Results 21 to 30 of about 23,262 (184)

The insect pathogen Serratia marcescens Db10 uses a hybrid non-ribosomal peptide synthetase-polyketide synthase to produce the antibiotic althiomycin [PDF]

, 2012
There is a continuing need to discover new bioactive natural products, such as antibiotics, in genetically-amenable micro-organisms. We observed that the enteric insect pathogen, Serratia marcescens Db10, produced a diffusible compound that inhibited the
Coulthurst Sarah J., Challis Gregory L., Stanley-Wall, Nicola R; id_orcid, Gregory L Challis, Gerc, Amy J., Amy J. Gerc, Gerc Amy J., Nicola R Stanley-Wall, Gregory L. Challis (136140), Song Lijiang, Coulthurst, Sarah J; id_orcid, Sarah J. Coulthurst, Lijiang Song (136135), Lijiang Song, Stanley-Wall, Nicola R., Stanley-Wall Nicola R., Coulthurst, Sarah J., Nicola R. Stanley-wall, Challis, Gregory L., Challis, Gregory L, Amy J Gerc, Sarah J. Coulthurst (136148), Song, Lijiang, Gerc, Amy J, Amy J. Gerc, Amy J. Gerc (136131), Nicola R. Stanley-Wall (136144), Sarah J Coulthurst, Gregory L. Challis   +28 more
core   +2 more sources

Polyketide synthesis in vitro on a modular polyketide synthase

Chemistry & Biology, 1995
The 6-deoxyerythronolide B synthase (DEBS) of Saccharopolyspora erythraea, which synthesizes the aglycone core of the antibiotic erythromycin A, contains some 30 active sites distributed between three multienzyme polypeptides (designated DEBS1-3). This complexity has hitherto frustrated mechanistic analysis of such enzymes.
Wiesmann, Kirsten E.H., Cortés, Jesus, Brown, Murray J.B., Cutter, Annabel L., Staunton, James, Leadlay, Peter F.   +5 more
openaire   +2 more sources

The role of the phosphopantetheinyltransferase enzyme, PswP, in the biosynthesis of antimicrobial secondary metabolites by Serratia marcescens Db10 [PDF]

, 2014
Phosphopantetheinyl transferase (PPTase) enzymes fulfil essential roles in primary and secondary metabolism in prokaryotes, archaea and eukaryotes. PPTase enzymes catalyse the essential modification of the carrier protein domain of fatty acid synthases ...
Gerc, Amy J., Stanley-Wall, Nicola R.; id_orcid, Coulthurst, Sarah J.; id_orcid   +2 more
core   +1 more source

Structure of polyketide synthases proteins.

, 2021
The conservative domain of polyketide synthases was clarified by InterProScan, and the visualization of different domains by using DOG 2.0.
Mengxue Xu (11846894), Rujun Zhou (11846897), Wenli Jiao (11846891), Yiwei Fu (1819771), Zibo Li (1312707), Caiyun Xue (6837773)   +5 more
core   +1 more source

Evolution of polyketide synthases in bacteria [PDF]

Proceedings of the National Academy of Sciences, 2008
The emergence of resistant strains of human pathogens to current antibiotics, along with the demonstrated ability of polyketides as antimicrobial agents, provides strong motivation for understanding how polyketide antibiotics have evolved and diversified in nature.
Christian P, Ridley, Ho Young, Lee, Chaitan, Khosla   +2 more
openaire   +2 more sources

Expanding the Utility of Bioinformatic Data for the Full Stereostructural Assignments of Marinolides A and B, 24- and 26-Membered Macrolactones Produced by a Chemically Exceptional Marine-Derived Bacterium

Marine Drugs, 2023
Marinolides A and B, two new 24- and 26-membered bacterial macrolactones, were isolated from the marine-derived actinobacterium AJS-327 and their stereostructures initially assigned by bioinformatic data analysis.
Min Cheol Kim, Jaclyn M. Winter, Reiko Cullum, Alexander J. Smith, William Fenical   +4 more
doaj   +1 more source

Designing and implementing an assay for the detection of rare and divergent NRPS and PKS clones in European, Antarctic and Cuban soils [PDF]

, 2015
The ever increasing microbial resistome means there is an urgent need for new antibiotics. Metagenomics is an underexploited tool in the field of drug discovery. In this study we aimed to produce a new updated assay for the discovery of biosynthetic gene
David A Pearce, Gregory C A Amos, Gregory C. A. Amos (799040), Leo Calvo-Bado (507757), Berry, Andrew E., Chiara Borsetto (799041), Andrew E Berry, Laskaris, Paris, Calvo-Bado, Leo, Paris Laskaris, Carlos Vallin (5665333), Berry, Andrew, Calvo-Bado, Leo A., David A. Pearce (189743), Leo Calvo-Bado, Elizabeth M H Wellington, Chiara Borsetto, Elizabeth M. H. Wellington (325617), Borsetto, Chiara, Kevin K Newsham, Amos, Gregory, Carlos Vallin, Paris Laskaris (325613), Andrew E. Berry (799043), Martin Krsek, Wellington, Elizabeth M. H., Martin Krsek (799042), Pearce, David, Pearce, David A., Kevin K. Newsham (352778), Vallin, Carlos, Krsek, Martin, Wellington, Elizabeth, Newsham, Kevin, Wellington, E. M. H., Amos, Gregory C. A., Newsham, Kevin K.   +36 more
core   +1 more source

An in vitro platform for engineering and harnessing modular polyketide synthases

Nature Communications, 2020
A robust platform to study modular polyketide synthases (PKSs) in vitro is still unavailable. Here, the authors report the reconstitution of the venemycin PKS, engineer hybrid venemycin/pikromycin PKSs, and obtain much improved yields through employing ...
Takeshi Miyazawa, Melissa Hirsch, Zhicheng Zhang, Adrian T. Keatinge-Clay   +3 more
doaj   +1 more source

A single amino acid residue controls acyltransferase activity in a polyketide synthase from Toxoplasma gondii

iScience, 2022
Summary: Type I polyketide synthases (PKSs) are multidomain, multimodule enzymes capable of producing complex polyketide metabolites. These modules contain an acyltransferase (AT) domain, which selects acyl-CoA substrates to be incorporated into the ...
Hannah K. D’Ambrosio, Jack G. Ganley, Aaron M. Keeler, Emily R. Derbyshire   +3 more
doaj   +1 more source

Iterative polyketide biosynthesis by modular polyketide synthases in bacteria [PDF]

Applied Microbiology and Biotechnology, 2015
Modular polyketide synthases (type I PKSs) in bacteria are responsible for synthesizing a significant percentage of bioactive natural products. This group of synthases has a characteristic modular organization, and each module within a PKS carries out one cycle of polyketide chain elongation; thus each module is non-iterative in function.
Haotong, Chen, Liangcheng, Du
openaire   +2 more sources