Results 241 to 250 of about 319,110 (303)

Engineered biosynthesis of peptide antibiotics

Biochemical Pharmacology, 1996
In certain bacteria and filamentous fungi, a wide variety of bioactive peptides are produced non-ribosomally on large protein templates, called peptide synthetases. Recently, significant progress has been made towards understanding the modular arrangement of these complex multifunctional enzymes and the mechanisms by which they generate their ...
T, Stachelhaus, A, Schneider, M A, Marahiel   +2 more
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Nonribosomal biosynthesis of peptide antibiotics

European Journal of Biochemistry, 1990
Peptide 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, 1974
INTRODucTION 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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Engineering the biosynthesis of fungal nonribosomal peptides

Natural Product Reports, 2023
Fungal nonribosomal peptides (NRPs) and the related polyketide–nonribosomal peptide hybrid products (PK–NRPs) are a prolific source of bioactive compounds, some of which have been developed into essential drugs.
Zhang, Liwen, Wang, Chen, Chen, Kang, Zhong, Weimao, Xu, Yuquan, Molnár, István   +6 more
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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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Biosynthesis of Hypothalamic Peptides

1977
In 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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The Biosynthesis of Regulatory Peptides

American Review of Respiratory Disease, 1987
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 Opioid Peptides

1990
The 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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