1887

Abstract

A putative prenyltransferase gene, , was identified in the genome sequence of . was cloned and expressed in , and the protein FtmPT1 was purified to near homogeneity and characterized biochemically. This enzyme was found to catalyse the prenylation of --trp--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. values for brevianamide F and dimethylallyl diphosphate were determined as 55 and 74 μM, respectively. The turnover number was 5·57 s. 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.

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2005-07-01
2024-04-20
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