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Control of antibiotic biosynthesis. - PubMed Central …

antibiotic biosynthesis

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The biosynthesis of the nucleoside antibiotics.

Nonribosomal peptide synthetases (NRPSs) are giant multi-enzymes that carry out sequencial assembly line couplings of amino acids to generate linear or cyclic peptides. NRPSs are composed of repeating enzyme domains with modular organization to activate and couple specific amino acids in a particular order. From a synthetic biology perspective, they can be considered as peptide assembly machines composed of devices to couple fatty acids to -amino acids, -amino acids to -amino acids, and -amino acids to -amino acids. The coupling devices are composed of specific parts that contain two or more enzyme domains that can be exchanged combinatorially to generate novel peptide assembly machines to produce novel peptides. The potent lipopeptide antibiotics daptomycin and A54145E have identical cyclic depsipeptide ring structures and stereochemistry but have divergent amino acid sequences. As their biosynthetic gene clusters are derived from an ancient ancestral lipopetide pathway, these lipopeptides provided an attractive model to develop combinatorial biosynthesis to generate antibiotics superior to daptomycin. These studies on combinatorial biosynthesis have helped generate guidelines for the successful assembly of NRPS parts and devices that can be used to generate novel lipopeptide structures and have established a basis for future synthetic biology studies to further develop combinatorial biosynthesis as a robust approach to natural product drug discovery.

Antibiotic biosynthesis - UniProt

The biosynthesis of the antitumor antibiotic sibiromycin by Streptosporangium sibiricum requires the construction of four units: the amino sugar from glucose; the anthranilate ring from DL-tryptophan probably via kynurenine; the aromatic methyl group from methionine; the propylidene proline from L-tyrosine with the loss of two aromatic carbons and addition of a C-1 from methionine. Retention of tritium from DL-[5-3H]tryptophan in sibiromycin suggests an NIH shift during hydroxylation of an intermediate.

Protein involved in the synthesis of antibiotics

antibiotic biosynthesis

The Wencewicz Lab is part of the Department of Chemistry at Washington University in St. Louis. Established in July 2013, our main research focus is antibiotic drug discovery. The Wencewicz Lab is a truly interdisciplinary research environment merging the fields of organic chemistry, enzymology, molecular biology, and microbiology. We utilize our knowledge of organic chemistry and enzyme function to elucidate the molecular mechanisms of antibiotic action, biosynthesis, resistance, and delivery. A strong bias is placed on studying antibiotics isolated from nature. Much can be learned from these "Natural Products" whose molecular scaffolds evolved over billions of years to solve many of the puzzles behind effective antibiotics. We aim to reveal Nature's antibiotic secrets to open new frontiers in antibiotic discovery including promising new antibiotic targets, novel modes of action, unique enzymatic biosynthetic transormations, resistance mechanisms, and targeted drug delivery.

The tetracycline antibiotics (1–5), which are produced by fermentation of various Streptomyces species, “are a group of natural products having notable antibacterial activity toward a broad range of pathogenic microorganisms and characterized [clinically] by very low toxicity to the mammalian hosts of these pathogens.” introduced his definitive review of the biosynthesis of the tetracycline antibiotics twelve years ago with this statement (, 1967). Despite the continued interest in the chemistry of these 2-naphthacenecarboxamide-4-(dimethylamino)-1,4,4a,5,6,11,12a-octahydro-3,6,10,12,12a-pentahydroxy-6-methyl-1,11-dioxo antibiotics ( and , 1973; , 1975), the literature contains only a few reports about their biosynthesis since the pioneering studies of the group (, 1967;, 1968). As most additions to the knowledge of the tetracycline’s biosynthetic pathway were reviewed in 1973 by et al., the present account highlights only the important experimental results obtained in the period 1968–1978. This review also covers the biosynthesis of the anthracycline antibiotics, typified by daunomycin and adriamycin, because they have a close structural and biogenetic relationship to the tetracyclines.

Biosynthesis of Antibiotics - 1st Edition

Chemical Biology: Antibiotic Synthesis

Talk in the introduction about antibiotic resistant as a problem and then state the important of find a new antibiotics. Then, talk about antibiotic biosynthesis or antibiotic production.

Talk in the introduction about antibiotic resistant as a problem and then state the important of find a new antibiotics. Then, talk about antibiotic biosynthesis or antibiotic production.

Biosynthesis of Antibiotics - ScienceDirect
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antibiotic biosynthesis - ONLINE ESSAY WRITINGS

N2 - Covering: up to 2014 Dithiolopyrrolone (DTP) group antibiotics were first isolated in the early half of the 20th century, but only recently has research been reawakened by insights gained from the synthesis and biosynthesis of this structurally intriguing class of molecules. DTPs are characterized by an electronically unique bicyclic structure, which contains a compact disulfide bridge between two ene-thiols. Points of diversity within the compound class occur outside of the bicyclic core, at the two amide nitrogens. Such modifications distinguish three of the most well studied members of the class, holomycin, thiolutin, and aureothricin; the DTP core has also more recently been identified in the marine antibiotic thiomarinol, in which it is linked to a marinolic acid moiety, analog of the FDA-approved topical antibiotic Bactroban® (GlaxoSmithKline). Dithiolopyrrolones exhibit relatively broad-spectrum antibiotic activity against many Gram-positive and Gram-negative bacteria, as well as strains of Mycobacterium tuberculosis. Additionally, they have been shown to exhibit potent and selective anti-cancer activity. Despite this promising profile, there is still much unknown about the mechanisms of action for DTPs. Early reports suggested that they inhibit yeast growth at the level of transcription and that this effect is largely responsible for their distinctive microbial static properties; a similar mechanism is supported in bacteria. Elucidation of biosynthetic pathways for holomycin in Streptomyces clavuligerus and Yersinia ruckeri and thiomarinol in Alteromonas rava sp. nov. SANK 73390, have contributed evidence suggesting that multiple mechanisms may be operative in the activity of these compounds. This review will comprehensively cover the history and development of dithiolopyrrolones with particular emphasis on the biosynthesis, synthesis, biological activity and mechanism of action. This journal is

Biosynthesis of thiopeptide antibiotics and their …

AB - The biosynthesis of the antitumor antibiotic sibiromycin by Streptosporangium sibiricum requires the construction of four units: the amino sugar from glucose; the anthranilate ring from DL-tryptophan probably via kynurenine; the aromatic methyl group from methionine; the propylidene proline from L-tyrosine with the loss of two aromatic carbons and addition of a C-1 from methionine. Retention of tritium from DL-[5-3H]tryptophan in sibiromycin suggests an NIH shift during hydroxylation of an intermediate.

Production of antibiotics - Wikipedia

N2 - The biosynthesis of the antitumor antibiotic sibiromycin by Streptosporangium sibiricum requires the construction of four units: the amino sugar from glucose; the anthranilate ring from DL-tryptophan probably via kynurenine; the aromatic methyl group from methionine; the propylidene proline from L-tyrosine with the loss of two aromatic carbons and addition of a C-1 from methionine. Retention of tritium from DL-[5-3H]tryptophan in sibiromycin suggests an NIH shift during hydroxylation of an intermediate.

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