Relevant bibliographies by topics / Polyketide synthase genes

Academic literature on the topic 'Polyketide synthase genes'

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Published: 4 June 2021
Last updated: 11 February 2022

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Journal articles on the topic "Polyketide synthase genes"

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Xu, Yuquan, Patricia Espinosa-Artiles, Vivien Schubert, Ya-ming Xu, Wei Zhang, Min Lin, A. A. Leslie Gunatilaka, Roderich Süssmuth, and István Molnár. "Characterization of the Biosynthetic Genes for 10,11-Dehydrocurvularin, a Heat Shock Response-Modulating Anticancer Fungal Polyketide from Aspergillus terreus." Applied and Environmental Microbiology 79, no. 6 (January 18, 2013): 2038–47. http://dx.doi.org/10.1128/aem.03334-12.

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ABSTRACT10,11-Dehydrocurvularin is a prevalent fungal phytotoxin with heat shock response and immune-modulatory activities. It features a dihydroxyphenylacetic acid lactone polyketide framework with structural similarities to resorcylic acid lactones like radicicol or zearalenone. A genomic locus was identified from the dehydrocurvularin producer strainAspergillus terreusAH-02-30-F7 to reveal genes encoding a pair of iterative polyketide synthases (A. terreusCURS1 [AtCURS1] and AtCURS2) that are predicted to collaborate in the biosynthesis of 10,11-dehydrocurvularin. Additional genes in this locus encode putative proteins that may be involved in the export of the compound from the cell and in the transcriptional regulation of the cluster. 10,11-Dehydrocurvularin biosynthesis was reconstituted inSaccharomyces cerevisiaeby heterologous expression of the polyketide synthases. Bioinformatic analysis of the highly reducing polyketide synthase AtCURS1 and the nonreducing polyketide synthase AtCURS2 highlights crucial biosynthetic programming differences compared to similar synthases involved in resorcylic acid lactone biosynthesis. These differences lead to the synthesis of a predicted tetraketide starter unit that forms part of the 12-membered lactone ring of dehydrocurvularin, as opposed to the penta- or hexaketide starters in the 14-membered rings of resorcylic acid lactones. TetraketideN-acetylcysteamine thioester analogues of the starter unit were shown to support the biosynthesis of dehydrocurvularin and its analogues, with yeast expressing AtCURS2 alone. Differential programming of the product template domain of the nonreducing polyketide synthase AtCURS2 results in an aldol condensation with a different regiospecificity than that of resorcylic acid lactones, yielding the dihydroxyphenylacetic acid scaffold characterized by an S-type cyclization pattern atypical for fungal polyketides.
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FUJII, Isao. "Fungal Polyketide Synthase Genes." Journal of the agricultural chemical society of Japan 72, no. 1 (1998): 56–59. http://dx.doi.org/10.1271/nogeikagaku1924.72.56.

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Komaki, Hisayuki, Ryosuke Fudou, Takashi Iizuka, Daisuke Nakajima, Koei Okazaki, Daisuke Shibata, Makoto Ojika, and Shigeaki Harayama. "PCR Detection of Type I Polyketide Synthase Genes in Myxobacteria." Applied and Environmental Microbiology 74, no. 17 (July 7, 2008): 5571–74. http://dx.doi.org/10.1128/aem.00224-08.

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ABSTRACT The diversity of type I modular polyketide synthase (PKS) was explored by PCR amplification of DNA encoding ketosynthase and acyltransferase domains in myxobacteria. The sequencing of the amplicons revealed that many PKS genes were distantly related to the published sequences. Thus, myxobacteria may be excellent resources for novel and diverse polyketides.
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Rein, K. S., P. D. L. Gibbs, A. Palacios, L. Abiy, R. Dickey, R. V. Snyder, and J. V. Lopez. "Polyketide Synthase Genes from Marine Dinoflagellates." Marine Biotechnology 5, no. 1 (February 1, 2003): 1–12. http://dx.doi.org/10.1007/s10126-002-0077-y.

