One ring or two? Determination of ring number in carotenoids by lycopene ɛ-cyclases

By F. Cunningham, E. Gantt. Proceedings of the National Academy of Sciences of the United States of America, 2001

200 citations recorded by the source corpus.

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

A novel type of lycopene ε-cyclase in the marine cyanobacterium Prochlorococcus marinus MED4 (2003, background): “Fig. 5 Comparison of amino acid sequence of a the extended motif B (Krubasik and Sandmann 2000b) in lycopene cyclases, and b a C-terminal region both of which determine the formation of β- or e‐ionone end groups ( Cunningham and Gantt 2001 ).”
Carotenoid biotechnology in plants for nutritionally improved foods (2006, background): “Interestingly, the lettuce LCYE enzyme, a close homologue of the Arabidopsis and tomato proteins, produces the bicyclic e,e-carotene rather than d-carotene from lycopene (Cunningham and Gantt 2001).”
Carotenoid metabolism in plants. (2015, unknown): “The lettuce ε-LCY enzyme, a close homolog of Arabidopsis and tomato proteins, appears to be atypical in generating bicyclic ε,ε-carotene and its hydroxylated derivative lactucaxanthin (Phillip and Young, 1995; Cunningham and Gantt, 2001).”