Zobrazeno 1 - 10
of 43
pro vyhledávání: '"Tomas, Laursen"'
Publikováno v:
Frontiers in Plant Science, Vol 15 (2024)
The phenylpropanoid pathway is one of the main carbon sinks in plants, channeling phenylalanine towards thousands of products including monolignols, stilbenes, flavonoids and volatile compounds. The enzymatic steps involved in many of these pathways
Externí odkaz:
https://doaj.org/article/2c6781dcc2ec4b2d8dbad5fbbac91f8a
Autor:
Silas B. Mellor, James B. Y. H. Behrendorff, Johan Ø. Ipsen, Christoph Crocoll, Tomas Laursen, Elizabeth M. J. Gillam, Mathias Pribil
Publikováno v:
Frontiers in Plant Science, Vol 13 (2023)
Photosynthetic organelles offer attractive features for engineering small molecule bioproduction by their ability to convert solar energy into chemical energy required for metabolism. The possibility to couple biochemical production directly to photo
Externí odkaz:
https://doaj.org/article/b1ad52d18b304558bbe630ecd49f0675
Autor:
Tomas Laursen, Hiu Yue Monatrice Lam, Kasper Kildegaard Sørensen, Pengfei Tian, Cecilie Cetti Hansen, Jay T. Groves, Knud Jørgen Jensen, Sune M. Christensen
Publikováno v:
Communications Biology, Vol 4, Iss 1, Pp 1-9 (2021)
Laursen et al. investigates the role of membrane anchoring for the organization and efficiency of P450-driven plant metabolism. They report an original experimental design to monitor interactions between anchoring segments of membrane-bound enzymes a
Externí odkaz:
https://doaj.org/article/3e1e47113b9c433fa180873c4a5ccde7
Autor:
Simon Bo Jensen, Sara Thodberg, Shaheena Parween, Matias E. Moses, Cecilie C. Hansen, Johannes Thomsen, Magnus B. Sletfjerding, Camilla Knudsen, Rita Del Giudice, Philip M. Lund, Patricia R. Castaño, Yanet G. Bustamante, Maria Natalia Rojas Velazquez, Flemming Steen Jørgensen, Amit V. Pandey, Tomas Laursen, Birger Lindberg Møller, Nikos S. Hatzakis
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-14 (2021)
P450 oxidoreductase (POR) selectively activates numerous cytochromes P450 (CYP), crucial for metabolism of drugs, steroids and xenobiotics and natural product biosynthesis. Here, the authors identify ligands that bind POR and bias its specificity tow
Externí odkaz:
https://doaj.org/article/ecd3eccafadb4f149283420e2e8e2cea
Publikováno v:
Frontiers in Chemistry, Vol 10 (2022)
The ability of plants to accumulate specific metabolites in concentrations beyond their solubility in both aqueous and lipid environments remains a key question in plant biology. Natural Deep Eutectic Solvents (NADES) are mixtures of natural compound
Externí odkaz:
https://doaj.org/article/4d14dde58f824607b9e320802206989d
Autor:
Rita Del Giudice, Nicolò Paracini, Tomas Laursen, Clement Blanchet, Felix Roosen-Runge, Marité Cárdenas
Publikováno v:
Molecules, Vol 27, Iss 21, p 7628 (2022)
Bicelles are disk-shaped models of cellular membranes used to study lipid–protein interactions, as well as for structural and functional studies on transmembrane proteins. One challenge for the incorporation of transmembrane proteins in bicelles is
Externí odkaz:
https://doaj.org/article/a054888cd4144c0b9aa766621771307b
Autor:
Krutika Bavishi, Darui Li, Stine Eiersholt, Emma N. Hooley, Troels C. Petersen, Birger Lindberg Møller, Nikos S. Hatzakis, Tomas Laursen
Publikováno v:
Scientific Reports, Vol 8, Iss 1, Pp 1-9 (2018)
Abstract Cytochrome P450 oxidoreductase (POR) is the primary electron donor in eukaryotic cytochrome P450 (CYP) containing systems. A wealth of ensemble biophysical studies of Cytochrome P450 oxidoreductase (POR) has reported a binary model of the co
Externí odkaz:
https://doaj.org/article/8fa4bf61be47432a9c951c289cdc90d1
Autor:
Rita Del Giudice, Natalia Putkaradze, Bruna Marques dos Santos, Cecilie Cetti Hansen, Christoph Crocoll, Mohammed Saddik Motawia, Folmer Fredslund, Tomas Laursen, Ditte Hededam Welner
Publikováno v:
Del Giudice, R, Putkaradze, N, dos Santos, B M, Hansen, C C, Crocoll, C, Motawia, M S, Fredslund, F, Laursen, T & Welner, D H 2022, ' Structure-guided engineering of key amino acids in UGT85B1 controlling substrate and stereo-specificity in aromatic cyanogenic glucoside biosynthesis ', Plant Journal, vol. 111, no. 6, pp. 1539-1549 . https://doi.org/10.1111/tpj.15904
