Relevant bibliographies by topics / Polyketide synthase (PKS-I)

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Academic literature on the topic 'Polyketide synthase (PKS-I)'

Author: Grafiati
Published: 3 June 2025
Last updated: 1 August 2025

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Journal articles on the topic "Polyketide synthase (PKS-I)"

1

Komaki, Hisayuki, Ryosuke Fudou, Takashi Iizuka, et al. "PCR Detection of Type I Polyketide Synthase Genes in Myxobacteria." Applied and Environmental Microbiology 74, no. 17 (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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Graziani, Stephane, Christelle Vasnier, and Marie-Josee Daboussi. "Novel Polyketide Synthase from Nectria haematococca." Applied and Environmental Microbiology 70, no. 5 (2004): 2984–88. http://dx.doi.org/10.1128/aem.70.5.2984-2988.2004.

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ABSTRACT We identified a polyketide synthase (PKS) gene, pksN, from a strain of Nectria haematococca by complementing a mutant unable to synthesize a red perithecial pigment. pksN encodes a 2,106-amino-acid polypeptide with conserved motifs characteristic of type I PKS enzymatic domains: β-ketoacyl synthase, acyltransferase, duplicated acyl carrier proteins, and thioesterase. The pksN product groups with the Aspergillus nidulans WA-type PKSs involved in conidial pigmentation and melanin, bikaverin, and aflatoxin biosynthetic pathways. Inactivation of pksN did not cause any visible change in fu
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3

Sucipto, H., J. H. Sahner, E. Prusov та ін. "In vitro reconstitution of α-pyrone ring formation in myxopyronin biosynthesis". Chemical Science 6, № 8 (2015): 5076–85. http://dx.doi.org/10.1039/c5sc01013f.

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α-Pyrone rings exist in many polyketide synthase (PKS) derived natural products. We report the first in vitro reconstitution of α-pyrone ring formation by a type I PKS using chemically synthesized substrates.
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4

Lohman, Jeremy R., Ming Ma, Jerzy Osipiuk, et al. "Structural and evolutionary relationships of “AT-less” type I polyketide synthase ketosynthases." Proceedings of the National Academy of Sciences 112, no. 41 (2015): 12693–98. http://dx.doi.org/10.1073/pnas.1515460112.

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Acyltransferase (AT)-less type I polyketide synthases (PKSs) break the type I PKS paradigm. They lack the integrated AT domains within their modules and instead use a discrete AT that acts in trans, whereas a type I PKS module minimally contains AT, acyl carrier protein (ACP), and ketosynthase (KS) domains. Structures of canonical type I PKS KS-AT didomains reveal structured linkers that connect the two domains. AT-less type I PKS KSs have remnants of these linkers, which have been hypothesized to be AT docking domains. Natural products produced by AT-less type I PKSs are very complex because
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5

Grijseels, Sietske, Carsten Pohl, Jens Christian Nielsen, et al. "Identification of the decumbenone biosynthetic gene cluster in Penicillium decumbens and the importance for production of calbistrin." Fungal Biology and Biotechnology 5, no. 1 (2018): 18. https://doi.org/10.1186/s40694-018-0063-4.

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<strong>Background: </strong>Filamentous fungi are important producers of secondary metabolites, low molecular weight molecules that often have bioactive properties. Calbistrin A is a secondary metabolite with an interesting structure that was recently found to have bioactivity against leukemia cells. It consists of two polyketides linked by an ester bond: a bicyclic decalin containing polyketide with structural similarities to lovastatin, and a linear 12 carbon dioic acid structure. Calbistrin A is known to be produced by several uniseriate black Aspergilli, <i>Aspergillus versicolor</i>-rela
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6

Trindade-Silva, Amaro E., Cintia P. J. Rua, Bruno G. N. Andrade, et al. "Polyketide Synthase Gene Diversity within the Microbiome of the Sponge Arenosclera brasiliensis, Endemic to the Southern Atlantic Ocean." Applied and Environmental Microbiology 79, no. 5 (2012): 1598–605. http://dx.doi.org/10.1128/aem.03354-12.

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ABSTRACTMicrobes associated with marine sponges are considered important producers of bioactive, structurally unique polyketides. The synthesis of such secondary metabolites involves type I polyketide synthases (PKSs), which are enzymes that reach a maximum complexity degree in bacteria. The Haplosclerida spongeArenosclera brasiliensishosts a complex microbiota and is the source of arenosclerins, alkaloids with cytotoxic and antibacterial activity. In the present investigation, we performed high-throughput sequencing of the ketosynthase (KS) amplicon to investigate the diversity of PKS genes p
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Amnuaykanjanasin, Alongkorn, Suranat Phonghanpot, Nattapong Sengpanich, Supapon Cheevadhanarak, and Morakot Tanticharoen. "Insect-Specific Polyketide Synthases (PKSs), Potential PKS-Nonribosomal Peptide Synthetase Hybrids, and Novel PKS Clades in Tropical Fungi." Applied and Environmental Microbiology 75, no. 11 (2009): 3721–32. http://dx.doi.org/10.1128/aem.02744-08.

