Zobrazeno 1 - 10 of 156 pro vyhledávání: '"Michael J. Danson"'
1
Akademický článek
Engineering enhanced thermostability into the Geobacillus pallidus nitrile hydratase
Autor: Jennifer C. Van Wyk, B. Trevor Sewell, Michael J. Danson, Tsepo L. Tsekoa, Muhammed F. Sayed, Don A. Cowan
Publikováno v: Current Research in Structural Biology, Vol 4, Iss , Pp 256-270 (2022)
Nitrile hydratases (NHases) are important biocatalysts for the enzymatic conversion of nitriles to industrially-important amides such as acrylamide and nicotinamide. Although thermostability in this enzyme class is generally low, there is not suffici
Externí odkaz: https://doaj.org/article/c90cb24114fc4f7986852852b84aaf3f
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2
Akademický článek
Inhibition of extracellular proteases improves the production of a xylanase in Parageobacillus thermoglucosidasius
Autor: Alexandria T. N. Holland, Michael J. Danson, Albert Bolhuis
Publikováno v: BMC Biotechnology, Vol 19, Iss 1, Pp 1-8 (2019)
Abstract Background Parageobacillus thermoglucosidasius is a thermophilic and ethanol-producing bacterium capable of utilising both hexose and pentose sugars for fermentation. The organism has been proposed to be a suitable organism for the productio
Externí odkaz: https://doaj.org/article/10681b5fcbdb4053ba161c5cc727e5a8
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3
Akademický článek
Development of an efficient technique for gene deletion and allelic exchange in Geobacillus spp.
Autor: Leann F. Bacon, Charlotte Hamley-Bennett, Michael J. Danson, David J. Leak
Publikováno v: Microbial Cell Factories, Vol 16, Iss 1, Pp 1-8 (2017)
Abstract Background Geobacillus thermoglucosidasius is a thermophilic, natural ethanol producer and a potential candidate for commercial bioethanol production. Previously, G. thermoglucosidasius has been genetically modified to create an industrially
Externí odkaz: https://doaj.org/article/ca9377896ca54916bbe6130433052cd9
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6
Structurally Informed Mutagenesis of a Stereochemically Promiscuous Aldolase Produces Mutants That Catalyze the Diastereoselective Syntheses of All Four Stereoisomers of 3-Deoxy-hexulosonic Acid
Autor: Sylvain F. Royer, Xuan Gao, Robin R. Groleau, Marc W. van der Kamp, Steven D. Bull, Michael J. Danson, Susan J. Crennell
Publikováno v: Royer, S F, Gao, X, Groleau, R R, Van der Kamp, M W, Bull, S D, Danson, M J & Crennell, S J 2022, ' Structurally Informed Mutagenesis of a Stereochemically Promiscuous Aldolase Produces Mutants That Catalyze the Diastereoselective Syntheses of All Four Stereoisomers of 3-Deoxy-hexulosonic Acid ', ACS Catalysis, vol. 12, no. 18, pp. 11444–11455 . https://doi.org/10.1021/acscatal.2c03285
A 2-keto-3-deoxygluconate aldolase from the hyperthermophile Sulfolobus solfataricus catalyzes the nonstereoselective aldol reaction of pyruvate and d-glyceraldehyde to produce 2-keto-3-deoxygluconate (d-KDGlc) and 2-keto-3-deoxy-d-galactonate (d-KDG
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78b6d4c96ba3044184ff63ead2e5d7e5
https://hdl.handle.net/1983/d48d0d06-2953-4693-b20e-046ce97900d9
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8
Chemical Mapping Exposes the Importance of Active Site Interactions in Governing the Temperature Dependence of Enzyme Turnover
Autor: Vickery L. Arcus, Samuel Winter, Christopher R. Pudney, Erica J. Prentice, Dora M. Răsădean, Hannah B. L. Jones, Michael J. Danson, G. Dan Pantoş, Rory M. Crean, Gergely Katona, Marc W. van der Kamp
Publikováno v: Winter, S, Jones, H B L, Răsădean, D M, Crean, R M, Van der Kamp, M W & Pudney, C R 2021, ' Chemical Mapping Exposes the Importance of Active Site Interactions in Governing the Temperature Dependence of Enzyme Turnover ', ACS Catalysis, vol. 11, no. 24, pp. 14854-14863 . https://doi.org/10.1021/acscatal.1c04679
ACS Catalysis
Uncovering the role of global protein dynamics in enzyme turnover is needed to fully understand enzyme catalysis. Recently, we have demonstrated that the heat capacity of catalysis, ΔCP‡, can reveal links between the protein free energy landscape,
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::190ba99b0f95305e563e8bbbec3a3647
https://research-information.bris.ac.uk/en/publications/5ae0ae7e-e25c-499a-8349-e605a8e52e02
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10
Uncovering the Relationship between the Change in Heat Capacity for Enzyme Catalysis and Vibrational Frequency through Isotope Effect Studies
Autor: Steven D. Bull, Anna B. Troya, Vickery L. Arcus, Rory M. Crean, Michael J. Danson, Marc W. van der Kamp, Christopher R. Pudney, Hannah B. L. Jones, Christopher Matthews
Publikováno v: Jones, H B L, Crean, R M, Matthews, C, Troya, A B, Danson, M J, Bull, S D, Arcus, V L, Van Der Kamp, M W & Pudney, C R 2018, ' Uncovering the relationship between the change in heat capacity for enzyme catalysis and vibrational frequency through isotope effect studies ', ACS Catalysis, vol. 8, no. 6, pp. 5340-5349 . https://doi.org/10.1021/acscatal.8b01025
Jones, H B L, Crean, R M, Matthews, C, Troya, A B, Danson, M J, Bull, S D, Arcus, V L, Van Der Kamp, M W & Pudney, C R 2018, ' Uncovering the Relationship between the Change in Heat Capacity for Enzyme Catalysis and Vibrational Frequency through Isotope Effect Studies ', ACS Catalysis, vol. 8, pp. 5340-5349 . https://doi.org/10.1021/acscatal.8b01025
Understanding how enzyme catalysis varies with temperature is key to understanding catalysis itself and, ultimately, how to tune temperature optima. Temperature dependence studies inform on the change in heat capacity during the reaction, ΔCP‡, an
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9fca5f442cdc5c2b3aa82d0f69127a72
https://doi.org/10.1021/acscatal.8b01025
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