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Engineering polyketide synthases and nonribosomal peptide synthetases [PDF]
Current Opinion in Structural Biology, 2013 Naturally occurring polyketides and nonribosomal peptides with broad and potent biological activities continue to inspire the discovery of new and improved analogs. The biosynthetic apparatus responsible for the construction of these natural products has been the target of intensive protein engineering efforts. Traditionally, engineering has focused on
Gavin Williams
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Frontiers in Molecular Biosciences, 2020 In nature, various enzymes govern diverse biochemical reactions through their specific three-dimensional structures, which have been harnessed to produce many useful bioactive compounds including clinical agents and commodity chemicals.
Soonkyu Hwang +7 more
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Frontiers in Microbiology, 2019 Identification of novel bioactive compounds represents an important field in modern biomedical research. Microorganisms of the underexplored environments, such as deserts, hot springs, oceans, and caves are highly promising candidates for screening such ...
Dominykas Bukelskis +6 more
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The parallel and convergent universes of polyketide synthases and nonribosomal peptide synthetases
Chemistry and Biology, 1999 Polyketide synthases (PKSs) and nonribosomal peptide synthetases (NRPSs) catalyze chain elongation from simple building blocks to create a diverse array of natural products. PKS and NRPS proteins share striking architectural and organizational similarities that can be exploited to generate entirely new natural products.
Christopher Walsh, David Cane
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Toxins, 2013 Polyketide synthase (PKSs) and nonribosomal peptide synthetase (NRPSs) are large multimodular enzymes involved in biosynthesis of polyketide and peptide toxins produced by fungi.
Massimo Ferrara +2 more
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UMYU Journal of Microbiology Research, 2021 There has been an increasing emphasis on the need to exploit un- and underexplored environments especially the marine environments for microbial and chemical diversity.
Afegbua, S. L. +4 more
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In vitro reconstitution reveals major differences between human and bacterial cytochrome c synthases
eLife, 2021 Cytochromes c are ubiquitous heme proteins in mitochondria and bacteria, all possessing a CXXCH (CysXxxXxxCysHis) motif with covalently attached heme. We describe the first in vitro reconstitution of cytochrome c biogenesis using purified mitochondrial ...
Molly C Sutherland +8 more
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Inhibition of Inositol Phosphorylceramide Synthase by the Cyclic Peptide Aureobasidin A [PDF]
Antimicrobial Agents and Chemotherapy, 2009 ABSTRACT By using a detergent-washed membrane preparation, the interaction of the fungal natural product inhibitor aureobasidin A (AbA) with inositol phosphorylceramide synthase (IPC synthase) was studied by kinetic analysis of wild-type and mutant enzyme-catalyzed reactions. AbA inhibited the wild-type enzyme from both
Paul A, Aeed +3 more
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Scientific Reports, 2023 We report here a new application, CustomProteinSearch (CusProSe), whose purpose is to help users to search for proteins of interest based on their domain composition. The application is customizable. It consists of two independent tools, IterHMMBuild and
Leonor Oliveira +6 more
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NRPSsp: non-ribosomal peptide synthase substrate predictor [PDF]
Bioinformatics, 2011 Abstract Summary: Non-ribosomal peptide synthetases (NRPSs) are multi-modular enzymes, which biosynthesize many important peptide compounds produced by bacteria and fungi. Some studies have revealed that an individual domain within the NRPSs shows significant substrate selectivity.
Carlos Prieto +3 more
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