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Journal articles on the topic 'Peptide Synthetase'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Annis, Seanna L., and Daniel G. Panaccione. "Presence of peptide synthetase gene transcripts and accumulation of ergopeptines in Claviceps purpurea and Neotyphodium coenophialum." Canadian Journal of Microbiology 44, no. 1 (1998): 80–86. http://dx.doi.org/10.1139/w97-130.

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The production of toxic ergopeptine alkaloids by the fungi Claviceps purpurea and Neotyphodium coenophialum involves the activity of one or more nonribosomal peptide synthetases. Claviceps purpurea and N. coenophialum each have several different peptide synthetase genes, fragments of which have been cloned previously. An additional Claviceps purpurea peptide synthetase gene was cloned by hybridization with one of the N. coenophialum peptide synthetase gene fragments. We detected the presence of mRNA from the peptide synthetase genes in cultures of different ages grown under conditions favorabl

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2

Rajendran, Narayanan. "Identification and Cloning of a Gene Locus Encoding Peptide Synthetase of Pseudomonas fluorescens by Two Sets of PCR Primers." Zeitschrift für Naturforschung C 54, no. 1-2 (1999): 105–9. http://dx.doi.org/10.1515/znc-1999-1-218.

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A chromosomal locus encoding biosynthetic genes for a putative peptide synthetase of Pseudomonas fluorescens was identified and cloned. To achieve this, two sets of degenerated oligonucleotide primers KAGGA:SGTTG and TGD :LGG were used in PCR. These primers were selected based on highly conserved units of known peptide synthetases involved in adenylation and thiolation regions of Bacillus subtilis. The discrete amplified bands from PCR ca. 300 bp for KAGGA:SGTTG and ca. 500 bp for TGD:LGG proved to be integral part of the genomic DNA of P. fluorescens were cloned and sequenced. Sequence alignm

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3

Johnson, R. D., L. Johnson, Y. Itoh, M. Kodama, H. Otani, and K. Kohmoto. "Cloning and Characterization of a Cyclic Peptide Synthetase Gene from Alternaria alternata Apple Pathotype Whose Product Is Involved in AM-Toxin Synthesis and Pathogenicity." Molecular Plant-Microbe Interactions® 13, no. 7 (2000): 742–53. http://dx.doi.org/10.1094/mpmi.2000.13.7.742.

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Alternaria alternata apple pathotype causes Alternaria blotch of susceptible apple cultivars through the production of a cyclic peptide host-specific toxin, AM-toxin. PCR (polymerase chain reaction), with primers designed to conserved domains of peptide synthetase genes, amplified several products from A. alternata apple pathotype that showed high similarity to other fungal peptide synthetases and were specific to the apple pathotype. Screening of a Lambda Zap genomic library with these PCR-generated probes identified overlapping clones containing a complete cyclic peptide synthetase gene of 1

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4

Puri, Rajinder N., та John W. Porter. "Isolation, purification, and characterization of a peptide that contains the β-ketoacyl reductase, enoyl reductase, and β-hydroxyacyl dehydrase activities of the pigeon liver fatty acid synthetase". Canadian Journal of Biochemistry and Cell Biology 63, № 1 (1985): 50–56. http://dx.doi.org/10.1139/o85-007.

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Controlled proteolytic cleavage of pigeon liver fatty acid synthetase with elastase (4% w/w) for 5 h yields two peptides that are designated II and IV. After 5 h of proteolysis the incubation mixture containing these peptides retains all of the component enzyme activities of the fatty acid synthetase complex. The two peptides are then separated by chromatography on an Affi-Gel Blue column. Gel filtration of the fraction containing peptide II yields a homogeneous peptide as shown by polyacrylamide gel electrophoresis in the presence and absence of sodium dodecyl sulfate. The molecular weight of

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5

Neilan, Brett A., Elke Dittmann, Leo Rouhiainen, et al. "Nonribosomal Peptide Synthesis and Toxigenicity of Cyanobacteria." Journal of Bacteriology 181, no. 13 (1999): 4089–97. http://dx.doi.org/10.1128/jb.181.13.4089-4097.1999.

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ABSTRACT Nonribosomal peptide synthesis is achieved in prokaryotes and lower eukaryotes by the thiotemplate function of large, modular enzyme complexes known collectively as peptide synthetases. These and other multifunctional enzyme complexes, such as polyketide synthases, are of interest due to their use in unnatural-product or combinatorial biosynthesis (R. McDaniel, S. Ebert-Khosla, D. A. Hopwood, and C. Khosla, Science 262:1546–1557, 1993; T. Stachelhaus, A. Schneider, and M. A. Marahiel, Science 269:69–72, 1995). Most nonribosomal peptides from microorganisms are classified as secondary

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6

Wilhite, S. E., R. D. Lumsden, and D. C. Straney. "Peptide Synthetase Gene in Trichoderma virens." Applied and Environmental Microbiology 67, no. 11 (2001): 5055–62. http://dx.doi.org/10.1128/aem.67.11.5055-5062.2001.