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OPANOWICZ, Magdalena, Juliane BLAHA, and Martin GRUBE. "Detection of paralogous polyketide synthase genes in Parmeliaceae by specific primers." Lichenologist 38, no. 1 (December 19, 2005): 47–54. http://dx.doi.org/10.1017/s0024282905005529.

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A first assessment of paralogy in non-reducing polyketide synthases of Parmeliaceae is presented. Primers which are specific to the keto-acyl synthase domain were used to amplify gene fragments of putative non-reducing polyketide synthases from various representatives of the family. The corresponding sequences were analysed together with a selection of known polyketide synthase genes from other fungi, including lichenized fungi. The results suggest that genes from Parmeliaceae represent at least 6 paralogs. Their different positions in the tree partly correlate with the variable presence of spliceosomal introns at particular positions in the gene fragments. Because only one paralog could be unambiguously detected in each species by direct sequencing of PCR products with this approach, we tested the applicability of clade-specific primers, designed by using orthologous signature sequences. With these primers more paralogs could be detected from the same DNA extract in a number of species, but certain paralogs were consistently not amplified in these species. The paralog-specific primer approach can potentially be used for a rapid screening of PKS genes from a broader range of lichen fungi.
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Gaffoor, Iffa, and Frances Trail. "Characterization of Two Polyketide Synthase Genes Involved in Zearalenone Biosynthesis in Gibberella zeae." Applied and Environmental Microbiology 72, no. 3 (March 2006): 1793–99. http://dx.doi.org/10.1128/aem.72.3.1793-1799.2006.

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ABSTRACT Zearalenone, a mycotoxin produced by several Fusarium spp., is most commonly found as a contaminant in stored grain and has chronic estrogenic effects on mammals. Zearalenone is a polyketide derived from the sequential condensation of multiple acetate units by a polyketide synthase (PKS), but the genetics of its biosynthesis are not understood. We cloned two genes, designated ZEA1 and ZEA2, which encode polyketide synthases that participate in the biosynthesis of zearalenone by Gibberella zeae (anamorph Fusarium graminearum). Disruption of either gene resulted in the loss of zearalenone production under inducing conditions. ZEA1 and ZEA2 are transcribed divergently from a common promoter region. Quantitative PCR analysis of both PKS genes and six flanking genes supports the view that the two polyketide synthases make up the core biosynthetic unit for zearalenone biosynthesis. An appreciation of the genetics of zearalenone biosynthesis is needed to understand how zearalenone is synthesized under field conditions that result in the contamination of grain.
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Zhang, Wenjun, Brian D. Ames, Shiou-Chuan Tsai, and Yi Tang. "Engineered Biosynthesis of a Novel Amidated Polyketide, Using the Malonamyl-Specific Initiation Module from the Oxytetracycline Polyketide Synthase." Applied and Environmental Microbiology 72, no. 4 (April 2006): 2573–80. http://dx.doi.org/10.1128/aem.72.4.2573-2580.2006.

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ABSTRACT Tetracyclines are aromatic polyketides biosynthesized by bacterial type II polyketide synthases (PKSs). Understanding the biochemistry of tetracycline PKSs is an important step toward the rational and combinatorial manipulation of tetracycline biosynthesis. To this end, we have sequenced the gene cluster of oxytetracycline (oxy and otc genes) PKS genes from Streptomyces rimosus. Sequence analysis revealed a total of 21 genes between the otrA and otrB resistance genes. We hypothesized that an amidotransferase, OxyD, synthesizes the malonamate starter unit that is a universal building block for tetracycline compounds. In vivo reconstitution using strain CH999 revealed that the minimal PKS and OxyD are necessary and sufficient for the biosynthesis of amidated polyketides. A novel alkaloid (WJ35, or compound 2) was synthesized as the major product when the oxy-encoded minimal PKS, the C-9 ketoreductase (OxyJ), and OxyD were coexpressed in CH999. WJ35 is an isoquinolone compound derived from an amidated decaketide backbone and cyclized with novel regioselectivity. The expression of OxyD with a heterologous minimal PKS did not afford similarly amidated polyketides, suggesting that the oxy-encoded minimal PKS possesses novel starter unit specificity.
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Bao, Wuli, Paul J. Sheldon, Evelyn Wendt-Pienkowski, and C. Richard Hutchinson. "The Streptomyces peucetius dpsC Gene Determines the Choice of Starter Unit in Biosynthesis of the Daunorubicin Polyketide." Journal of Bacteriology 181, no. 15 (August 1, 1999): 4690–95. http://dx.doi.org/10.1128/jb.181.15.4690-4695.1999.

