'The lycopene cyclase CrtY from Pantoea ananatis (formerly Erwinia uredovora) catalyzes an FAD<sub>red</sub>-dependent non-redox reaction'. Together they form a unique fingerprint.

Cite this