Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Sjon Hendriks"'
Autor:
Kalyanasundaram Subramanian, Karolina Mitusińska, John Raedts, Feras Almourfi, Henk-Jan Joosten, Sjon Hendriks, Svetlana E. Sedelnikova, Servé W. M. Kengen, Wilfred R. Hagen, Artur Góra, Vitor A. P. Martins dos Santos, Patrick J. Baker, John van der Oost, Peter J. Schaap
Publikováno v:
Biomolecules, Vol 9, Iss 6, p 212 (2019)
The cupin-type phosphoglucose isomerase (PfPGI) from the hyperthermophilic archaeon Pyrococcus furiosus catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate. We investigated PfPGI using protein-engineering bioinformat
Externí odkaz:
https://doaj.org/article/3ade833aae9f4dc9bba8abd111a6ffad
Autor:
Kalyanasundaram Subramanian, Svetlana E. Sedelnikova, Servé W. M. Kengen, John van der Oost, Karolina Mitusińska, Henk-Jan Joosten, Peter J. Schaap, Vitor A. P. Martins dos Santos, Sjon Hendriks, John Raedts, Feras M. Almourfi, Patrick J. Baker, Wilfred R. Hagen, Artur Góra
Publikováno v:
Biomolecules 9 (2019) 6
Biomolecules
Biomolecules, Vol 9, Iss 6, p 212 (2019)
Volume 9
Issue 6
Biomolecules, 9(6)
Biomolecules
Biomolecules, Vol 9, Iss 6, p 212 (2019)
Volume 9
Issue 6
Biomolecules, 9(6)
The cupin-type phosphoglucose isomerase (PfPGI) from the hyperthermophilic archaeon Pyrococcus furiosus catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate. We investigated PfPGI using protein-engineering bioinformat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::589fca03af98376ffde3b8e98edd8c8f
https://research.wur.nl/en/publications/distant-non-obvious-mutations-influence-the-activity-of-a-hyperth
https://research.wur.nl/en/publications/distant-non-obvious-mutations-influence-the-activity-of-a-hyperth
Autor:
Ruud A. Weusthuis, Peter J. Schaap, G.Bwee Houweling-Tan, Marc W. T. Werten, Mark Levisson, Sjon Hendriks, Y. Griekspoor, Hetty van der Wal, Audrey Leprince, Emil J.H. Wolbert, Astrid E. Mars, Jan Springer, Truus de Vrije, John van der Oost, Gerrit Eggink, Antoine P. H. A. Moers, O. Mendes
Publikováno v:
Metabolic Engineering 42 (2017)
Metabolic Engineering, 42, 66-73
Metabolic Engineering, 42, 66-73
A Monascus ruber strain was isolated that was able to grow on mineral medium at high sugar concentrations and 175 g/l lactic acid at pH 2.8. Its genome and transcriptomes were sequenced and annotated. Genes encoding lactate dehydrogenase (LDH) were i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f2a1a28cf60d5820588ef0483c83ff8a
https://research.wur.nl/en/publications/monascus-ruber-as-cell-factory-for-lactic-acid-production-at-low-
https://research.wur.nl/en/publications/monascus-ruber-as-cell-factory-for-lactic-acid-production-at-low-
Autor:
Marc-André Elsliger, Qingping Xu, Mark Levisson, Sjon Hendriks, Frank von Delft, Gye Won Han, Pietro Roversi, Marc C. Deller, Daniel McMullan, Scott A. Lesley, Ashley M. Deacon, Servé W. M. Kengen, Ian A. Wilson, Lynn F. Ten Eyck, Mitchell D. Miller, Peter Biely, Andreas Kreusch, John van der Oost, Claus Flensburg
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 80:1545-1559
TM0077 from Thermotoga maritima is a member of the carbohydrate esterase family 7 and is active on a variety of acetylated compounds, including cephalosporin C. TM0077 esterase activity is confined to short-chain acyl esters (C2-C3), and is optimal a
Autor:
Lei Sun, Mark Levisson, Servé W. M. Kengen, Sjon Hendriks, Twan Akveld, John van der Oost, Bauke W. Dijkstra
Publikováno v:
Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 63, 777-779
Acta Crystallographica Section F. Structural Biology and Crystallization Communications 63 (2007) 9
Acta Crystallographica Section F. Structural Biology and Crystallization Communications, 63(9), 777-779
Acta Crystallographica Section F. Structural Biology and Crystallization Communications 63 (2007) 9
Acta Crystallographica Section F. Structural Biology and Crystallization Communications, 63(9), 777-779
A predicted esterase ( EstA) with an unusual new domain from the hyperthermophilic bacterium Thermotoga maritima has been cloned and overexpressed in Escherichia coli. The purified protein was crystallized by the hanging-drop vapour-diffusion techniq