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ABSTRACT The starter unit used in the biosynthesis of daunorubicin is propionyl coenzyme A (CoA) rather than acetyl-CoA, which is used in the production of most of the bacterial aromatic polyketides studied to date. In the daunorubicin biosynthesis gene cluster ofStreptomyces peucetius, directly downstream of the genes encoding the β-ketoacyl:acyl carrier protein synthase subunits, are two genes, dpsC and dpsD, encoding proteins that are believed to function as the starter unit-specifying enzymes. Recombinant strains containing plasmids carrying dpsC anddpsD, in addition to other daunorubicin polyketide synthase (PKS) genes, incorporate the correct starter unit into polyketides made by these genes, suggesting that, contrary to earlier reports, the enzymes encoded by dpsC and dpsD play a crucial role in starter unit specification. Additionally, the results of a cell-free synthesis of 21-carbon polyketides from propionyl-CoA and malonyl-CoA that used the protein extracts of recombinant strains carrying other daunorubicin PKS genes to which purified DpsC was added suggest that this enzyme has the primary role in starter unit discrimination for daunorubicin biosynthesis.
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Hong, Hui, Yuhui Sun, Yongjun Zhou, Emily Stephens, Markiyan Samborskyy, and Peter F. Leadlay. "Evidence for an iterative module in chain elongation on the azalomycin polyketide synthase." Beilstein Journal of Organic Chemistry 12 (October 11, 2016): 2164–72. http://dx.doi.org/10.3762/bjoc.12.206.

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The assembly-line synthases that produce bacterial polyketide natural products follow a modular paradigm in which each round of chain extension is catalysed by a different set or module of enzymes. Examples of deviation from this paradigm, in which a module catalyses either multiple extensions or none are of interest from both a mechanistic and an evolutionary viewpoint. We present evidence that in the biosynthesis of the 36-membered macrocyclic aminopolyol lactones (marginolactones) azalomycin and kanchanamycin, isolated respectively from Streptomyces malaysiensis DSM4137 and Streptomyces olivaceus Tü4018, the first extension module catalyses both the first and second cycles of polyketide chain extension. To confirm the integrity of the azl gene cluster, it was cloned intact on a bacterial artificial chromosome and transplanted into the heterologous host strain Streptomyces lividans, which does not possess the genes for marginolactone production. When furnished with 4-guanidinobutyramide, a specific precursor of the azalomycin starter unit, the recombinant S. lividans produced azalomycin, showing that the polyketide synthase genes in the sequenced cluster are sufficient to accomplish formation of the full-length polyketide chain. This provides strong support for module iteration in the azalomycin and kanchanamycin biosynthetic pathways. In contrast, re-sequencing of the gene cluster for biosynthesis of the polyketide β-lactone ebelactone in Streptomyces aburaviensis has shown that, contrary to a recently-published proposal, the ebelactone polyketide synthase faithfully follows the colinear modular paradigm.
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KHATUN, SAYRA, ALASTAIR C. W. WAUGH, MARIA B. REDPATH, and PAUL F. LONG. "Distribution of Polyketide Synthase Genes in Bacterial Populations." Journal of Antibiotics 55, no. 1 (2002): 107–8. http://dx.doi.org/10.7164/antibiotics.55.107.