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ABSTRACT Trichoderma virens (synonym, Gliocladium virens), a deuteromycete fungus, suppresses soilborne plant diseases caused by a number of fungi and is used as a biocontrol agent. Several traits that may contribute to the antagonistic interactions ofT. virens with disease-causing fungi involve the production of peptide metabolites (e.g., the antibiotic gliotoxin and siderophores used for iron acquisition). We cloned a 5,056-bp partial cDNA encoding a putative peptide synthetase (Psy1) fromT. virens using conserved motifs found within the adenylate domain of peptide synthetases. Sequence simi

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7

Schauwecker, Florian, Frank Pfennig, Werner Schröder, and Ullrich Keller. "Molecular Cloning of the Actinomycin Synthetase Gene Cluster from Streptomyces chrysomallus and Functional Heterologous Expression of the Gene Encoding Actinomycin Synthetase II." Journal of Bacteriology 180, no. 9 (1998): 2468–74. http://dx.doi.org/10.1128/jb.180.9.2468-2474.1998.

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ABSTRACT The actinomycin synthetases ACMS I, II, and III catalyze the assembly of the acyl peptide lactone precursor of actinomycin by a nonribosomal mechanism. We have cloned the genes of ACMS I (acmA) and ACMS II (acmB) by hybridization screening of a cosmid library of Streptomyces chrysomallusDNA with synthetic oligonucleotides derived from peptide sequences of the two enzymes. Their genes were found to be closely linked and are arranged in opposite orientations. Hybridization mapping and partial sequence analyses indicate that the gene of an additional peptide synthetase, most likely the g

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8

Baldwin, J. E., C. Y. Shiau, M. F. Byford та C. J. Schofield. "Substrate specificity of l-δ-(α-aminoadipoyl)-l-cysteinyl-d-valine synthetase from Cephalosporium acremonium: demonstration of the structure of several unnatural tripeptide products". Biochemical Journal 301, № 2 (1994): 367–72. http://dx.doi.org/10.1042/bj3010367.

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Potential substrates for L-delta-(alpha-aminoadipoyl)-L-(cysteinyl)-D-valine (ACV) synthetase were initially identified using both the amino-acid-dependent ATP<-->pyrophosphate exchange reaction catalysed by the enzyme and the incorporation of 14C-radiolabelled cysteine and valine into potential peptide products. S-Carboxymethylcysteine was an effective substitute for alpha-aminoadipate and both allylglycine and vinylglycine could substitute for cysteine, indicating that the thiol group of cysteine is not essential for peptide formation. L-allo-Isoleucine but not L-isoleucine substituted

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9

Abe, Tomoko, Yoshiteru Hashimoto, Ye Zhuang, Yin Ge, Takuto Kumano, and Michihiko Kobayashi. "Peptide Bond Synthesis by a Mechanism Involving an Enzymatic Reaction and a Subsequent Chemical Reaction." Journal of Biological Chemistry 291, no. 4 (2015): 1735–50. http://dx.doi.org/10.1074/jbc.m115.700989.

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We recently reported that an amide bond is unexpectedly formed by an acyl-CoA synthetase (which catalyzes the formation of a carbon-sulfur bond) when a suitable acid and l-cysteine are used as substrates. DltA, which is homologous to the adenylation domain of nonribosomal peptide synthetase, belongs to the same superfamily of adenylate-forming enzymes, which includes many kinds of enzymes, including the acyl-CoA synthetases. Here, we demonstrate that DltA synthesizes not only N-(d-alanyl)-l-cysteine (a dipeptide) but also various oligopeptides. We propose that this enzyme catalyzes peptide syn

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10

Ackerley, David F., Tom T. Caradoc-Davies, and Iain L. Lamont. "Substrate Specificity of the Nonribosomal Peptide Synthetase PvdD from Pseudomonas aeruginosa." Journal of Bacteriology 185, no. 9 (2003): 2848–55. http://dx.doi.org/10.1128/jb.185.9.2848-2855.2003.

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ABSTRACT Pseudomonas aeruginosa PAO1 secretes a siderophore, pyoverdinePAO, which contains a short peptide attached to a dihydroxyquinoline moiety. Synthesis of this peptide is thought to be catalyzed by nonribosomal peptide synthetases, one of which is encoded by the pvdD gene. The first module of pvdD was overexpressed in Escherichia coli, and the protein product was purified. l-Threonine, one of the amino acid residues in pyoverdinePAO, was an effective substrate for the recombinant protein in ATP-PPi exchange assays, showing that PvdD has peptide synthetase activity. Other amino acids, inc

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11

Christiansen, Guntram, Jutta Fastner, Marcel Erhard, Thomas Börner, and Elke Dittmann. "Microcystin Biosynthesis in Planktothrix: Genes, Evolution, and Manipulation." Journal of Bacteriology 185, no. 2 (2003): 564–72. http://dx.doi.org/10.1128/jb.185.2.564-572.2003.

