Results 91 to 100 of about 1,070,439 (189)
Structural Biology of Nonribosomal Peptide Synthetases [PDF]
The nonribosomal peptide synthetases are modular enzymes that catalyze synthesis of important peptide products from a variety of standard and non-proteinogenic amino acid substrates. Within a single module are multiple catalytic domains that are responsible for incorporation of a single residue. After the amino acid is activated and covalently attached
Bradley R, Miller, Andrew M, Gulick
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Caffeic acid is a central metabolite in the fungal bioluminescence pathway. We identified and characterized caffeylpyruvate hydrolase from Neonothopanus gardneri (ngarCPH) and demonstrate its ability to hydrolyze fungal oxyluciferin into caffeic and pyruvic acids, confirming a complete and self‐sustained fungal bioluminescence cycle.
Caio K. Zamuner +8 more
wiley +1 more source
Despite their cosmopolitan distribution, knowledge on cyanobacteria in the family Coelosphaeriaceae is limited. In this study, a single species culture of a coelosphaeran cyanobacterium isolated from a brackish rock pool in the Baltic Sea was established.
Kerstin Häggqvist +4 more
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The tryptophan prenyltransferase ComQ from Bacillus subtilis 168 can prenylate daptomycin at Trp1
ComQ168 from Bacillus subtilis 168 catalyzes C‐terminal tryptophan farnesylation of ComX to generate a competence‐inducing pheromone. Recombinant ComQ168 also modifies cyclic peptides, including Daptomycin, likely at the N‐terminal tryptophan. Structural modeling highlights a C‐terminal binding region, supporting substrate promiscuity and establishing ...
Yanli Xu +2 more
wiley +1 more source
Flexing and Stretching in Nonribosomal Peptide Synthetases
Re-engineering of nonribosomal peptide synthetase molecular assembly lines has been hampered by a lack of detailed knowledge concerning inter-domain substrate transfer. Recent structural studies of catalytically relevant domain-domain interactions provide valuable insights into this problem (Liu et al., 2011; Sundlov et al., 2012 [in this issue of ...
Pfennig, Sabrina, Stubbs, Milton T.
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ABSTRACT After an initial evolution in a reducing environment, life got successively challenged by reactive oxygen species (ROS), especially during the great oxidation event (GOE) that followed the development of photosynthesis. Therefore, ROS are deeply intertwined into the physiological, morphological and transcriptional responses of most present‐day
Stephanie Frohn +12 more
wiley +1 more source
Antifungal peptides in marine invertebrates
A majority of terrestrial and marine organisms use to fend off a wide range of microorganisms, including bacteria and fungi by employing “antimicrobial peptides (AMPs)” that are ribosomally synthesized from proteinogenic amino acids.
N Fusetani
doaj
Actinomycin Derivatives: Structural Diversification and Biological Activities
Actinomycins are chromopeptide antibiotics exhibiting remarkable structural diversity and broad bioactivity. This review traces their development from naturally occurring D‐, X‐, A‐, G‐, Y‐, and Z‐type analogs to precursor‐directed, synthetic, and semisynthetic derivatives.
Özge Can, Erdal Bedir
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Improved Incorporation of Arylglycines Into Ramoplanin Sequences via Solid‐Phase Peptide Synthesis
The incorporation of arylglycines using solid‐phase peptide synthesis remains challenging due to the sensitivity of these residues for epimerization. Here, exploring multiple conditions for the incorporation of arylglycine residues into peptides using SPPS demonstrates how small changes to current synthesis protocols can lead to significant ...
Edward Marschall +3 more
wiley +1 more source
[Biologically active nonribosomal peptides. II. Nonribosomal peptides of various biological action].
The second part of the review concerned with investigation of nonribosomal peptides.
T. I. Orlova +2 more
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