EC 2.5.1.109 - Brevianamide F prenyltransferase (deoxybrevianamide E-forming)

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IntEnz Enzyme Nomenclature
EC 2.5.1.109

Names

Accepted name:
brevianamide F prenyltransferase (deoxybrevianamide E-forming)
Other names:
NotF
BrePT
brevianamide F reverse prenyltransferase
Systematic name:
dimethylallyl-diphosphate:brevianamide-F tert-dimethylallyl-C-2-transferase

Reaction

Comments:

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
UniProtKB/Swiss-Prot:

References

  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 2.5.1.109 created 2013]