Results 251 to 260 of about 900,801 (302)
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Nonribosomal biosynthesis of peptide antibiotics
European Journal of Biochemistry, 1990Peptide antibiotics are known to contain non‐protein amino acids, D‐amino acids, hydroxy acids, and other unusual constituents. In addition they may be modified by N‐methylation and cyclization reactions. Their biosynthetic origin has been connected in many cases to an enzymatic system referred to as the ‘thiotemplate multienzymic mechanism’.
H, Kleinkauf, H, von Döhren
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Biosynthesis of Small Peptides
Annual Review of Biochemistry, 1974INTRODucTION 445 CURRENT PROBLEMS OF BIOSYNTHESIS OF SPECIFIC OLIGOPEPT1DES 446 Grarnicidin S and Tyrocidines 446 Linear Grarnicidins 450 Polymyxins 450 Bacitracins 451 Malforrain 452 Edeine 452 Aciinomyeins ’ 453 Quinoxaline Antibiotics .....
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The Biosynthesis of Regulatory Peptides
American Review of Respiratory Disease, 1987Abstract Regulatory peptides are synthesized in their cells of origin as large, usually inactive, precursors. The gene sequences encoding many peptides are now known. Although these indicate the primary structure of the precursor, it remains necessary to define the actual peptide products of cells expressing a particular gene.
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Biosynthesis of peptide–nucleobase hybrids in ribosomal peptides
Nature Chemical BiologyThe main biopolymers in nature are oligonucleotides and polypeptides. However, naturally occurring peptide-nucleobase hybrids are rare. Here we report the characterization of the founding member of a class of peptide-nucleobase hybrid natural products with a pyrimidone motif from a widely distributed ribosomally synthesized and post-translationally ...
Zeng-Fei Pei +4 more
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Biosynthesis of Hypothalamic Peptides
1977In this paper, I will attempt to summarize current knowledge about the biosynthesis of hypothalamic peptides of biological interest and will emphasize methodological aspects of peptide biosynthetic studies, a subject which I feel is of utmost importance at the present time.
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Biosynthesis of Opioid Peptides
1990The endogenous opioid peptides all contain the enkephalin sequence Tyr-Gly-Gly-Phe-Met and Tyr-Gly-Gly-Phe-Leu at their aminoterminus. Three distinct families of these peptides (endorphins, enkephalins and dynorphins) are present in different neuronal pathways within the central nervous system. Molecular genetics have shown that these three families of
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Biosynthesis of Nonribosomal Peptides
Annual Review of Microbiology, 2004▪ Abstract Bacteria and fungi use large multifunctional enzymes, the so-called nonribosomal peptide synthetases (NRPSs), to produce peptides of broad structural and biological activity. Biochemical studies have contributed substantially to the understanding of the key principles of these modular enzymes that can draw on a much larger number of ...
Robert Finking, Mohamed A. Marahiel
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In Situ Biosynthesis of Peptide Arrays
2009Polypeptide and protein arrays enable high-throughput screening capabilities for studying molecular interactions and profiling of biomarkers, and provide a powerful functional screening tool for peptidomics. To overcome the limitations of conventional arraying methods, we have exploited cell-free systems for generating arrays of polypeptides by direct ...
Mingyue, He, Oda, Stoevesandt
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Biosynthesis of Neuronal Peptides
1977The general acceptance of the idea that peptides represent a new class of intercellular messengers in the nervous system (i.e., neurotransmitters and neuromodulators) naturally raises the question whether the biosynthetic mechanisms for peptides in “peptidergic” neurons (i.e., neurons that synthesize peptides for release as intercellular messengers ...
Harold Gainer, Y. Peng Loh, Yosef Sarne
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Nonribosomal biosynthesis of backbone-modified peptides
Nature Chemistry, 2017Biosynthetic modification of nonribosomal peptide backbones represents a potentially powerful strategy to modulate the structure and properties of an important class of therapeutics. Using a high-throughput assay for catalytic activity, we show here that an L-Phe-specific module of an archetypal nonribosomal peptide synthetase can be reprogrammed to ...
David L. Niquille +5 more
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