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ABSTRACT Polyketides draw much attention because of their potential use in pharmaceutical and biotechnological applications. This study identifies an abundant pool of polyketide synthase (PKS) genes from local isolates of tropical fungi found in Thailand in three different ecological niches: insect pathogens, marine inhabitants, and lichen mutualists. We detected 149 PKS genes from 48 fungi using PCR with PKS-specific degenerate primers. We identified and classified 283 additional PKS genes from 13 fungal genomes. Phylogenetic analysis of all these PKS sequences the comprising ketosynthase (KS
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8

Schirmer, Andreas, Rishali Gadkari, Christopher D. Reeves, Fadia Ibrahim, Edward F. DeLong, and C. Richard Hutchinson. "Metagenomic Analysis Reveals Diverse Polyketide Synthase Gene Clusters in Microorganisms Associated with the Marine Sponge Discodermia dissoluta." Applied and Environmental Microbiology 71, no. 8 (2005): 4840–49. http://dx.doi.org/10.1128/aem.71.8.4840-4849.2005.

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ABSTRACT Sponge-associated bacteria are thought to produce many novel bioactive compounds, including polyketides. PCR amplification of ketosynthase domains of type I modular polyketide synthases (PKS) from the microbial community of the marine sponge Discodermia dissoluta revealed great diversity and a novel group of sponge-specific PKS ketosynthase domains. Metagenomic libraries totaling more than four gigabases of bacterial genomes associated with this sponge were screened for type I modular PKS gene clusters. More than 90% of the clones in total sponge DNA libraries represented bacterial DN
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Gaffoor, Iffa, Daren W. Brown, Ron Plattner, Robert H. Proctor, Weihong Qi, and Frances Trail. "Functional Analysis of the Polyketide Synthase Genes in the Filamentous Fungus Gibberella zeae (Anamorph Fusarium graminearum)." Eukaryotic Cell 4, no. 11 (2005): 1926–33. http://dx.doi.org/10.1128/ec.4.11.1926-1933.2005.

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ABSTRACT Polyketides are a class of secondary metabolites that exhibit a vast diversity of form and function. In fungi, these compounds are produced by large, multidomain enzymes classified as type I polyketide synthases (PKSs). In this study we identified and functionally disrupted 15 PKS genes from the genome of the filamentous fungus Gibberella zeae. Five of these genes are responsible for producing the mycotoxins zearalenone, aurofusarin, and fusarin C and the black perithecial pigment. A comprehensive expression analysis of the 15 genes revealed diverse expression patterns during grain co
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Nguyen, Hoang Nhat Tan, Thi Truc Mai Ha, Thi Thuy Duong Luong, and Vu Phong Nguyen. "Biological characteristics and ability of Streptomyces rochei BT02 to inhibit the Ralstonia solanacearum causing bacterial wilt disease." Ministry of Science and Technology, Vietnam 65, no. 7 (2023): 67–72. http://dx.doi.org/10.31276/vjst.65(7).67-72.

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In the agricultural field, actinomycetes are outstanding biological control agents to inhibit the growth of pathogenic microorganisms. Based on the manual of bacterial classification of the International Streptomyces Project (ISP) and the 16S-rRNA gene sequence, the actinomycete BT02 strain was named Streptomyces rochei BT02. This strain contains two polyketide synthase type I (pks-I) and polyketide synthase type II (pks-II) genes related to antibiotic synthesis. The result showed that the actinomycetes S. rochei BT02 grow well at 31οC, 1% salt, pH 7.0, and assimilate different carbon and nitr
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Book chapters on the topic "Polyketide synthase (PKS-I)"

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Nowruzi, Bahareh. "Cyanobacteria Natural Products as Sources for Future Directions in Antibiotic Drug Discovery." In Cyanobacteria - Recent Advances and New Perspectives [Working Title]. IntechOpen, 2022. http://dx.doi.org/10.5772/intechopen.106364.

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Cyanobacteria, an abundant source of natural products with a broad diversity of secondary metabolites, have emerged as a novel resource for the progression of synthetic analogs. Due to the rise of antibiotic resistance, there is a need for new medications and cyanobacteria-derived compounds have shown promising important alternatives for new therapeutics. These secondary metabolites are produced through nonribosomal peptide synthetase (NRPS), polyketide synthase (PKS), and mainly through mixed NRPS-PKS enzymatic systems. Current research is focused on the exploitation of cyanobacteria for the
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