Construction and in vivo assembly of a catalytically proficient and hyperthermostable de novo enzyme

Autor: Daniel W. Watkins, Jonathan M. X. Jenkins, Katie J. Grayson, Nicola Wood, Jack W. Steventon, Kristian K. Le Vay, Matthew I. Goodwin, Anna S. Mullen, Henry J. Bailey, Matthew P. Crump, Fraser MacMillan, Adrian J. Mulholland, Gus Cameron, Richard B. Sessions, Stephen Mann, J. L. Ross Anderson

Publikováno v: Nature Communications, Vol 8, Iss 1, Pp 1-9 (2017)

Catalytic mechanisms of enzymes are well understood, but achieving diverse reaction chemistries in re-engineered proteins can be difficult. Here the authors show a highly efficient and thermostable artificial enzyme that catalyzes a diverse array of

Externí odkaz: https://doaj.org/article/872155373e0341fa822353dc3be89d1d

The ascent of man(made oxidoreductases)

Autor: Katie J. Grayson, J. L. Ross Anderson

Publikováno v: Grayson, K & Anderson, R 2018, ' The ascent of man(made oxidoreductases) ', Current Opinion in Structural Biology, vol. 51, pp. 149-155 . https://doi.org/10.1016/j.sbi.2018.04.008
Current Opinion in Structural Biology

Highlights • Here we highlight our recent advances in de novo enzyme design. • Heme C-binding maquettes with minimal complexity serve as promiscuous and efficient enzymes. • Well-defined substrate binding sites are possibly not required for eff

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f0c297c3b5316ec6097a30019c753124
https://doi.org/10.1016/j.sbi.2018.04.008

Probing the quality control mechanism of the Escherichia coli twin-arginine translocase with folding variants of a de novo –designed heme protein

Autor: George A. Sutherland, Andrew Hitchcock, Nathan B. P. Adams, C. Neil Hunter, Fabio Sterpone, Pierre Tufféry, Katie J. Grayson, Dirk B. Auman, Daphne M.J. Mermans, P. Leslie Dutton, Angus J. Robertson, Alexander S. Jones, Colin Robinson, Amanda A. Brindley, Philippe Derreumaux

Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2018, 293 (18), pp.6672-6681. ⟨10.1074/jbc.RA117.000880⟩
The Journal of Biological Chemistry

Protein transport across the cytoplasmic membrane of bacterial cells is mediated by either the general secretion (Sec) system or the twin-arginine translocase (Tat). The Tat machinery exports folded and cofactor-containing proteins from the cytoplasm

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::11d47a2941212908a5e7afb119168d42
https://hal.archives-ouvertes.fr/hal-02360042

Construction and in vivo assembly of a catalytically proficient and hyperthermostable de novo enzyme

Autor: J. L. Ross Anderson, Adrian J. Mulholland, Daniel W. Watkins, Jack W. Steventon, Richard B. Sessions, Henry J. Bailey, Fraser MacMillan, Jonathan M. X. Jenkins, Matthew Goodwin, Anna Mullen, Matthew P. Crump, Kristian Le Vay, Gus Cameron, Stephen Mann, Nicola Wood, Katie J. Grayson

Publikováno v: Nature Communications
Watkins, D W, Jenkins, J M X, Grayson, K J, Wood, N, Steventon, J W, Le Vay, K, Goodwin, M I, Mullen, A S, Bailey, H J, Crump, M P, MacMillan, F, Mulholland, A J, Cameron, G, Sessions, R B, Mann, S & Anderson, J L R 2017, ' Construction and in vivo assembly of a catalytically proficient and hyperthermostable de novo enzyme ', Nature Communications, vol. 8, 358 . https://doi.org/10.1038/s41467-017-00541-4
Nature Communications, Vol 8, Iss 1, Pp 1-9 (2017)

Although catalytic mechanisms in natural enzymes are well understood, achieving the diverse palette of reaction chemistries in re-engineered native proteins has proved challenging. Wholesale modification of natural enzymes is potentially compromised

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c10b296ef11faca1cd395758080bef3
https://pubmed.ncbi.nlm.nih.gov/28842561