Functional analysis of an indole‐diterpene gene cluster for lolitrem B biosynthesis in the grass endosymbiont <i>Epichloë festucae</i>

Saikia, Sanjay; Takemoto, Daigo; Tapper, B.A.; Lane, George; Fraser, Karl; Scott, Barry

doi:10.1016/j.febslet.2012.06.035

Cited by 64 publications

(90 citation statements)

References 28 publications

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“…They suggested that LtmE catalyzes the di-prenylation of the A-ring of terpendole I, a paxilline-related compound, at positions, 20 and 21. 40) In the present study, AmyD was found to catalyze regular di-prenylation at the same positions of paxilline (Fig. 5).…”

Section: Discussionsupporting

confidence: 59%

“…The other one showed high similarity to LtmJ (64% identity), a cytochrome P450 monooxygenase, which has been reported to be responsible for lolitremanes formation. 40) In sum, it is suggested that the cluster identified in this study participates in the generation of a lolilline/ lolitrem type of compound. To confirm this, the same strategy used for functional analysis of the paxilline biosynthetic gene cluster, the introduction of the pax genes into A. oryzae and an analysis of the compound produced by the transformant, 23) might be also useful.…”

Section: Discussionmentioning

confidence: 56%

“…Furthermore, three P450 monooxygenase genes are present in the amy gene cluster. In a search for homologous enzymes, two of them, AmyP and AmyQ, were found to show similarity to PaxP/LtmP (28%/34% identity) and PaxQ/LtmQ (22%/27%), 22,40) which catalyze successive reactions converting paspaline to paxilline. The other one showed high similarity to LtmJ (64% identity), a cytochrome P450 monooxygenase, which has been reported to be responsible for lolitremanes formation.…”

Section: Discussionmentioning

confidence: 99%

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A fungal prenyltransferase catalyzes the regular di-prenylation at positions 20 and 21 of paxilline

Liu

Noike

Minami

et al. 2014

Bioscience, Biotechnology, and Biochemistry

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A putative indole diterpene biosynthetic gene cluster composed of eight genes was identified in a genome database of Phomopsis amygdali, and from it, biosynthetic genes of fusicoccin A were cloned and characterized. The six genes showed significant similarities to pax genes, which are essential to paxilline biosynthesis in Penicillium paxilli. Recombinants of the three putative prenyltransferase genes in the cluster were overexpressed in Escherichia coli and characterized by means of in vitro experiments. AmyG is perhaps a GGDP synthase. AmyC and AmyD were confirmed to be prenyltransferases catalyzing the transfer of GGDP to IGP and a regular di-prenylation at positions 20 and 21 of paxilline, respectively. AmyD is the first know example of an enzyme with this function. The Km values for AmyD were calculated to be 7.6 ± 0.5 μM for paxilline and 17.9 ± 1.7 μM for DMAPP at a kcat of 0.12 ± 0.003/s.

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Section: Discussionsupporting

confidence: 59%

Section: Discussionmentioning

confidence: 56%

Section: Discussionmentioning

confidence: 99%

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A fungal prenyltransferase catalyzes the regular di-prenylation at positions 20 and 21 of paxilline

Liu

Noike

Minami

et al. 2014

Bioscience, Biotechnology, and Biochemistry

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“…Moreover, the very low Km value for DMAPP reasonably supports the result that farnesyl diphosphate and GGDP were not accepted as substrates. On the other hand, the Km value for paxilline was calculated to be higher than for DMAPP, suggesting that paxilline-related compounds, such as paspaline, 13-desoxypaxilline, lolitrems (Saikia et al 2012), and terpendoles (Motoyama et al 2012), might be accepted by PaxD.…”

Section: Discussionmentioning

confidence: 99%

Functional analysis of a prenyltransferase gene (paxD) in the paxilline biosynthetic gene cluster

Liu

Noike

Minami

et al. 2013

Appl Microbiol Biotechnol

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Paxilline is an indole diterpene produced by Penicillium paxilli. Six genes (paxB, C, G, M, P, and Q) in paxilline biosynthetic gene cluster were previously shown to be responsible for paxilline biosynthesis. In this study, we have characterized paxD, which is located next to paxQ and has weak similarities to fungal dimethylallyl tryptophan synthase genes. PaxD was overexpressed in E. coli and the purified enzyme was used for in vitro analysis. When paxilline and dimethylallyl diphosphate were used as substrates, one major and one minor product, which were identified as di-prenyl paxilline and mono-prenyl paxilline by liquid chromatography-mass spectrometry analysis, were formed. The structure of the major product was determined to be 21,22-diprenylated paxilline, showing that PaxD catalyzed the successive di-prenylation. Traces of both products were detected in culture broth of P. paxilli by liquid chromatography-mass spectrometry analysis. The enzyme is likely to be a dimer and required no divalent cations. The optimum pH and temperature were 8.0 and 37°C, respectively. The Km values were calculated as 106.4 ± 5.4 µM for paxilline and 0.57 ± 0.02 µM for DMAPP with a kcat of 0.97 ± 0.01/sec.

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“…No structural or detailed mechanistic information is available for prenyl cyclases involved in the biosynthesis of indole diterpenoids [47,[54][55][56] and of some meroterpenoids [57][58][59].…”

Section: C40 -Phyotenementioning

confidence: 99%

Biosynthesis of Terpenoid Natural Products in Fungi

Schmidt‐Dannert

2014

Advances in Biochemical Engineering/Biotechnology

108

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Tens of thousands of terpenoid natural products have been isolated from plants and microbial sources. Higher fungi (Ascomycota and Basidiomycota) are known to produce an array of well-known terpenoid natural products, including mycotoxins, antibiotics, antitumor compounds, and phytohormones. Except for a few well-studied fungal biosynthetic pathways, the majority of genes and biosynthetic pathways responsible for the biosynthesis of a small number of these secondary metabolites have only been discovered and characterized in the past 5-10 years. This chapter provides a comprehensive overview of the current knowledge on fungal terpenoid biosynthesis from biochemical, genetic, and genomic viewpoints. Enzymes involved in synthesizing, transferring, and cyclizing the prenyl chains that form the hydrocarbon scaffolds of fungal terpenoid natural products are systematically discussed. Genomic information and functional evidence suggest differences between the terpenome of the two major fungal phyla--the Ascomycota and Basidiomycota--which will be illustrated for each group of terpenoid natural products.

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Functional analysis of an indole‐diterpene gene cluster for lolitrem B biosynthesis in the grass endosymbiont Epichloë festucae

Cited by 64 publications

References 28 publications

A fungal prenyltransferase catalyzes the regular di-prenylation at positions 20 and 21 of paxilline

A fungal prenyltransferase catalyzes the regular di-prenylation at positions 20 and 21 of paxilline

Functional analysis of a prenyltransferase gene (paxD) in the paxilline biosynthetic gene cluster

Biosynthesis of Terpenoid Natural Products in Fungi

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