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ABSTRACT Microcystins represent an extraordinarily large family of cyclic heptapeptide toxins that are nonribosomally synthesized by various cyanobacteria. Microcystins specifically inhibit the eukaryotic protein phosphatases 1 and 2A. Their outstanding variability makes them particularly useful for studies on the evolution of structure-function relationships in peptide synthetases and their genes. Analyses of microcystin synthetase genes provide valuable clues for the potential and limits of combinatorial biosynthesis. We have sequenced and analyzed 55.6 kb of the potential microcystin synthe

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12

Payne, Jennifer A. E., Melanie Schoppet, Mathias Henning Hansen, and Max J. Cryle. "Diversity of nature's assembly lines – recent discoveries in non-ribosomal peptide synthesis." Molecular BioSystems 13, no. 1 (2017): 9–22. http://dx.doi.org/10.1039/c6mb00675b.

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13

Bloudoff, Kristjan, Christopher D. Fage, Mohamed A. Marahiel, and T. Martin Schmeing. "Structural and mutational analysis of the nonribosomal peptide synthetase heterocyclization domain provides insight into catalysis." Proceedings of the National Academy of Sciences 114, no. 1 (2016): 95–100. http://dx.doi.org/10.1073/pnas.1614191114.

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Nonribosomal peptide synthetases (NRPSs) are a family of multidomain, multimodule enzymes that synthesize structurally and functionally diverse peptides, many of which are of great therapeutic or commercial value. The central chemical step of peptide synthesis is amide bond formation, which is typically catalyzed by the condensation (C) domain. In many NRPS modules, the C domain is replaced by the heterocyclization (Cy) domain, a homologous domain that performs two consecutive reactions by using hitherto unknown catalytic mechanisms. It first catalyzes amide bond formation, and then the intram

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14

Eys, S., D. Schwartz, W. Wohlleben, and E. Schinko. "Three Thioesterases Are Involved in the Biosynthesis of Phosphinothricin Tripeptide in Streptomyces viridochromogenes Tü494." Antimicrobial Agents and Chemotherapy 52, no. 5 (2008): 1686–96. http://dx.doi.org/10.1128/aac.01053-07.

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ABSTRACT Phosphinothricin tripeptide (PTT) is a peptide antibiotic produced by Streptomyces viridochromogenes Tü494, and it is synthesized by nonribosomal peptide synthetases. The PTT biosynthetic gene cluster contains three peptide synthetase genes: phsA, phsB, and phsC. Each of these peptide synthetases comprises only one module. In neither PhsB nor PhsC is a typical C-terminal thioesterase domain present. In contrast, a single thioesterase GXSXG motif has been identified in the N terminus of the first peptide synthetase, PhsA. In addition, two external thioesterase genes, theA and theB, ar

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15

Kim, Dong Kyu, Hyun Joo Lee, Jiwon Kong, Ha Yeon Cho, Sunghoon Kim, and Beom Sik Kang. "Structural basis for the dynamics of human methionyl-tRNA synthetase in multi-tRNA synthetase complexes." Nucleic Acids Research 49, no. 11 (2021): 6549–68. http://dx.doi.org/10.1093/nar/gkab453.

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Abstract In mammals, eight aminoacyl-tRNA synthetases (AARSs) and three AARS-interacting multifunctional proteins (AIMPs) form a multi-tRNA synthetase complex (MSC). MSC components possess extension peptides for MSC assembly and specific functions. Human cytosolic methionyl-tRNA synthetase (MRS) has appended peptides at both termini of the catalytic main body. The N-terminal extension includes a glutathione transferase (GST) domain responsible for interacting with AIMP3, and a long linker peptide between the GST and catalytic domains. Herein, we determined crystal structures of the human MRS c

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16

Reimer, Janice M., Maximilian Eivaskhani, Ingrid Harb, Alba Guarné, Martin Weigt, and T. Martin Schmeing. "Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility." Science 366, no. 6466 (2019): eaaw4388. http://dx.doi.org/10.1126/science.aaw4388.