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Dissertations / Theses on the topic "Polyketide synthase genes"

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Walsh, Maura Stephanie. "Cloning fungal polyketide synthase genes." Thesis, University of Bristol, 1993. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.333957.

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Wiesmann, Kristen E. H. "Engineering of the erythromycin-producing polyketide synthase." Thesis, University of Cambridge, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.264505.

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Roberts, Gareth A. "The erythromycin-producing polyketide synthase from Saccharopolyspora erythraea." Thesis, University of Cambridge, 1993. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.308298.

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Arrowsmith, Teresa Jayne. "Characterisation of putative polyketide synthase genes from Streptomyces cinnamonensis." Thesis, University of Southampton, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.292909.

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Yu, Tin-Wein. "Physical and functional studies of polyketide synthase genes of Streptomyces." Thesis, University of East Anglia, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.260005.

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Chooi, Yit Heng, and not supplied. "Genetic potential of lichen-forming fungi in polyketide biosynthesis." RMIT University. Applied Sciences, 2008. http://adt.lib.rmit.edu.au/adt/public/adt-VIT20081027.161315.

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Lichens produce a diverse array of bioactive secondary metabolites, many of which are unique to the organisms. Their potential applications, however, are limited by their finite sources and the slow-growing nature of the organisms in both laboratory and environmental conditions. This thesis set out to investigate polyketide synthase genes in lichens, with the ultimate goal of providing a sustainable source of lichen natural products to support these applications. To expand the diversity of PKS genes that could be detected in lichens, new degenerate primers targeting ketoacylsynthase (KS) domains of specific clades of PKS genes have been developed and tested on various lichen samples. Using these primers, 19 KS domains from various lichens were obtained. Phylogenetic analysis of the KS domains was used to infer the function of the PKS genes based on the predicted PKS domain architecture and chemical analysis by TLC and/or HPLC. KS domains from PKS clades not previously known in lichens were identified; this included the clade III NR (non-reducing)-PKSs, PR (partially reducing)-PKSs and HR (highly reducing)-PKSs. The discovery of clade III NR-PKSs with C-methyltransferase (CMeT) domain and their wide occurrence in lichens was especially significant. Based on the KS domain phylogenetic analysis and compounds detected in the individual lichens, the clade III NR-PKSs were hypothesized to be involved in the biosynthesis of β-orsellinic acid and methylphloroacetopheno ne - the monoaromatic precursors for many lichen coupled phenolic compounds, such as β-orcinol depsides/depsidones and usnic acid. A strategy has been developed to isolate clade III NR-PKSs directly from environmental lichen DNA using clade III NR-type KS amplified from the degenerate primers (NR3KS-F/R) as homologous probes. Another pair of degenerate primers specific to the CMeT domain of NR-PKSs has also been developed to facilitate the cloning and probing of new clade III NR-PKS genes in lichens. A clade III NR-PKS gene (xsepks1) from X. semiviridis was cloned successfully. This is the first report of the isolation of a full-length PKS gene from environmental lichen DNA. The domain architecture of xsepks1 is KS-AT-ACP-CMeT, as expected for a clade III NR-PKS, suggesting that the newly developed clade-specific primers are useful for cloning new clade III NR-PKS genes and that KS domain phylogenetic analysis can predict the functional domains in PKSs. Attempts were made to characterize the function of xsepks1 by heterologous expression in Aspergillus species. Both A. nidulans (transformed with 5´partial xsepks1 including native promoter) and A. oryzae (transformed with full-length xsepks1 under the regulation of starch-inducible amyB promoter) were tested as potential hosts for the expression of lichen PKS genes. Transcriptional analysis showed that A. nidulans could potentially utilize the lichen PKS gene promoter and both fungal hosts could splice the introns of a lichen PKS gene. Several compounds unique to the A. oryzae transformants carrying xsepks1 were detected, but they could not be reproduced in subsequent fermentations even though the gene was transcribed into mRNA. None of the expected products (β-orsellinic acid, methylphloroacetophenone or similar methylated monoaromatic compounds) was detected in A. oryzae transformants, and the function of xsepks1 remains to be determined. The other clade III NR-PKS genes detected in X. semiviridis cou ld also be responsible for the biosynthesis of β-orsellinic acid or methylphloroacetophenone, as precursors of the major secondary metabolites detected in X. semiviridis (i.e. fumarprotocetraric acid, succinprotocetraric acid and usnic acid). Overall, the work in this thesis demonstrated the prospect of using a molecular approach to access the lichen biosynthetic potential without going through the cumbersome culturing stage.
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Morris, Nathan Z. "Molecular detection of type II polyketide synthase genes in Cuban soils." Thesis, University of Warwick, 2000. http://wrap.warwick.ac.uk/59431/.