Cyanogenic glucosides are important defense molecules in plants with useful biological activities in animals. Their last biosynthetic step consists of a glycosylation reaction that confers stability and increases structural diversity and is catalyzed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::897dc0dfe10ca6ba66cd58e48bedc4b9
https://doi.org/10.1111/tpj.15904
https://doi.org/10.1111/tpj.15904
Autor:
Kasper K. Sørensen, Knud J. Jensen, Tomas Laursen, Pengfei Tian, Sune M. Christensen, Cecilie Cetti Hansen, Jay T. Groves, Hiu Yue Monatrice Lam
Publikováno v:
Communications Biology, Vol 4, Iss 1, Pp 1-9 (2021)
Laursen, T, Lam, H Y M, Sorensen, K K, Tian, P, Hansen, C C, Groves, J T, Jensen, K J & Christensen, S M 2021, ' Membrane anchoring facilitates colocalization of enzymes in plant cytochrome P450 redox systems ', Communications Biology, vol. 4, 1057 . https://doi.org/10.1038/s42003-021-02604-1
Laursen, T, Lam, H Y M, Sorensen, K K, Tian, P, Hansen, C C, Groves, J T, Jensen, K J & Christensen, S M 2021, ' Membrane anchoring facilitates colocalization of enzymes in plant cytochrome P450 redox systems ', Communications Biology, vol. 4, 1057 . https://doi.org/10.1038/s42003-021-02604-1
Plant metabolism depends on cascade reactions mediated by dynamic enzyme assemblies known as metabolons. In this context, the cytochrome P450 (P450) superfamily catalyze key reactions underpinning the unique diversity of bioactive compounds. In contr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b91c52c21778d70a0229ebcf53dec938
https://doi.org/10.1038/s42003-021-02604-1
https://doi.org/10.1038/s42003-021-02604-1
Autor:
Sara Thodberg, Rita Del Giudice, Matias E. Moses, Tomas Laursen, Nikos S. Hatzakis, Amit V. Pandey, Yanet G. Bustamante, Flemming Jørgensen, Maria Natalia Rojas Velazquez, Cecilie Cetti Hansen, Shaheena Parween, Birger Lindberg Møller, Simon Bo Jensen, Camilla Knudsen, Magnus Berg Sletfjerding, Philip M. Lund, Johannes Thomsen, Patricia Rodríguez Castaño
Publikováno v:
Jensen, Simon Bo; Thodberg, Sara; Parween, Shaheena; Moses, Matias E.; Hansen, Cecilie C.; Thomsen, Johannes; Sletfjerding, Magnus B.; Knudsen, Camilla; Del Giudice, Rita; Lund, Philip M.; Castaño, Patricia R.; Bustamante, Yanet G.; Rojas Velazquez, Maria Natalia; Jørgensen, Flemming Steen; Pandey, Amit Vikram; Laursen, Tomas; Møller, Birger Lindberg; Hatzakis, Nikos S. (2021). Biased cytochrome P450-mediated metabolism via small-molecule ligands binding P450 oxidoreductase. Nature Communications, 12(1), p. 2260. Springer Nature 10.1038/s41467-021-22562-w
Nature Communications, Vol 12, Iss 1, Pp 1-14 (2021)
Nature Communications
Jensen, S B, Thodberg, S, Parween, S, Moses, M E, Hansen, C C, Thomsen, J, Sletfjerding, M B, Knudsen, C, Del Giudice, R, Lund, P M, Castaño, P R, Bustamante, Y G, Velazquez, M N R, Jørgensen, F S, Pandey, A V, Laursen, T, Møller, B L & Hatzakis, N S 2021, ' Biased cytochrome P450-mediated metabolism via small-molecule ligands binding P450 oxidoreductase ', Nature Communications, vol. 12, no. 1, 2260 . https://doi.org/10.1038/s41467-021-22562-w
Nature Communications, Vol 12, Iss 1, Pp 1-14 (2021)
Nature Communications
Jensen, S B, Thodberg, S, Parween, S, Moses, M E, Hansen, C C, Thomsen, J, Sletfjerding, M B, Knudsen, C, Del Giudice, R, Lund, P M, Castaño, P R, Bustamante, Y G, Velazquez, M N R, Jørgensen, F S, Pandey, A V, Laursen, T, Møller, B L & Hatzakis, N S 2021, ' Biased cytochrome P450-mediated metabolism via small-molecule ligands binding P450 oxidoreductase ', Nature Communications, vol. 12, no. 1, 2260 . https://doi.org/10.1038/s41467-021-22562-w
Metabolic control is mediated by the dynamic assemblies and function of multiple redox enzymes. A key element in these assemblies, the P450 oxidoreductase (POR), donates electrons and selectively activates numerous (>50 in humans and >300 in plants)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::01559cb2dc61b0b1595ccbe1e3266cd4
https://boris.unibe.ch/155910/1/2021_NatureCommunications_s41467-021-22562-w.pdf
https://boris.unibe.ch/155910/1/2021_NatureCommunications_s41467-021-22562-w.pdf
