Reinvestigation of a Cyclic Dipeptide <i>N</i>‐Prenyltransferase Reveals Rearrangement of N‐1 Prenylated Indole Derivatives

Ruan, Han‐Li; Yin, Wen‐Bing; Wu, Ji-Zhou; Li, Shu-Ming

doi:10.1002/cbic.200700723

Cited by 30 publications

(45 citation statements)

References 11 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…2) with a typical UV spectrum of indole derivatives (data not shown). This compound was isolated on a preparative scale and subjected to 1 (37)(38)(39). In addition, two aromatic systems with four coupled protons each were also observed (Table 1).…”

Section: Resultsmentioning

confidence: 99%

“…It could be expected that at least three genes/enzymes are involved in the biosynthesis of acetylaszonalenin, i.e. a non-ribosomal peptide synthetase for the formation of the cyclic dipeptide (40, 41), a prenyltransferase for prenyl transfer (36,37), and an acetyltransferase for acetyl transfer. The formation of the ring system between the indoline and the diketopiperazine ring would require an additional enzyme or would be catalyzed during the prenylation by the prenyltransferase.…”

Section: Resultsmentioning

confidence: 99%

“…A large number of simple tryptophan derivatives were accepted by the dimethylallyltryptophan synthases FgaPT2 and 7-dimethylallyltryptophan synthase and converted to 4-or 7-prenylated derivatives, respectively (38,39). All of the tryptophancontaining cyclic dipeptides were converted by CdpNPT and FtmPT1 to N1-prenylated or C2-prenylated derivatives, respectively (36,37). It would be interesting to test the substrate specificity of AnaPT toward cyclic dipeptides.…”

Section: Discussionmentioning

confidence: 99%

See 2 more Smart Citations

Acetylaszonalenin Biosynthesis in Neosartorya fischeri

Yin

Grundmann

Cheng

et al. 2009

Journal of Biological Chemistry

Self Cite

155

129

View full text Add to dashboard Cite

Based on the structural information of acetylaszonalenin isolated from Neosartorya fischeri, a putative biosynthetic gene cluster was identified in the genome sequence of this fungus by genomic mining. This cluster consists of three genes coding for a putative non-ribosomal peptide synthetase (AnaPS), a prenyltransferase (AnaPT), and an acetyltransferase (AnaAT). The coding sequences of anaPT and anaAT were cloned in pQE70 and pQE60, respectively, and overexpressed in Escherichia coli. The soluble His 6 fusion proteins were purified to near homogeneity and characterized biochemically. The structures of the enzymatic products were elucidated by NMR and mass spectroscopy analysis. AnaPT was found to catalyze the reverse prenylation of (

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Acetylaszonalenin Biosynthesis in Neosartorya fischeri

Yin

Grundmann

Cheng

et al. 2009

Journal of Biological Chemistry

Self Cite

155

129

View full text Add to dashboard Cite

show abstract

“…Furthermore, SirD shows lower, but clear, sequence similarities to other indole prenyltransferases, e.g. CdpNPT, FtmPT1 and FtmPT2, all from A. fumigatus (Grundmann & Li, 2005;Ruan et al, 2008;Yin et al, 2007). Most of the indole prenyltransferases mentioned above show broad substrate specificity, and accept simple indole derivatives and Trp-containing cyclic dipeptides as prenylation substrates.…”

Section: Sequence Analysis Of the Putative Prenyltransferase Gene Sirdmentioning

confidence: 99%

A tyrosine O-prenyltransferase catalyses the first pathway-specific step in the biosynthesis of sirodesmin PL

Kremer

2010

Microbiology

Self Cite

View full text Add to dashboard Cite

A putative prenyltransferase gene sirD has been identified in the gene cluster encoding the biosynthesis of the phytotoxin sirodesmin PL in Leptosphaeria maculans. The gene product was found to comprise 449 aa, with a molecular mass of 51 kDa. In this study, the coding region of sirD was amplified by PCR from cDNA, cloned into pQE70, and overexpressed in Escherichia coli. The overproduced protein was purified to apparent homogeneity, and characterized biochemically. The dimeric recombinant SirD was found to catalyse the O-prenylation of L-Tyr in the presence of dimethylallyl diphosphate; this was demonstrated unequivocally by isolation and structural elucidation of the enzymic product. Therefore, SirD catalyses the first pathway-specific step in the biosynthesis of sirodesmin PL. K m values for L-Tyr and dimethylallyl diphosphate were determined as 0.13 and 0.17 mM, respectively. Interestingly, SirD was found to share significant sequence similarity with indole prenyltransferases, which catalyse prenyl transfer reactions onto different positions of indole rings. In contrast to indole prenyltransferases, which accept indole derivatives, but not Tyr or structures derived thereof, as substrates, SirD also prenylated L-Trp, resulting in the formation of 7-dimethylallyltryptophan. A K m value of 0.23 mM was determined for L-Trp. Turnover numbers of 1.0 and 0.06 S "1 were calculated for L-Tyr and L-Trp, respectively.

show abstract

“…Recently, Yin et al have reported the biosynthesis of an aszonalenin and its derivatives from A. fumigatus and Neosartorya fischeri, and described the stereo specific features as a cis-configuration between the two fivemembered rings. [12][13][14] We hope that further investigations in the near future will reveal new information about the stereo specific biosynthesis.…”

mentioning

confidence: 99%