The biosynthetic genes for prenylated phenazines are located at two different chromosomal loci of Streptomyces cinnamonensis DSM 1042.
Bottom Line: The protein EpzP was expressed in Escherichia coli in form of a his-tag fusion protein and purified.The enzyme catalysed the prenylation of 5,10-dihydrophenazine-1-carboxylic acid (dihydro-PCA) using dimethylallyl diphosphate (DMAPP) as isoprenoid substrate.K(m) values were determined as 108 µM for dihydro-PCA and 25 µM for DMAPP.
Affiliation: Eberhard-Karls-University of Tübingen, Pharmaceutical Institute, Auf der Morgenstelle 8, D-72076 Tübingen, Germany.Show MeSH
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Mentions: In our search for new members of the ABBA prenyltransferase class, we investigated Streptomyces cinnamonensis DSM 1042 which produces two different types of isoprenylated aromatic secondary metabolites, i.e. furanonaphthoquinone I (FNQ I) and endophenazines (Fig. 1) (Tax et al., 1983; Sedmera et al., 1991). We identified a 55 kb gene cluster which contained genes for both FNQ I and endophenazine biosynthesis (Haagen et al., 2006). Inactivation experiments confirmed the involvement of these genes in the respective pathways. The cluster was found to contain genes for two new members of the ABBA prenyltransferases. One of these, fnq26, was shown to encode the prenyltransferase of FNQ I biosynthesis (Haagen et al., 2007). Unexpectedly, the other gene, fnq28, was proven not to be involved in FNQ I or endophenazine biosynthesis (Haagen et al., 2006). Therefore, the prenyltransferase of endophenazine biosynthesis in S. cinnamonensis remained unknown.
Affiliation: Eberhard-Karls-University of Tübingen, Pharmaceutical Institute, Auf der Morgenstelle 8, D-72076 Tübingen, Germany.