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Nonribosomal peptide synthetases (NRPSs) are biosynthetic enzymes that synthesize natural product therapeutics using a modular synthetic logic, whereby each module adds one aminoacyl substrate to the nascent peptide. We have determined five x-ray crystal structures of large constructs of the NRPS linear gramicidin synthetase, including a structure of a full core dimodule in conformations organized for the condensation reaction and intermodular peptidyl substrate delivery. The structures reveal differences in the relative positions of adjacent modules, which are not strictly coupled to the cata

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17

Samel, Stefan A., Paul Czodrowski, and Lars-Oliver Essen. "Structure of the epimerization domain of tyrocidine synthetase A." Acta Crystallographica Section D Biological Crystallography 70, no. 5 (2014): 1442–52. http://dx.doi.org/10.1107/s1399004714004398.

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Tyrocidine, a macrocyclic decapeptide fromBacillus brevis, is nonribosomally assembled by a set of multimodular peptide synthetases, which condense two D-amino acids and eight L-amino acids to produce this membrane-disturbing antibiotic. D-Phenylalanine, the first amino acid incorporated into tyrocidine, is catalytically derived from enzyme-bound L-Phe by the C-terminal epimerization (E) domain of tyrocidine synthetase A (TycA). The 1.5 Å resolution structure of the cofactor-independent TycA E domain reveals an intimate relationship to the condensation (C) domains of peptide synthetases. In co

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18

Scholz-Schroeder, Brenda K., Jonathan D. Soule, and Dennis C. Gross. "The sypA, sypB, and sypC Synthetase Genes Encode Twenty-Two Modules Involved in the Nonribosomal Peptide Synthesis of Syringopeptin by Pseudomonas syringae pv. syringae B301D." Molecular Plant-Microbe Interactions® 16, no. 4 (2003): 271–80. http://dx.doi.org/10.1094/mpmi.2003.16.4.271.

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Syringopeptin is a necrosis-inducing phytotoxin, composed of 22 amino acids attached to a 3-hydroxy fatty acid tail. Syringopeptin, produced by Pseudomonas syringae pv. syringae, functions as a virulence determinant in the plant-pathogen interaction. A 73,800-bp DNA region was sequenced, and analysis identified three large open reading frames, sypA, sypB, and sypC, that are 16.1, 16.3, and 40.6 kb in size. Sequence analysis of the putative SypA, SypB, and SypC sequences determined that they are homologous to peptide synthetases, containing five, five, and twelve amino acid activation modules,

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Scholz-Schroeder, Brenda K., Michael L. Hutchison, Ingeborg Grgurina, and Dennis C. Gross. "The Contribution of Syringopeptin and Syringomycin to Virulence of Pseudomonas syringae pv. syringae strain B301D on the Basis of sypA and syrB1 Biosynthesis Mutant Analysis." Molecular Plant-Microbe Interactions® 14, no. 3 (2001): 336–48. http://dx.doi.org/10.1094/mpmi.2001.14.3.336.

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Sequencing of an approximately 3.9-kb fragment downstream of the syrD gene of Pseudomonas syringae pv. syringae strain B301D revealed that this region, designated sypA, codes for a peptide synthetase, a multifunctional enzyme involved in the thiotemplate mechanism of peptide biosynthesis. The translated protein sequence encompasses a complete amino acid activation module containing the conserved domains characteristic of peptide synthetases. Analysis of the substrate specificity region of this module indicates that it incorporates 2,3-dehydroaminobutyric acid into the syringopeptin peptide str

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20

Mukhopadhyay, N. K., S. Majumder, S. K. Ghosh, and S. K. Bose. "Characterization of three-fraction mycobacillin synthetase." Biochemical Journal 235, no. 3 (1986): 639–43. http://dx.doi.org/10.1042/bj2350639.

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Mycobacillin synthetase lacks aspartic acid racemase, alanine racemase and glutamic acid racemase activities. The enzyme also does not respond to ATP-[32P]Pi exchange, nor does it catalyse the antibiotic synthesis in presence of amino acids of configuration opposite to that present in the molecule. Preincubation with optical isomers of opposite configuration inhibited the ATP-[32P]Pi exchange reaction to the extent of 60-90%. None of the three fractions of mycobacillin synthetase contained a pantothenic acid arm. Two molecules of ATP are required to synthesize one peptide bond of mycobacillin.

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21

Cubillos-Ruiz, Andres, Jessie W. Berta-Thompson, Jamie W. Becker, Wilfred A. van der Donk, and Sallie W. Chisholm. "Evolutionary radiation of lanthipeptides in marine cyanobacteria." Proceedings of the National Academy of Sciences 114, no. 27 (2017): E5424—E5433. http://dx.doi.org/10.1073/pnas.1700990114.

