Zobrazeno 1 - 10
of 48
pro vyhledávání: '"Manuela Tosin"'
Autor:
Songya Zhang, Lin Zhang, Anja Greule, Julien Tailhades, Edward Marschall, Panward Prasongpholchai, Daniel J. Leng, Jingfan Zhang, Jing Zhu, Joe A. Kaczmarski, Ralf B. Schittenhelm, Oliver Einsle, Colin J. Jackson, Fabrizio Alberti, Andreas Bechthold, Youming Zhang, Manuela Tosin, Tong Si, Max J. Cryle
Publikováno v:
Acta Pharmaceutica Sinica B, Vol 13, Iss 8, Pp 3561-3574 (2023)
WS9326A is a peptide antibiotic containing a highly unusual N-methyl-E-2-3-dehydrotyrosine (NMet-Dht) residue that is incorporated during peptide assembly on a non-ribosomal peptide synthetase (NRPS). The cytochrome P450 encoded by sas16 (P450Sas) ha
Externí odkaz:
https://doaj.org/article/7d63ec27ecab4b6da2493ecc0f966b70
Autor:
Y. T. Candace Ho, Thierry Izoré, Joe A. Kaczmarski, Edward Marschall, Minuri S. Ratnayake, Julien Tailhades, David L. Steer, Ralf B. Schittenhelm, Manuela Tosin, Colin J. Jackson, Max J. Cryle
Publikováno v:
Frontiers in Catalysis, Vol 3 (2023)
In nonribosomal peptide synthesis, condensation (C) domains are key catalytic domains that most commonly link carrier protein bound substrates to form peptides or depsipeptides. While adenylation domains have been well characterized due to their role
Externí odkaz:
https://doaj.org/article/024e1c8ed96e462289c72f4969cb2512
Autor:
Thierry Izoré, Y. T. Candace Ho, Joe A. Kaczmarski, Athina Gavriilidou, Ka Ho Chow, David L. Steer, Robert J. A. Goode, Ralf B. Schittenhelm, Julien Tailhades, Manuela Tosin, Gregory L. Challis, Elizabeth H. Krenske, Nadine Ziemert, Colin J. Jackson, Max J. Cryle
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-14 (2021)
Non-ribosomal peptide synthetases (NRPSs) are multi-modular enzymes assembling complex natural products. Here, the structures of a Thermobifida fusca NRPS condensation domain bound to the substrate-bearing peptidyl carrier protein (PCP) domain provid
Externí odkaz:
https://doaj.org/article/fbb66a8fa3204b6a841066cc1c1e62db
Autor:
Tim Kirkman, Suk Fun Tan, Sair Maximo Chavez Pacheco, Alexander Hammer, Manuela Tosin, Anthony Coyne, Marcio Dias
Publikováno v:
ChemMedChem.
Autor:
Max J. Cryle, Thierry Izoré, Julien Tailhades, Ka Ho Chow, Colin J. Jackson, Gregory L. Challis, David Steer, Elizabeth H. Krenske, Robert J. A. Goode, Nadine Ziemert, Manuela Tosin, Ralf B. Schittenhelm, Y. T. Candace Ho, Athina Gavriilidou, Joe A. Kaczmarski
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-14 (2021)
Nature Communications
Nature Communications
Non-ribosomal peptide synthetases are important enzymes for the assembly of complex peptide natural products. Within these multi-modular assembly lines, condensation domains perform the central function of chain assembly, typically by forming a pepti
Autor:
Samantha L. Kilgour, Peter B. O’Connor, David P. A. Kilgour, Panward Prasongpholchai, Manuela Tosin
Publikováno v:
Chemistry (Weinheim an Der Bergstrasse, Germany)
A discrete acyl carrier protein (ACP) bearing a photolabile nonhydrolysable carba(dethia) malonyl pantetheine cofactor was chemoenzymatically prepared and utilised for the trapping of biosynthetic polyketide intermediates following light activation.
Publikováno v:
Chemistry (Weinheim an Der Bergstrasse, Germany)
A photolabile carba(dethia) malonyl N‐acetylcysteamine derivative was devised and prepared for the trapping of biosynthetic polyketide intermediates following light activation. From the lasalocid A polyketide assembly in a mutant strain of the soil
Autor:
Yuhui Sun, Hui Hong, Robert Jenkins, Yuliya Demydchuk, Fernanda C. R. de Paiva, Marcio Vinicius Bertacine Dias, Manuela Tosin, Markiyan Samborskyy, Rory F. Little, Finian J. Leeper, Peter F. Leadlay
Publikováno v:
Nature Catalysis. 2:1045-1054
Enzymes that catalyse remarkable Diels–Alder-like [4+2] cyclizations have been previously implicated in the biosynthesis of spirotetronate and spirotetramate antibiotics. Biosynthesis of the polyether antibiotic tetronasin is not expected to requir
Publikováno v:
Chemical communications (Cambridge, England). 57(18)
Glycopeptides such as vancomycin are antibiotics of last resort whose biosynthetic pathways still hold undefined details. Chemical probes were used to capture biosynthetic intermediates generated in the nonribosomal peptide formation of vancomycin in
Autor:
Elizabeth H. Krenske, Manuela Tosin, Y. T. Ho, Ralf B. Schittenhelm, Gregory L. Challis, Colin J. Jackson, Robert J. A. Goode, David Steer, Nadine Ziemert, Joe A. Kaczmarski, Julien Tailhades, Thierry Izoré, Ka Chow, Max J. Cryle, Athina Gavriilidou
Non-ribosomal peptide synthetases are important enzymes for the assembly of complex peptide natural products. Within these multi-modular assembly lines, condensation domains perform the central function of chain assembly, typically by forming a pepti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9012ed81f488c08a8811b029b25de880
https://doi.org/10.21203/rs.3.rs-125509/v1
https://doi.org/10.21203/rs.3.rs-125509/v1