Discovery and Characterization of Terpenoid Biosynthetic Pathways of Fungi

Wawrzyn, Grayson T.; Bloch, Sarah E.; Schmidt‐Dannert, Claudia

doi:10.1016/b978-0-12-394290-6.00005-7

Cited by 41 publications

(41 citation statements)

References 51 publications

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“…This has proven difficult in plants, where TPS sequences are dominated by species relationships rather than product, but the addition of a large number of sequenced fungal and bacterial genomes has reignited these efforts (78). Recent work on terpene synthases from Basidiomycota has attempted to categorize them based on the type of ring closure catalyzed by the enzymes (34,35,79). Most ascomycete terpene synthases in our phylogeny, including those from E7406B, appear distinct from the basidiomycete enzymes as well as plants and bacteria.…”

Section: Discussionmentioning

confidence: 99%

Identification of a Fungal 1,8-Cineole Synthase from Hypoxylon sp. with Specificity Determinants in Common with the Plant Synthases

Shaw

Berbasova

Sasaki

et al. 2015

Journal of Biological Chemistry

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Background: 1,8-Cineole, a commercially important monoterpene, was identified as a fungal product. Results: The 1,8-cineole synthase was identified from a Hypoxylon fungal genome, and mutagenesis revealed a critical asparagine residue. Conclusion:The fungal 1,8-cineole synthase uses a mechanism similar to the plant version. Significance: This is the first identified fungal monoterpene synthase and may facilitate future terpene synthase identification and production.

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Section: Discussionmentioning

confidence: 99%

Identification of a Fungal 1,8-Cineole Synthase from Hypoxylon sp. with Specificity Determinants in Common with the Plant Synthases

Shaw

Berbasova

Sasaki

et al. 2015

Journal of Biological Chemistry

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“…The reaction cascade is either initiated by a metal iondependent ionization of the diphosphate moiety or a protonation of the substrate, and can be terminated by proton abstraction or water addition (11,13,15). Because the reaction cascade may be branched and termination may occur at multiple levels, many TPSs are multiproduct enzymes forming complex mixtures of compounds (16)(17)(18)(19). Moreover, some TPSs also accept multiple substrates to produce monoterpenes, sesquiterpenes, and diterpenes (11).…”

mentioning

confidence: 99%

Novel family of terpene synthases evolved from trans -isoprenyl diphosphate synthases in a flea beetle

Beran

Rahfeld

Luck

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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Sesquiterpenes play important roles in insect communication, for example as pheromones. However, no sesquiterpene synthases, the enzymes involved in construction of the basic carbon skeleton, have been identified in insects to date. We investigated the biosynthesis of the sesquiterpene (6R,7S)-himachala-9,11-diene in the crucifer flea beetle Phyllotreta striolata, a compound previously identified as a male-produced aggregation pheromone in several Phyllotreta species. A (6R,7S)-himachala-9,11-diene–producing sesquiterpene synthase activity was detected in crude beetle protein extracts, but only when (Z,E)-farnesyl diphosphate [(Z,E)-FPP] was offered as a substrate. No sequences resembling sesquiterpene synthases from plants, fungi, or bacteria were found in the P. striolata transcriptome, but we identified nine divergent putative trans-isoprenyl diphosphate synthase (trans-IDS) transcripts. Four of these putative trans-IDSs exhibited terpene synthase (TPS) activity when heterologously expressed. Recombinant PsTPS1 converted (Z,E)-FPP to (6R,7S)-himachala-9,11-diene and other sesquiterpenes observed in beetle extracts. RNAi-mediated knockdown of PsTPS1 mRNA in P. striolata males led to reduced emission of aggregation pheromone, confirming a significant role of PsTPS1 in pheromone biosynthesis. Two expressed enzymes showed genuine IDS activity, with PsIDS1 synthesizing (E,E)-FPP, whereas PsIDS3 produced neryl diphosphate, (Z,Z)-FPP, and (Z,E)-FPP. In a phylogenetic analysis, the PsTPS enzymes and PsIDS3 were clearly separated from a clade of known coleopteran trans-IDS enzymes including PsIDS1 and PsIDS2. However, the exon–intron structures of IDS and TPS genes in P. striolata are conserved, suggesting that this TPS gene family evolved from trans-IDS ancestors.

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“…The genes encoding pathway enzymes tend to occur in gene clusters that are co-regulated in complex ways, often controlled by regulatory genes located in the cluster [69]. A classical hallmark of gene clusters, and therefore the starting point for functional analysis, is the presence of genes encoding molecular machines involved in biosynthesis of the carbon backbone of secondary metabolites: either a PKS [70], or NRPS [71], or hybrid PKS-NRPS gene [72], or terpenoid synthase (TPS [73]). Dimethylallyltryptophan synthases (DMATS) required for synthesis of prenylated indole-type metabolites are absent in F. graminearum but prominent in other fungi, especially Aspergillus [74].…”

Section: Plant Resistance To Small Molecule Effectors With a Role In mentioning

confidence: 99%

Fusarium Mycotoxins and Their Role in Plant–Pathogen Interactions

2015

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Discovery and Characterization of Terpenoid Biosynthetic Pathways of Fungi

Cited by 41 publications

References 51 publications

Identification of a Fungal 1,8-Cineole Synthase from Hypoxylon sp. with Specificity Determinants in Common with the Plant Synthases

Identification of a Fungal 1,8-Cineole Synthase from Hypoxylon sp. with Specificity Determinants in Common with the Plant Synthases

Novel family of terpene synthases evolved from trans -isoprenyl diphosphate synthases in a flea beetle

Fusarium Mycotoxins and Their Role in Plant–Pathogen Interactions

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