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Relevant bibliographies by topics / Peptide Synthetase

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Journal articles

Academic literature on the topic 'Peptide Synthetase'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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Journal articles on the topic "Peptide Synthetase"

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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