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Lanthipeptides are ribosomally derived peptide secondary metabolites that undergo extensive posttranslational modification. Prochlorosins are a group of lanthipeptides produced by certain strains of the ubiquitous marine picocyanobacteriaProchlorococcusandSynechococcus. Unlike other lanthipeptide-producing bacteria, picocyanobacteria use an unprecedented mechanism of substrate promiscuity for the production of numerous and diverse lanthipeptides using a single lanthionine synthetase. Through a cross-scale analysis of prochlorosin biosynthesis genes—from genomes to oceanic populations—we show t

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22

Lautru, Sylvie, and Gregory L. Challis. "Substrate recognition by nonribosomal peptide synthetase multi-enzymes." Microbiology 150, no. 6 (2004): 1629–36. http://dx.doi.org/10.1099/mic.0.26837-0.

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Nonribosomal peptide synthetases (NRPSs) are giant multi-domain enzymes that catalyse the biosynthesis of many commercially important peptides produced by bacteria and fungi. Several studies over the last decade have shown that many of the individual domains within NRPSs exhibit significant substrate selectivity, which impacts on our ability to engineer NRPSs to produce new bioactive microbial peptides. Adenylation domains appear to be the primary determinants of substrate selectivity in NRPSs. Much progress has been made towards an empirical understanding of substrate selection by these domai

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23

Ramarathnam, Rajesh, Shen Bo, Yu Chen, W. G. Dilantha Fernando, Gao Xuewen, and Teresa de Kievit. "Molecular and biochemical detection of fengycin- and bacillomycin D-producing Bacillus spp., antagonistic to fungal pathogens of canola and wheat." Canadian Journal of Microbiology 53, no. 7 (2007): 901–11. http://dx.doi.org/10.1139/w07-049.

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Bacillus species are well known for their ability to control plant diseases through various mechanisms, including the production of secondary metabolites. Bacillus subtilis DFH08, an antagonist of Fusarium graminearum , and other Bacillus spp. that are antagonists of common fungal pathogens of canola were screened for peptide synthetase biosynthetic genes of fengycin and bacillomycin D. Specific polymerase chain reaction (PCR) primers identified B. subtilis strains DFH08 and 49 for the presence of the fenD gene of the fengycin operon. Bacillus cereus DFE4, Bacillus amyloliquefaciens strains DF

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24

Bender, Carol L., Francisco Alarcón-Chaidez, and Dennis C. Gross. "Pseudomonas syringae Phytotoxins: Mode of Action, Regulation, and Biosynthesis by Peptide and Polyketide Synthetases." Microbiology and Molecular Biology Reviews 63, no. 2 (1999): 266–92. http://dx.doi.org/10.1128/mmbr.63.2.266-292.1999.

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SUMMARY Coronatine, syringomycin, syringopeptin, tabtoxin, and phaseolotoxin are the most intensively studied phytotoxins of Pseudomonas syringae, and each contributes significantly to bacterial virulence in plants. Coronatine functions partly as a mimic of methyl jasmonate, a hormone synthesized by plants undergoing biological stress. Syringomycin and syringopeptin form pores in plasma membranes, a process that leads to electrolyte leakage. Tabtoxin and phaseolotoxin are strongly antimicrobial and function by inhibiting glutamine synthetase and ornithine carbamoyltransferase, respectively. Ge

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25

Wang, Ing-Kae, C. Reeves, and G. M. Gaucher. "Isolation and sequencing of a genomic DNA clone containing the 3′ terminus of the 6-methylsalicylic acid polyketide synthetase gene of Penicillium urticae." Canadian Journal of Microbiology 37, no. 1 (1991): 86–95. http://dx.doi.org/10.1139/m91-013.

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A 7.7-kilobase (kb) Penicillium urticae genomic DNA fragment containing the 3′ terminus of the 6-methylsalicylic acid polyketide synthetase gene was cloned using a 41-mer mixed oligodeoxynucleotide probe which was based on a cyanogen bromide cleavage peptide of 35 amino acids obtained from pure synthetase. Nucleotide sequence analysis of a 2.2-kb region of the cloned fragment revealed a large open reading frame of 1866 bases which was devoid of introns and which corresponded to amino acids of the carboxyl terminus of the enzyme. This was followed by a putative transcription termination–polyade

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Deigner, H. P., J. M. Mato, and M. A. Pajares. "Study of the rat liver S-adenosylmethionine synthetase active site with 8-azido ATP." Biochemical Journal 308, no. 2 (1995): 565–71. http://dx.doi.org/10.1042/bj3080565.

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The active site of rat liver S-adenosylmethionine synthetase was studied using 8-azido ATP, a photolabile analogue of ATP. Both forms of the enzyme, tetramer and dimer, could be labelled by using concentrations of the analogue similar to the KmATP values for each form, 350 microM and 1 mM respectively. Labelling of both S-adenosylmethionine synthetase forms with 8-azido [alpha-32P]ATP, followed by tryptic digestion and purification by HPLC, afforded one specifically labelled peptide in each case. Identification of the labelled peptide by amino acid analysis and peptide sequencing, and comparis

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27

Lee, Bee-Na, Scott Kroken, David Y. T. Chou, Barbara Robbertse, O. C. Yoder, and B. Gillian Turgeon. "Functional Analysis of All Nonribosomal Peptide Synthetases in Cochliobolus heterostrophus Reveals a Factor, NPS6, Involved in Virulence and Resistance to Oxidative Stress." Eukaryotic Cell 4, no. 3 (2005): 545–55. http://dx.doi.org/10.1128/ec.4.3.545-555.2005.

