EC - Brevianamide F prenyltransferase (deoxybrevianamide E-forming)

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature


Accepted name:
brevianamide F prenyltransferase (deoxybrevianamide E-forming)
Other names:
brevianamide F reverse prenyltransferase
Systematic name:
prenyl-diphosphate:brevianamide-F 2-methylbut-3-en-2-yl-C-2-transferase



The enzyme from the fungus Aspergilus sp. MF297-2 is specific for brevianamide F [1], while the enzyme from Aspergillus versicolor accepts a broad range of trytophan-containing cyclic dipeptides [2]. Involved in the biosynthetic pathways of several indole alkaloids such as paraherquamides and malbrancheamides.

Links to other databases

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


  1. Ding, Y., de Wet, J. R., Cavalcoli, J., Li, S., Greshock, T. J., Miller, K. A., Finefield, J. M., Sunderhaus, J. D., McAfoos, T. J., Tsukamoto, S., Williams, R. M., Sherman, D. H.
    Genome-based characterization of two prenylation steps in the assembly of the stephacidin and notoamide anticancer agents in a marine-derived Aspergillus sp.
    J. Am. Chem. Soc. 132 : 12733-12740 (2010). [PMID: 20722388]
  2. Yin, S., Yu, X., Wang, Q., Liu, X. Q., Li, S. M.
    Identification of a brevianamide F reverse prenyltransferase BrePT from Aspergillus versicolor with a broad substrate specificity towards tryptophan-containing cyclic dipeptides.
    Appl. Microbiol. Biotechnol. 97 : 1649-1660 (2013). [PMID: 22660767]

[EC created 2013]