Zobrazeno 1 - 10
of 56
pro vyhledávání: '"Martin K M Engqvist"'
Publikováno v:
PLoS Biology, Vol 19, Iss 10, p e3001402 (2021)
The Michaelis constant KM describes the affinity of an enzyme for a specific substrate and is a central parameter in studies of enzyme kinetics and cellular physiology. As measurements of KM are often difficult and time-consuming, experimental estima
Externí odkaz:
https://doaj.org/article/e744724226e24f99b89ce9de3626d7c7
Autor:
Elzbieta Rembeza, Martin K M Engqvist
Publikováno v:
PLoS Computational Biology, Vol 17, Iss 9, p e1009446 (2021)
Only a small fraction of genes deposited to databases have been experimentally characterised. The majority of proteins have their function assigned automatically, which can result in erroneous annotations. The reliability of current annotations in pu
Externí odkaz:
https://doaj.org/article/9d656493b80a40cea28c4f707d8fb1a1
Autor:
Anna-Karin Berglund, Clara Navarrete, Martin K M Engqvist, Emily Hoberg, Zsolt Szilagyi, Robert W Taylor, Claes M Gustafsson, Maria Falkenberg, Anders R Clausen
Publikováno v:
PLoS Genetics, Vol 13, Iss 2, p e1006628 (2017)
Previous work has demonstrated the presence of ribonucleotides in human mitochondrial DNA (mtDNA) and in the present study we use a genome-wide approach to precisely map the location of these. We find that ribonucleotides are distributed evenly betwe
Externí odkaz:
https://doaj.org/article/4a85ef4ec3074dc5bafede1810a9ce1a
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-13 (2023)
Abstract For most proteins annotated as enzymes, it is unknown which primary and/or secondary reactions they catalyze. Experimental characterizations of potential substrates are time-consuming and costly. Machine learning predictions could provide an
Externí odkaz:
https://doaj.org/article/9a14800df9344922b342fa032ed19bcb
Autor:
Veronica Saez-Jimenez, Simone Scrima, Matteo Lambrughi, Elena Papaleo, Valeria Mapelli, Martin K. M. Engqvist, Lisbeth Olsson
Publikováno v:
Saez-Jimenez, V, Scrima, S, Lambrughi, M, Papaleo, E, Mapelli, V, Engqvist, M K M & Olsson, L 2022, ' Directed Evolution of ( R )-2-Hydroxyglutarate Dehydrogenase Improves 2-Oxoadipate Reduction by 2 Orders of Magnitude ', ACS Synthetic Biology, vol. 11, no. 8, pp. 2779-2790 . https://doi.org/10.1021/acssynbio.2c00162
Pathway engineering is commonly employed to improve the production of various metabolites but may incur in bottlenecks due to the low catalytic activity of a particular reaction step. The reduction of 2-oxoadipate to (R)-2-hydroxyadipate is a key rea
Autor:
Matúš Gajdoš, Jendrik Wagner, Felipe Ospina, Antonia Köhler, Martin K. M. Engqvist, Stephan C. Hammer
Publikováno v:
Angewandte Chemie (International ed. in English).
Enantioselective synthesis of chiral alcohols through asymmetric addition of water across an unactivated alkene is a highly sought-after transformation and a big challenge in catalysis. Here we report the identification and directed evolution of a fa
Autor:
Veronica, Saez-Jimenez, Simone, Scrima, Matteo, Lambrughi, Elena, Papaleo, Valeria, Mapelli, Martin K M, Engqvist, Lisbeth, Olsson
Publikováno v:
ACS synthetic biology. 11(8)
Pathway engineering is commonly employed to improve the production of various metabolites but may incur in bottlenecks due to the low catalytic activity of a particular reaction step. The reduction of 2-oxoadipate to (
Autor:
Otto Savolainen, Elzbieta Rembeza, Laurynas Karpus, Wissam Abuajwa, Aleksej Zelezniak, Vykintas Jauniskis, Martin K. M. Engqvist, Jan Zrimec, Simona Poviloniene, Sandra Viknander, Irmantas Rokaitis, Rolandas Meškys, Audrius Laurynenas, Donatas Repecka
Publikováno v:
Nature Machine Intelligence. 3:324-333
De novo protein design for catalysis of any desired chemical reaction is a long-standing goal in protein engineering because of the broad spectrum of technological, scientific and medical applications. However, mapping protein sequence to protein fun
Publikováno v:
ACS Omega, Vol 6, Iss 3, Pp 1985-1990 (2021)
ACS Omega
ACS Omega
Microfluidic platforms offer a drastic increase in throughput while minimizing sample usage and hands-on time, which make them important tools for large-scale biological studies. A range of such systems have been developed for enzyme activity studies
For a comprehensive understanding of metabolism, it is necessary to know all potential substrates for each enzyme encoded in an organism’s genome. However, for most proteins annotated as enzymes, it is unknown which primary and/or secondary reactio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e80b24293125310aa5761e5437c4cc95
https://doi.org/10.1101/2022.05.24.493213
https://doi.org/10.1101/2022.05.24.493213