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Molecular detection methods were developed to study the distribution of type II polyketide synthase (PKS) genes in Cuban soils. A PCR based detection method targeting the α and β ketosynthase genes was applied to a number of different total community DNA samples. These genes were detected in 43% of samples tested from a number of different locations. A botanical garden site located in Havana, Cuba, was found to show the greatest distribution of type II PKS genes across the sites tested. It was not possible to amplify type II PKS genes from a pristine island site off the coast of Cuba. Further investigation revealed that actinornycetes containing type II PKS were present in the soil community at a level above the detection limit of the PCR protocol. Further total community DNA cleanup steps failed to allow the detection of type II PKS genes within the DNA samples suggesting PCR inhibition was responsible for negative results. The molecular detection of type II PKS genes in total community DNA was compared to the detection of type II PKS genes in actinomycete isolates. A lack of correlation between these two approaches was observed with the molecular detection limit unable to amplify type II PKS genes in <50% of crop soils tested. Actinomycetes containing type II PKS genes could be isolated from all crop soils tested. No difference was seen in the detection of type II PKS genes between rhizosphere and bulk soil samples. Actinomycetes were isolated using a selective isolation procedure at a level of approximately 10(7) cfu g-1 soil compared to 10(8) cfu g-1 for total bacterial counts. Actinomycetes were isolated from Cuban crop soils and screened for the presence of type II PKS genes. Out of 100 isolates 26 were found to contain the genes of interest. Phylogenetic analysis of these isolates based on 16S rDNA and recA sequence data showed them to be closely grouped within the streptomycetes. Sequence data based on KSα genes from Cuban isolates showed them to be representative of both spore pigment and antibiotic polyketide genes. A representative clone library was constructed containing type II PKS genes amplified from total community DNA. Rhizosphere and bulk soil samples were compared from the same site. Sequences obtained from rhizosphere total community DNA appeared to be widely distributed when compared to published sequences and included examples of both spore pigment and antibiotic polyketide genes. A molecular method was developed to amplify near full length α and β KS genes from type II PKS gene clusters. Expression vectors were constructed to allow these genes to be expressed along with an ACP to give a functional minimal PKS for polyketide chain production. This method was used on total community DNA in an attempt to extract diverse genes from as yet uncultured organisms.
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Punya, Juntira. "Polyketide synthase genes from the wood-decaying fungus Xylaria sp. BCC1067." Thesis, University of Westminster, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.251721.

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Nicholson, Thomas Peter. "Design and development of oligonucleotide probes for novel fungal polyketide synthase genes." Thesis, University of Bristol, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.322607.

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Kim, Kwang Hyung. "Functional Analysis of Secondary Metabolite Biosynthesis-Related Genes in Alternaria brassicicola." Diss., Virginia Tech, 2009. http://hdl.handle.net/10919/39452.

