Results 261 to 270 of about 200,892 (306)

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
openaire   +1 more source

Nonribosomal biosynthesis of backbone-modified peptides

Nature Chemistry, 2017
Biosynthetic 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, Douglas A. Hansen, Takahiro Mori, David Fercher, Hajo Kries, Donald Hilvert   +5 more
openaire   +3 more sources

Biosynthesis of antibiotic peptides with isoleucine stereoisomers

Archives of Biochemistry and Biophysics, 1972
Abstract Streptomyces antibioticus normally synthesizes an actinomycin mixture which contains N -methyl- l -valine and d -valine in the antibiotic peptides. Amino acid analyses indicate that trace amounts of isoleucine and, possibly, N -methylalloisoleucine are present also in actinomycin molecules. S.
T, Yajima, M A, Grigg, E, Katz
openaire   +2 more sources

Biosynthesis of Cardiac Natriuretic Peptides

2009
Cardiac-derived peptide hormones were identified more than 25 years ago. An astonishing amount of clinical studies have established cardiac natriuretic peptides and their molecular precursors as useful markers of heart disease. In contrast to the clinical applications, the biogenesis of cardiac peptides has only been elucidated during the last decade ...
openaire   +3 more sources

Combinatorial biosynthesis of polyketides and nonribosomal peptides

Current Opinion in Chemical Biology, 2001
The engineering of polyketide biosynthesis has begun to provide robust targeted libraries for screening against pharmaceutically relevant targets. New technologies that offer methodology for the rapid generation of more structurally diverse libraries have now been demonstrated.
J, Staunton, B, Wilkinson
openaire   +2 more sources

Biosynthesis of Neuronal Peptides

1977
The 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
openaire   +1 more source

The Biosynthesis of Neuropeptides: Peptide alpha-Amidation

Annual Review of Neuroscience, 1992
The prevalence, diversity, and multiplicity of functions of pep tides in the nervous system are well known. However, we are only now approaching the point at which our knowledge about the biosynthesis of neuropeptides can provide us with insights into nervous system function, just as our knowledge of the enzymes involved in the biosynthesis of ...
B A, Eipper, D A, Stoffers, R E, Mains
openaire   +2 more sources

The role of ascorbate in the biosynthesis of neuroendocrine peptides

The American Journal of Clinical Nutrition, 1991
The biosynthesis of all alpha-amidated peptides requires the participation of peptidylglycine alpha-amidating monooxygenase (PAM), a bifunctional enzyme dependent on molecular oxygen, ascorbate, and copper. In the AtT-20 corticotrope cell line, reduced concentrations of PAM and ascorbate can make alpha-amidation the rate-limiting step in the production
B A, Eipper, R E, Mains
openaire   +2 more sources

Combinatorial Biosynthesis of Non-Ribosomal Peptides

Combinatorial Chemistry & High Throughput Screening, 2003
Non-ribosomal peptide synthetases (NRPS) are modular assembly lines catalysing the synthesis of many small peptides in microbes. Genetic replacements of domains or modules in NRPS encoded by gene clusters in Bacillus sp. with corresponding domains or modules from foreign NRPS have led in several cases to the in vivo synthesis of peptides with predicted
Ullrich, Keller, Florian, Schauwecker
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Biosynthesis of Peptide Antibiotics

Annual Review of Microbiology, 1987
H, Kleinkauf, H, von Döhren
openaire   +3 more sources