KEGG   ENZYME: 2.5.1.109Help
Entry
EC 2.5.1.109                Enzyme                                 

Name
brevianamide F prenyltransferase (deoxybrevianamide E-forming);
NotF;
BrePT;
brevianamide F reverse prenyltransferase
Class
Transferases;
Transferring alkyl or aryl groups, other than methyl groups;
Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
BRITE hierarchy
Sysname
dimethylallyl-diphosphate:brevianamide-F tert-dimethylallyl-C-2-transferase
Reaction(IUBMB)
dimethylallyl diphosphate + brevianamide F = diphosphate + deoxybrevianamide E [RN:R10456]
Reaction(KEGG)
Substrate
dimethylallyl diphosphate [CPD:C00235];
brevianamide F [CPD:C20563]
Product
diphosphate [CPD:C00013];
deoxybrevianamide E [CPD:C20636]
Comment
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.
History
EC 2.5.1.109 created 2013
Pathway
Biosynthesis of antibiotics
Reference
1  [PMID:20722388]
  Authors
Ding Y, de Wet JR, Cavalcoli J, Li S, Greshock TJ, Miller KA, Finefield JM, Sunderhaus JD, McAfoos TJ, Tsukamoto S, Williams RM, Sherman DH
  Title
Genome-based characterization of two prenylation steps in the assembly of the stephacidin and notoamide anticancer agents in a marine-derived Aspergillus sp.
  Journal
J. Am. Chem. Soc. 132 (2010) 12733-40.
  Sequence
Reference
2  [PMID:22660767]
  Authors
Yin S, Yu X, Wang Q, Liu XQ, Li SM
  Title
Identification of a brevianamide F reverse prenyltransferase BrePT from Aspergillus versicolor with a broad substrate specificity towards tryptophan-containing cyclic dipeptides.
  Journal
Appl. Microbiol. Biotechnol. 97 (2013) 1649-60.
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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