Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Nicolas M. Kosa"'
Autor:
Lorillee Tallorin, JiaLei Wang, Woojoo E. Kim, Swagat Sahu, Nicolas M. Kosa, Pu Yang, Matthew Thompson, Michael K. Gilson, Peter I. Frazier, Michael D. Burkart, Nathan C. Gianneschi
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-10 (2018)
The discovery of peptide substrates for enzymes with selective activities is a central goal in chemical biology. Here, the authors develop a hybrid method combining machine learning and experimental testing for fast optimization of peptides for speci
Externí odkaz:
https://doaj.org/article/d9ae7a50ccf5436cb95b497dfe663903
Autor:
Mary W Trucksess, Christina A. Mireles DeWitt, Krebs Joseph F, Nicolas M. Kosa, Swapna Gone, James M. Hungerford
Publikováno v:
Journal of AOAC INTERNATIONAL. 101:783-792
Bioo Scientific Corp. has developed a rapid enzymatic quantitative assay for the determination of histamine in seafood. Fresh/frozen tuna, canned tuna, pouched tuna, and frozen mahi mahi samples were used for the validation study under the specific g
Autor:
Nicolas M. Kosa, Matthew P. Thompson, Lorillee Tallorin, Michael D. Burkart, Michael K. Gilson, Jialei Wang, Pu Yang, Swagat Sahu, Woojoo E. Kim, Peter I. Frazier, Nathan C. Gianneschi
Publikováno v:
Nature Communications
Nature communications, vol 9, iss 1
Nature Communications, Vol 9, Iss 1, Pp 1-10 (2018)
Nature communications, vol 9, iss 1
Nature Communications, Vol 9, Iss 1, Pp 1-10 (2018)
The discovery of peptide substrates for enzymes with exclusive, selective activities is a central goal in chemical biology. In this paper, we develop a hybrid computational and biochemical method to rapidly optimize peptides for specific, orthogonal
Autor:
Shiteng Duan, Christopher R. Vickery, Joseph P. Noel, Nicolas M. Kosa, Ellen P. Casavant, Michael D. Burkart
Publikováno v:
ACS Chemical Biology
4'-Phosphopantetheinyl transferases (PPTase) post-translationally modify carrier proteins with a phosphopantetheine moiety, an essential reaction in all three domains of life. In the bacterial genus Mycobacteria, the Sfp-type PPTase activates pathway
Publikováno v:
Chem. Sci.. 5:1179-1186
Evaluation of new acyl carrier protein hydrolase (AcpH, EC 3.1.4.14) homologs from proteobacteria and cyanobacteria reveals significant variation in substrate selectivity and kinetic parameters for phosphopantetheine hydrolysis from carrier proteins.
Publikováno v:
Nature Methods. 9:981-984
Provided herein, inter alia, are methods and compositions for removing a phosphopantethiene analogue moiety from an ACP-phosphopantetheine conjugate thereby providing Apo-ACP proteins.
Autor:
Nathan C. Gianneschi, Ti-Hsuan Ku, Kevin M. Pham, Michael D. Burkart, Swagat Sahu, Nicolas M. Kosa
Publikováno v:
Journal of the American Chemical Society. 136(50)
We present a spherical micelle generated in a three-step sequence in which a farnesyl-pantetheine conjugate is phosphorylated, adenylated, and phosphorylated once more to generate a farnesyl-CoA amphiphile that self-assembles into spherical micelles.
Autor:
Adam Yasgar, Michael D. Burkart, Thomas Daniel, Timothy L. Foley, Matias S. Attene-Ramos, William Leister, Ganesha Rai, Anton Simeonov, Nicolas M. Kosa, Ajit Jadhav, Heather L. Baker, David J. Maloney
Publikováno v:
Journal of Medicinal Chemistry
4'-Phosphopantetheinyl transferases (PPTases) catalyze a post-translational modification essential to bacterial cell viability and virulence. We present the discovery and medicinal chemistry optimization of 2-pyridinyl-N-(4-aryl)piperazine-1-carbothi
The post-translational modifying enzymes phophopantetheinyl transferase and acyl carrier protein hydrolase have shown utility in the functional modification of acyl carrier proteins. Here we develop these tools as immobilized biocatalysts on agarose
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ffdf42bdcb93976d4374cd1636bc42ad
https://europepmc.org/articles/PMC4012645/
https://europepmc.org/articles/PMC4012645/
Publikováno v:
The Journal of antibiotics. 67(1)
Phosphopantetheinyl transferase (E.C. 2.7.8.-) activates biosynthetic pathways that synthesize both primary and secondary metabolites in bacteria. Inhibitors of these enzymes have the potential to serve as antibiotic compounds that function through a