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ABSTRACT Nonribosomal peptides, made by nonribosomal peptide synthetases, have diverse biological activities, including roles as fungal virulence effectors. Inspection of the genome of Cochliobolus heterostrophus, a fungal pathogen of maize and a member of a genus noted for secondary metabolite production, revealed eight multimodular nonribosomal peptide synthase (NPS) genes and three monomodular NPS-like genes, one of which encodes a nonribosomal peptide synthetase/polyketide synthase hybrid enzyme presumed to be involved in synthesis of a peptide/polyketide molecule. Deletion of each NPS gen

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Tsuge, Kenji, Takanori Akiyama, and Makoto Shoda. "Cloning, Sequencing, and Characterization of the Iturin A Operon." Journal of Bacteriology 183, no. 21 (2001): 6265–73. http://dx.doi.org/10.1128/jb.183.21.6265-6273.2001.

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ABSTRACT Bacillus subtilis RB14 is a producer of the antifungal lipopeptide iturin A. Using a transposon, we identified and cloned the iturin A synthetase operon of RB14, and the sequence of this operon was also determined. The iturin A operon spans a region that is more than 38 kb long and is composed of four open reading frames, ituD, ituA, ituB, and ituC. The ituD gene encodes a putative malonyl coenzyme A transacylase, whose disruption results in a specific deficiency in iturin A production. The second gene, ituA, encodes a 449-kDa protein that has three functional modules homologous to fa

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Sun, Xun, Hao Li, Jonas Alfermann, Henning D. Mootz, and Haw Yang. "Kinetics Profiling of Gramicidin S Synthetase A, a Member of Nonribosomal Peptide Synthetases." Biochemistry 53, no. 50 (2014): 7983–89. http://dx.doi.org/10.1021/bi501156m.

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Alfermann, Jonas, Xun Sun, Florian Mayerthaler, et al. "FRET monitoring of a nonribosomal peptide synthetase." Nature Chemical Biology 13, no. 9 (2017): 1009–15. http://dx.doi.org/10.1038/nchembio.2435.

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Sosio, M., E. Bossie, A. Bianchi, and S. Donadio. "Multiple peptide synthetase gene clusters in Actinomycetes." Molecular Genetics and Genomics 264, no. 3 (2000): 213–21. http://dx.doi.org/10.1007/s004380000336.

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Clugston, Susan L., Stephan A. Sieber, Mohamed A. Marahiel, and Christopher T. Walsh. "Chirality of Peptide Bond-Forming Condensation Domains in Nonribosomal Peptide Synthetases: The C5Domain of Tyrocidine Synthetase Is aDCLCatalyst†." Biochemistry 42, no. 41 (2003): 12095–104. http://dx.doi.org/10.1021/bi035090+.

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33

O'Hanlon, Karen A., Timothy Cairns, Deirdre Stack, et al. "Targeted Disruption of Nonribosomal Peptide Synthetasepes3Augments the Virulence of Aspergillus fumigatus." Infection and Immunity 79, no. 10 (2011): 3978–92. http://dx.doi.org/10.1128/iai.00192-11.

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ABSTRACTNonribosomal peptide synthesis (NRPS) is a documented virulence factor for the opportunistic pathogenAspergillus fumigatusand other fungi. Secreted or intracellularly located NRP products include the toxic molecule gliotoxin and the iron-chelating siderophores triacetylfusarinine C and ferricrocin. No structural or immunologically relevant NRP products have been identified in the organism. We investigated the function of the largest gene inA. fumigatus, which encodes the NRP synthetase Pes3 (AFUA_5G12730), by targeted gene deletion and extensive phenotypic analysis. It was observed tha

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McArdell, J. E. C., C. J. Bruton, and T. Atkinson. "The isolation of a peptide from the catalytic domain of Bacillus stearothermophilus tryptophyl-tRNA synthetase. The interaction of Brown MX-5BR with tyrosyl-tRNA synthetase." Biochemical Journal 243, no. 3 (1987): 701–7. http://dx.doi.org/10.1042/bj2430701.

