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Publikováno v:
Journal of Biological Chemistry. 292:10321-10327
Encapsulation of specific enzymes in self-assembling protein cages is a hallmark of bacterial compartments that function as counterparts to eukaryotic organelles. The cage-forming enzyme lumazine synthase (LS) from Bacillus subtilis (BsLS), for examp
Publikováno v:
Journal of Biological Chemistry. 284:21856-21862
Thermotoga maritima is a Gram-negative, hyperthermophilic bacterium whose peptidoglycan contains comparable amounts of L- and D-lysine. We have determined the fine structure of this cell-wall polymer. The muropeptides resulting from the digestion of
Publikováno v:
Journal of Biological Chemistry. 284:18070-18077
The peptide toxins of poisonous Amanita mushrooms are bicyclic octapeptides (amatoxins) or heptapeptides (phallotoxins). In Amanita bisporigera, alpha-amanitin and phallacidin are synthesized as 35- and 34-amino acid proproteins, respectively, in whi
Autor:
Sagaya Theresa Leena Philominathan, Osamu Matsushita, Soenke Seifert, Takaki Koide, Joshua Sakon, Hiroyuki Yasui, Kentaro Hamada
Publikováno v:
Journal of Biological Chemistry. 284:10868-10876
Histotoxic clostridia produce collagenases responsible for extensive tissue destruction in gas gangrene. The C-terminal collagen-binding domain (CBD) of these enzymes is the minimal segment required to bind to collagen fibril. Collagen binding effici
Autor:
Shih-Tung Liu, Friedrich Götz, Yu-Hsiu Lee, Ying-Chung Wu, Hung-Yu Shu, Cheng-Yeu Wu, Chyi-Liang Chen, Yu-Chieh Cheng
Publikováno v:
Journal of Biological Chemistry. 282:5608-5616
Fengycin, a lipopeptidic antibiotic, is synthesized nonribosomally by five fengycin synthetases (FenC, FenD, FenE, FenA, and FenB) in Bacillus subtilis F29-3. This work demonstrates that these fengycin synthetases interlock to form a chain, which coi
Autor:
Paul F. Alewood, Alun Jones, David J. Adams, Simon T. Nevin, Annette Nicke, Christina I. Schroeder, Marion L. Loughnan, Richard J. Lewis
Publikováno v:
Journal of Biological Chemistry. 281:24745-24755
The venoms of predatory marine snails (Conus spp.) contain diverse mixtures of peptide toxins with high potency and selectivity for a variety of voltage-gated and ligand-gated ion channels. Here we describe the chemical and functional characterizatio
Publikováno v:
Journal of Biological Chemistry. 280:42391-42396
Peptide deformylase is an attractive target for developing novel antibiotics. Previous studies at pH 3.0 showed peptide deformylase from Leptospira interrogans (LiPDF) exists as a dimer in which one monomer is in a closed form and the other is in an
Autor:
Dmitri I. Svergun, Peter Goettig, Walter Göhring, Peter V. Konarev, Hans Brandstetter, Robert Huber, Michael Groll, Jeong-Sun Kim
Publikováno v:
Journal of Biological Chemistry. 280:33387-33396
The tricorn-interacting factor F1 of the archaeon Thermoplasma acidophilum cleaves small hydrophobic peptide products of the proteasome and tricorn protease. F1 mutants of the active site residues that are involved in substrate recognition and cataly
Autor:
Raymond S. Norton, Catherine Y. Dy, Mark G. Hinds, Luke A. Miles, Kevin J. Barnham, Grzegorz Bulaj, Jake Nielsen, Baldomero M. Olivera
Publikováno v:
Journal of Biological Chemistry. 277:43033-43040
Conotoxin gm9a, a putative 27-residue polypeptide encoded by Conus gloriamaris, was recently identified as a homologue of the "spasmodic peptide", tx9a, isolated from the venom of the mollusk-hunting cone shell Conus textile (Lirazan, M. B., Hooper,
Publikováno v:
Journal of Biological Chemistry. 277:36351-36356
PW2 (HPLKQYWWRPSI) was selected from phage display libraries through an alternative panning method using living sporozoites of Eimeria acervulina as target. Synthetic PW2 shows anticoccidial activity against E. acervulina and Eimeria tenella with ver