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pro vyhledávání: '"amino acid activation"'
Akademický článek
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Akademický článek
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Autor:
Colin T. Bedford
Publikováno v:
Journal of Chemical Research. 45:334-342
The mechanisms of several types of thiol-independent peptide ligation reported over the past 14 years have been reviewed.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::af9f93324532152c43c96439337f7a47
https://doi.org/10.1177/1747519820983759
https://doi.org/10.1177/1747519820983759
Autor:
Norbert E. Juettner, Hans-Lothar Fuchsbauer, Jan P. Bogen, Tobias A Bauer, Felicitas Pfeifer, Andreas Kraemer, Reinhard Meusinger, Stefan H Huettenhain, Stefan Knapp
Publikováno v:
Journal of Natural Products. 83:2983-2995
Streptomyces mobaraensis produces the papain inhibitor SPI consisting of a 12 kDa protein and small active compounds (SPIac). Purification of the papain inhibitory compounds resulted in four diverse chymostatin derivatives that were characterized by
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::daf665314dc23b71bf1241bb389e0f5d
https://doi.org/10.1021/acs.jnatprod.0c00201
https://doi.org/10.1021/acs.jnatprod.0c00201
Autor:
Michael Ibba, Tammy J. Bullwinkle, Jesse Rinehart, Kyle Mohler, Kym F. Faull, Kaeli F. Loeb, Nien-Ching Han
Publikováno v:
Journal of Biological Chemistry. 295:1402-1410
β-N-methylamino-l-alanine (BMAA) is a nonproteinogenic amino acid that has been associated with neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and Alzheimer's disease (AD). BMAA has been found in human protein extracts; ho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d27c22215bad6cb693b86e740c88c338
https://doi.org/10.1016/s0021-9258(17)49898-x
https://doi.org/10.1016/s0021-9258(17)49898-x
Autor:
Karin Musier-Forsyth, Ronald C. Wek, Sheree A. Wek, Marina Bakhtina, William A. Cantara, Nathan T. Kudlapur, Danni Jin
Publikováno v:
The Journal of Biological Chemistry
Aminoacyl-tRNA synthetases (ARSs) catalyze the charging of specific amino acids onto cognate tRNAs, an essential process for protein synthesis. Mutations in ARSs are frequently associated with a variety of human diseases. The human EPRS1 gene encodes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ce97fb563092e3b298c457fe5bda992
http://europepmc.org/articles/PMC8511952
http://europepmc.org/articles/PMC8511952
Publikováno v:
Organic Process Research & Development. 23:2099-2105
Evolution of hydrogen cyanide (HCN) during amino acid activation using the reagent combination ethyl cyano(hydroxyimino)acetate (Oxyma)/diisopropylcarbodiimide (DIC) is observed under ambient condi...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::06e3ad1c5ff87c350b18b06dc50bee8f
https://doi.org/10.1021/acs.oprd.9b00344
https://doi.org/10.1021/acs.oprd.9b00344
Publikováno v:
ACS Chemical Biology. 14:288-295
Aminoacyl-tRNA synthetases (AARSs) charge their cognate tRNAs with corresponding amino acids, playing key roles in ribosomal protein synthesis. A series of proteomic studies have demonstrated that AARSs have levels of lysine acetylation much higher t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7147da10ed191fe71e1c1abfb66d9611
https://doi.org/10.1021/acschembio.8b01013
https://doi.org/10.1021/acschembio.8b01013
Autor:
Robert J. A. Goode, Julien Tailhades, Edward A. Marschall, Ralf B. Schittenhelm, Milda Kaniusaite, Max J. Cryle
Publikováno v:
Chemical Science. 10:9466-9482
Non-ribosomal peptide biosynthesis produces highly diverse natural products through a complex cascade of enzymatic reactions that together function with high selectivity to produce bioactive peptides. The modification of non-ribosomal peptide synthet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ba0a9e02709633de42de6c7714f98573
https://doi.org/10.1039/c9sc03678d
https://doi.org/10.1039/c9sc03678d
Autor:
Anja Kirchberg, Roderich D. Süssmuth, Vincent Wiebach, Evi Stegmann, Madeleine Peschke, Max J. Cryle, Melanie Schoppet
Publikováno v:
Chemical Science
The condensation domain synthesising the last peptide bond in glycopeptide antibiotic biosynthesis has a preference for linear peptide substrates, with effective peptide formation linked to the rate of amino acid activation by the preceding adenylati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63c22ab908e5498e8934dff85d34d24e
https://doi.org/10.1039/c8sc03530j
https://doi.org/10.1039/c8sc03530j