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Tryptophyl-tRNA synthetase is irreversibly inactivated by Procion Brown MX-5BR with an apparent dissociation constant (KD) of 8.8 microM and maximum rate of inactivation k3 0.192 s-1. The specificity of the interaction is supported by two previously reported observations. Firstly, Brown MX-5BR inactivation of tryptophyl-tRNA synthetase is inhibited by substrates, and secondly, the animated derivative of Brown MX-5BR is a competitive inhibitor of tryptophyl-tRNA synthetase with a Ki of 2 X 10(-4) M with respect to both tryptophan and ATP. Tryptic digestion of the dye-affinity-labelled enzyme an

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35

Bloudoff, Kristjan, and T. Martin Schmeing. "Crystallization and preliminary crystallographic analysis of the first condensation domain of viomycin synthetase." Acta Crystallographica Section F Structural Biology and Crystallization Communications 69, no. 4 (2013): 412–15. http://dx.doi.org/10.1107/s1744309113004004.

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Nonribosomal peptide synthetases (NRPSs) are large multimodular enzymes that synthesize important secondary metabolites such as antibiotics. NRPSs follow a modular synthetic logic whereby each successive amino-acid monomer is added to the peptide chain by successive multi-domain modules. The condensation domain catalyzes the central chemical event in the synthetic cycle, peptide-bond formation, and is present in every elongation module of the NRPS. Viomycin is an antituberculosis nonribosomal peptide that is synthesized by a series of four NRPS proteins and then modified by tailoring proteins.

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Cheng, Yi-Qiang, Min Yang, and Andrea M. Matter. "Characterization of a Gene Cluster Responsible for the Biosynthesis of Anticancer Agent FK228 in Chromobacterium violaceum No. 968." Applied and Environmental Microbiology 73, no. 11 (2007): 3460–69. http://dx.doi.org/10.1128/aem.01751-06.

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ABSTRACT A gene cluster responsible for the biosynthesis of anticancer agent FK228 has been identified, cloned, and partially characterized in Chromobacterium violaceum no. 968. First, a genome-scanning approach was applied to identify three distinctive C. violaceum no. 968 genomic DNA clones that code for portions of nonribosomal peptide synthetase and polyketide synthase. Next, a gene replacement system developed originally for Pseudomonas aeruginosa was adapted to inactivate the genomic DNA-associated candidate natural product biosynthetic genes in vivo with high efficiency. Inactivation of

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Gulick, Andrew M. "Nonribosomal peptide synthetase biosynthetic clusters of ESKAPE pathogens." Natural Product Reports 34, no. 8 (2017): 981–1009. http://dx.doi.org/10.1039/c7np00029d.

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Binz, Tina M., Sonia I. Maffioli, Margherita Sosio, Stefano Donadio, and Rolf Müller. "Insights into an Unusual Nonribosomal Peptide Synthetase Biosynthesis." Journal of Biological Chemistry 285, no. 43 (2010): 32710–19. http://dx.doi.org/10.1074/jbc.m110.146803.

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Vila-Farres, Xavier, John Chu, Daigo Inoyama, et al. "Antimicrobials Inspired by Nonribosomal Peptide Synthetase Gene Clusters." Journal of the American Chemical Society 139, no. 4 (2017): 1404–7. http://dx.doi.org/10.1021/jacs.6b11861.

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Bloudoff, Kristjan, and Thomas Schmeing. "NRPS condensation domain–substrate studies using X-ray crystallography." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C438. http://dx.doi.org/10.1107/s2053273314095618.

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Nonribosomal peptide synthetases (NRPSs) are a family of large multimodular enzymes that synthesize structurally and functionally diverse peptides including siderophores, toxins, agriculturally-important compounds and pharmaceutically-important compounds. The condensation (C) domain is responsible for peptide bond formation, the central chemical step in nonribosomal peptide synthesis. Here we present the crystal structure of the first condensation domain of the calcium-dependent antibiotic (CDA) synthetase (CDA-C1) from Streptomyces coelicolor soaked with a small molecule compound representing

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Imamura, Kazuhiko, Yoshihito Tsuyama, Terukage Hirata, et al. "Identification of a Gene Involved in the Synthesis of a Dipeptidyl Peptidase IV Inhibitor in Aspergillus oryzae." Applied and Environmental Microbiology 78, no. 19 (2012): 6996–7002. http://dx.doi.org/10.1128/aem.01770-12.

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ABSTRACTWYK-1 is a dipeptidyl peptidase IV inhibitor produced byAspergillus oryzaestrain AO-1. Because WYK-1 is an isoquinoline derivative consisting of threel-amino acids, we hypothesized that a nonribosomal peptide synthetase was involved in its biosynthesis. We identified 28 nonribosomal peptide synthetase genes in the sequenced genome ofA. oryzaeRIB40. These genes were also identified in AO-1. Among them, AO090001000009 (wykN) was specifically expressed under WYK-1-producing conditions in AO-1. Therefore, we constructedwykNgene disruptants of AO-1 after nonhomologous recombination was supp

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Miyanaga, Akimasa, Fumitaka Kudo, and Tadashi Eguchi. "Protein–protein interactions in polyketide synthase–nonribosomal peptide synthetase hybrid assembly lines." Natural Product Reports 35, no. 11 (2018): 1185–209. http://dx.doi.org/10.1039/c8np00022k.

