Substrate promiscuity of RdCCD1, a carotenoid cleavage oxygenase from Rosa damascena

Fong Chin Huang, Györgyi Horváth, Péter Molnár, Erika Turcsi, József Deli, Jens Schrader, Gerhard Sandmann, Holger Schmidt, Wilfried Schwab

Research output: Contribution to journalArticle

69 Citations (Scopus)


Several of the key flavor compounds in rose essential oil are C13-norisoprenoids, such as β-damascenone, β-damascone, and β-ionone which are derived from carotenoid degradation. To search for genes putatively responsible for the cleavage of carotenoids, cloning of carotenoid cleavage (di-)oxygenase (CCD) genes from Rosa damascena was carried out by a degenerate primer approach and yielded a full-length cDNA (RdCCD1). The RdCCD1 gene was expressed in Escherichia coli and recombinant protein was assayed for its cleavage activity with a multitude of carotenoid substrates. The RdCCD1 protein was able to cleave a variety of carotenoids at the 9-10 and 9′-10′ positions to produce a C14 dialdehyde and two C13 products, which vary depending on the carotenoid substrates. RdCCD1 could also cleave lycopene at the 5-6 and 5′-6′ positions to produce 6-methyl-5-hepten-2-one. Expression of RdCCD1 was studied by real-time PCR in different tissues of rose. The RdCCD1 transcript was present predominantly in rose flower, where high levels of volatile C13-norisoprenoids are produced. Thus, the accumulation of C13-norisoprenoids in rose flower is correlated to the expression of RdCCD1.

Original languageEnglish
Pages (from-to)457-464
Number of pages8
Issue number4
Publication statusPublished - Mar 1 2009


  • (9Z)-, (9′Z)- and (di-Z)-carotenoids
  • C-norisoprenoids
  • Carotenoid cleavage oxygenase
  • RdCCD1
  • Rosa damascena
  • Rose essential oil

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Plant Science
  • Horticulture

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  • Cite this

    Huang, F. C., Horváth, G., Molnár, P., Turcsi, E., Deli, J., Schrader, J., Sandmann, G., Schmidt, H., & Schwab, W. (2009). Substrate promiscuity of RdCCD1, a carotenoid cleavage oxygenase from Rosa damascena. Phytochemistry, 70(4), 457-464.