EC - Lycopene elongase/hydratase (dihydrobisanhydrobacterioruberin-forming)

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature


Accepted name:
lycopene elongase/hydratase (dihydrobisanhydrobacterioruberin-forming)
Systematic name:
dimethylallyl-diphosphate:all-trans-lycopene dimethylallyltransferase (hydrating, dihydrobisanhydrobacterioruberin-forming)



The enzyme, characterized from the bacterium Dietzia sp. CQ4 and the halophilic archaea Halobacterium salinarum and Haloarcula japonica, is bifunctional. It catalyses the elongation of the C40 carotenoid all-trans-lycopene by attaching an isoprene unit at C-2 as well as the hydroxylation of the previous end of the molecule. The enzyme acts at both ends of the substrate, and combined with the action of EC, 1-hydroxy-2-isopentenylcarotenoid 3,4-desaturase, it forms the C50 carotenoid dihydrobisanhydrobacterioruberin. cf. EC, lycopene elongase/hydratase (flavuxanthin-forming).

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB


  1. Tao, L., Yao, H., Cheng, Q.
    Genes from a Dietzia sp. for synthesis of C40 and C50 beta-cyclic carotenoids.
    Gene 386 : 90-97 (2007). [PMID: 17008032]
  2. Dummer, A. M., Bonsall, J. C., Cihla, J. B., Lawry, S. M., Johnson, G. C., Peck, R. F.
    Bacterioopsin-mediated regulation of bacterioruberin biosynthesis in Halobacterium salinarum.
    J. Bacteriol. 193 : 5658-5667 (2011). [PMID: 21840984]
  3. Yang, Y., Yatsunami, R., Ando, A., Miyoko, N., Fukui, T., Takaichi, S., Nakamura, S.
    Complete biosynthetic pathway of the C50 carotenoid bacterioruberin from lycopene in the extremely halophilic archaeon Haloarcula japonica.
    J. Bacteriol. 197 : 1614-1623 (2015). [PMID: 25712483]

[EC created 2018]