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Microbiology 151 (2005), 2199-2207; DOI  10.1099/mic.0.27962-0
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Microbiology 151 (2005), 2199-2207; DOI  10.1099/mic.0.27962-0
© 2005 Society for General Microbiology

Overproduction, purification and characterization of FtmPT1, a brevianamide F prenyltransferase from Aspergillus fumigatus

Alexander Grundmann and Shu-Ming Li

Pharmazeutische Biologie, Pharmazeutisches Institut, Eberhard-Karls-Universität Tübingen, Auf der Morgenstelle 8, 72076 Tübingen, Germany

Correspondence
Shu-Ming Li
shuming.li{at}uni-tuebingen.de

A putative prenyltransferase gene, ftmPT1, was identified in the genome sequence of Aspergillus fumigatus. ftmPT1 was cloned and expressed in Escherichia coli, and the protein FtmPT1 was purified to near homogeneity and characterized biochemically. This enzyme was found to catalyse the prenylation of cyclo-L-trp-L-Pro (brevianamide F) at the C-2 position of the indole nucleus. FtmPT1 is a soluble monomeric protein, which does not contain the usual prenyl diphosphate binding site (N/D)DXXD found in most prenyltransferases, and which does not require divalent metal ions for its enzymic activity. Km values for brevianamide F and dimethylallyl diphosphate were determined as 55 and 74 µM, respectively. The turnover number was 5·57 s–1. FtmPT1 showed a high substrate specificity towards dimethylallyl diphosphate, but accepted different tryptophan-containing cyclic dipeptides. Together with dimethylallyltryptophan synthase of ergot alkaloid biosynthesis, FtmPT1 belongs to a new group of prenyltransferases with aromatic substrates.

Abbreviations: DMAPP, dimethylallyl diphosphate; DMATS, dimethylallyltryptophan synthase; EI, electron impact; FAB, fast-atom bombardment




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