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Fujii, Kiyonaga, Kaarina Sivonen, Tomoyo Nakano, and Ken-ichi Harada. "Structural elucidation of cyanobacterial peptides encoded by peptide synthetase gene in Anabaena species." Tetrahedron 58, no. 34 (2002): 6863–71. http://dx.doi.org/10.1016/s0040-4020(02)00747-0.

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Fewer, David P., Julia Österholm, Leo Rouhiainen, Jouni Jokela, Matti Wahlsten, and Kaarina Sivonen. "Nostophycin Biosynthesis Is Directed by a Hybrid Polyketide Synthase-Nonribosomal Peptide Synthetase in the Toxic Cyanobacterium Nostoc sp. Strain 152." Applied and Environmental Microbiology 77, no. 22 (2011): 8034–40. http://dx.doi.org/10.1128/aem.05993-11.

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ABSTRACTCyanobacteria are a rich source of natural products with interesting pharmaceutical properties. Here, we report the identification, sequencing, annotation, and biochemical analysis of the nostophycin (npn) biosynthetic gene cluster. Thenpngene cluster spans 45.1 kb and consists of three open reading frames encoding a polyketide synthase, a mixed polyketide nonribosomal peptide synthetase, and a nonribosomal peptide synthetase. The genetic architecture and catalytic domain organization of the proteins are colinear in arrangement, with the putative order of the biosynthetic assembly of t

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Carroll, Cassandra S., and Margo M. Moore. "Ironing out siderophore biosynthesis: a review of non-ribosomal peptide synthetase (NRPS)-independent siderophore synthetases." Critical Reviews in Biochemistry and Molecular Biology 53, no. 4 (2018): 356–81. http://dx.doi.org/10.1080/10409238.2018.1476449.

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Jenner, Matthew, Xinyun Jian, Yousef Dashti, et al. "An unusual Burkholderia gladioli double chain-initiating nonribosomal peptide synthetase assembles ‘fungal’ icosalide antibiotics." Chemical Science 10, no. 21 (2019): 5489–94. http://dx.doi.org/10.1039/c8sc04897e.

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Scholz-Schroeder, Brenda K., Jonathan D. Soule, Shi-En Lu, Ingeborg Grgurina, and Dennis C. Gross. "A Physical Map of the Syringomycin and Syringopeptin Gene Clusters Localized to an Approximately 145-kb DNA Region of Pseudomonas syringae pv. syringae Strain B301D." Molecular Plant-Microbe Interactions® 14, no. 12 (2001): 1426–35. http://dx.doi.org/10.1094/mpmi.2001.14.12.1426.

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Genetic and phenotypic mapping of an approximately 145-kb DraI fragment of Pseudomonas syringae pv. syringae strain B301D determined that the syringomycin (syr) and syringopeptin (syp) gene clusters are localized to this fragment. The syr and syp gene clusters encompass approximately 55 kb and approximately 80 kb, respectively. Both phytotoxins are synthesized by a thiotemplate mechanism of biosynthesis, requiring large multienzymatic proteins called peptide synthetases. Genes encoding peptide synthetases were identified within the syr and syp gene clusters, accounting for 90% of the DraI frag

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Gonsior, Melanie, Agnes Mühlenweg, Marcel Tietzmann, Saskia Rausch, Annette Poch, and Roderich D. Süssmuth. "Biosynthesis of the Peptide Antibiotic Feglymycin by a Linear Nonribosomal Peptide Synthetase Mechanism." ChemBioChem 16, no. 18 (2015): 2610–14. http://dx.doi.org/10.1002/cbic.201500432.

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Izoré, Thierry, and Max J. Cryle. "The many faces and important roles of protein–protein interactions during non-ribosomal peptide synthesis." Natural Product Reports 35, no. 11 (2018): 1120–39. http://dx.doi.org/10.1039/c8np00038g.

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Non-ribosomal peptide synthetase (NRPS) machineries are complex, multi-domain proteins that are responsible for the biosynthesis of many important, peptide-derived compounds. In this review, we present the current state of understanding of the protein–protein interactions that govern NRPS-mediated biosynthesis.

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Kaniusaite, Milda, Julien Tailhades, Edward A. Marschall, Robert J. A. Goode, Ralf B. Schittenhelm, and Max J. Cryle. "A proof-reading mechanism for non-proteinogenic amino acid incorporation into glycopeptide antibiotics." Chemical Science 10, no. 41 (2019): 9466–82. http://dx.doi.org/10.1039/c9sc03678d.

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