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Alternaria brassicicola is a necrotrophic pathogen that causes black spot disease on virtually all cultivated Brassicas, A. brassicicola is renowned for its ability to prodigiously produce secondary metabolites. To test the hypothesis that secondary metabolites produced by A. brassicicola contribute to pathogenicity, we identified seven nonribosomal peptide synthetases (NPSs) and 10 polyketide synthases (PKSs) in the A. brassicicola genome. The phenotype resulting from knockout mutations of each PKS and NPS gene was investigated with an emphasis on discovery of fungal virulence factors. A highly efficient gene disruption method using a short linear double stranded DNA construct with minimal elements was developed, optimized, and used to functionally disrupt all NPS and PKS genes in A. brassicicola. Three NPS and two PKS genes, and one NPS-like gene appeared to be virulence factors based upon reduced lesion development of each mutant on inoculated green cabbage and Arabidopsis compared with the wild-type strain. Furthermore some of the KO mutants exhibited developmental phenotypic changes in pigmentation and conidiogenesis. To further characterize the roles of several genes of interest in A. brassicicola development and pathogenesis, the genes AbNPS2, AbPKS9, and NPS-like tmpL were selected for in-depth functional analysis. We provide substantial evidence that the AbNPS2-associated metabolite is involved in conidial cell wall construction, possibly as an anchor connecting two cell wall layers. We also characterized a biosynthetic gene cluster harboring the AbPKS9 gene and demonstrated that this cluster is responsible for the biosynthesis of depudecin, an inhibitor of histone deacetylases and a minor virulence factor. Finally, we demonstrated that a NPS-like protein named TmpL is involved in a filamentous fungi-specific mechanism for regulating levels of intracellular reactive oxygen species during conidiation and pathogenesis in both plant and animal pathogenic fungi. Collectively our results indicate that small molecule nonribosomal peptides and polyketides in A. brassicicola play diverse, but also fundamental, roles in fungal development and pathogenesis.
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Book chapters on the topic "Polyketide synthase genes"

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Hrazdina, Geza, and Desen Zheng. "Expression and Function of Aromatic Polyketide Synthase Genes in Raspberries (Rubus idaeussp.)." In ACS Symposium Series, 128–40. Washington, DC: American Chemical Society, 2007. http://dx.doi.org/10.1021/bk-2007-0955.ch009.

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Anand, Swadha, and Debasisa Mohanty. "Computational Methods for Identification of Novel Secondary Metabolite Biosynthetic Pathways by Genome Analysis." In Handbook of Research on Computational and Systems Biology, 380–405. IGI Global, 2011. http://dx.doi.org/10.4018/978-1-60960-491-2.ch018.

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Secondary metabolites belonging to polyketide and nonribosomal peptide families constitute a major class of natural products with diverse biological functions and a variety of pharmaceutically important properties. Experimental studies have shown that the biosynthetic machinery for polyketide and nonribosomal peptides involves multi-functional megasynthases like Polyketide Synthases (PKSs) and nonribosomal peptide synthetases (NRPSs) which utilize a thiotemplate mechanism similar to that for fatty acid biosynthesis. Availability of complete genome sequences for an increasing number of microbial organisms has provided opportunities for using in silico genome mining to decipher the secondary metabolite natural product repertoire encoded by these organisms. Therefore, in recent years there have been major advances in development of computational methods which can analyze genome sequences to identify genes involved in secondary metabolite biosynthesis and help in deciphering the putative chemical structures of their biosynthetic products based on analysis of the sequence and structural features of the proteins encoded by these genes. These computational methods for deciphering the secondary metabolite biosynthetic code essentially involve identification of various catalytic domains present in this PKS/NRPS family of enzymes; a prediction of various reactions in these enzymatic domains and their substrate specificities and also precise identification of the order in which these domains would catalyze various biosynthetic steps. Structural bioinformatics analysis of known secondary metabolite biosynthetic clusters has helped in formulation of predictive rules for deciphering domain organization, substrate specificity, and order of substrate channeling. In this chapter, the progress in development of various computational methods is discussed by different research groups, and specifically, the utility in identification of novel metabolites by genome mining and rational design of natural product analogs by biosynthetic engineering studies.
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