Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Lukas Gericke"'
Autor:
Lukas Gericke, Dipali Mhaindarkar, Lukas C. Karst, Sören Jahn, Marco Kuge, Michael K. F. Mohr, Jana Gagsteiger, Nicolas V. Cornelissen, Xiaojin Wen, Silja Mordhorst, Henning J. Jessen, Andrea Rentmeister, Florian P. Seebeck, Gunhild Layer, Christoph Loenarz, Jennifer N. Andexer
Publikováno v:
ChemBioChem. 24
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3e17b3f9ec2708e6df8c4b7058a6dd50
https://doi.org/10.1002/cbic.202300133
https://doi.org/10.1002/cbic.202300133
Autor:
Lukas Gericke, Dipali Mhaindarkar, Lukas Karst, Sören Jahn, Marco Kuge, Michael K. F. Mohr, Jana Gagsteiger, Nicolas V. Cornelissen, Xiaojin Wen, Silja Mordhorst, Henning J. Jessen, Andrea Rentmeister, Florian P. Seebeck, Gunhild Layer, Christoph Loenarz, Jennifer N. Andexer
S-Adenosylmethionine (SAM) is an enzyme cofactor involved in methylation, aminopropyl transfer, and radical reactions. This versatility renders SAM-dependent enzymes of great interest in biocatalysis. The usage of SAM analogues adds to this diversity
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::08fe24e923b40be13a74349ce540daf4
https://doi.org/10.1101/2022.09.26.509380
https://doi.org/10.1101/2022.09.26.509380
Autor:
Jana Gagsteiger, Sören Jahn, Lorenz Heidinger, Lukas Gericke, Jennifer N. Andexer, Thorsten Friedrich, Christoph Loenarz, Gunhild Layer
Publikováno v:
Angew. Chem. Int. Ed.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d23c88d449434cc5714ee4d220f4f136
https://doi.org/10.1002/ange.202204198
https://doi.org/10.1002/ange.202204198
Autor:
Jana, Gagsteiger, Sören, Jahn, Lorenz, Heidinger, Lukas, Gericke, Jennifer N, Andexer, Thorsten, Friedrich, Christoph, Loenarz, Gunhild, Layer
Publikováno v:
Angewandte Chemie (International ed. in English). 61(32)
Methyl-coenzyme M reductase, which is responsible for the production of the greenhouse gas methane during biological methane formation, carries several unique posttranslational amino acid modifications, including a 2-(S)-methylglutamine. The enzyme r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::114770781eccea3aadf0e83ba0999e13
https://pubmed.ncbi.nlm.nih.gov/35638156
https://pubmed.ncbi.nlm.nih.gov/35638156