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Gideon Davies

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Gideon Davies
FRS FRSC FMedSci
Gideon Davies in 2010
Born
Gideon John Davies

(1964-07-06) 6 July 1964 (age 60)[6]
Great Sutton, Cheshire
NationalityBritish
Alma materUniversity of Bristol (BSc, PhD, DSc)
ChildrenTwo daughters[6]
Awards
Scientific career
Fields
Institutions
ThesisPhosphoglycerate kinase from Bacillus stearothermophilus (1990)
Doctoral advisor
  • Herman Watson
  • Len Hall[4]
Doctoral studentsTracey Gloster[5]
Websitewww.york.ac.uk/chemistry/staff/academic/d-g/gdavies/ Edit this at Wikidata

Gideon John Davies (born 6 July 1964) is a professor of chemistry in the Structural Biology Laboratory (YSBL) at the University of York, UK.[2][7][8] Davies is best known for his ground-breaking studies into carbohydrate-active enzymes, notably analysing the conformational and mechanistic basis for catalysis and applying this for societal benefit. In 2016 Davies was appointed the Royal Society Ken Murray Research Professor at the University of York. Gideon Davies has recently been elected to the Council of the Royal Society.

Education

[edit]

Davies was educated at the University of Bristol where he was awarded a Bachelor of Science degree in Biochemistry and a PhD in 1990 for research on the enzyme phosphoglycerate kinase isolated from the bacterium Bacillus stearothermophilus, and supervised by Herman Watson and Len Hall.[4][9] He was awarded a Doctor of Science (DSc) degree from the University of Bristol in 2007.[1]

Career

[edit]

Following his PhD, Davies did postdoctoral research at the European Molecular Biology Laboratory (EMBL) outstation in Hamburg working with Keith S. Wilson on the use of synchrotron radiation in protein crystallography and also at the French National Centre for Scientific Research (CNRS) in Grenoble.[10] in 1990, Davies moved to York to work with Dale Wigley and Guy Dodson on DNA gyrase, starting his own group within YSBL in 1996 upon receiving a Royal Society University Research Fellowship.[11] He was appointed Professor at the University of York in 2001[10] and awarded a Royal Society Ken Murray Research Professorship[12] in 2016. He has collaborated with Alywn Jones, Bernard Henrissat,[13][14] Steve Withers and David Vocadlo.[3] Among those who undertook doctoral research with him are Tracey Gloster.[5]

Research

[edit]

Davies research investigates the biological chemistry of carbohydrates, from their structure[15][16][17] to their roles in enzymology,[18][19] glycobiology,[20][21][22][23] use as biofuels[24][25][26] and implications for gut microbiota.[27][28] His research has been funded by the Biotechnology and Biological Sciences Research Council (BBSRC),[29] European Research Council (ERC) and Alzheimer's Research UK.[10]

Davies has over 400 publications in peer-reviewed journals.[2][7][8]

Awards and honours

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Davies has won a number of awards for his work. These include The Davy Medal and Gabor Medal of the Royal Society, the John and Rita Cornforth Award (with Paul Walton[30]), the Haworth Memorial, Khorana, Peptide and Protein, Corday-Morgan and Carbohydrate Chemistry medals of the Royal Society of Chemistry, the iChemE Global Energy Award of the Institution of Chemical Engineers (with Paul Walton and Bernard Henrissat), The Whistler Prize of the International Carbohydrate Organization,[31] and the GlaxoSmithKline Award[32] of the Biochemical Society. In 2019 he was one of the members of the York Structural Biology Laboratory at the University of York that received the Queen's Anniversary Prize.

Davies was elected a member of the European Molecular Biology Organization (EMBO) in 2010[10] and is a Fellow of the Royal Society of Chemistry (FRSC)

In 2010, Davies was elected a Fellow of the Royal Society (FRS). His nomination reads:

Professor Gideon Davies' research is focused on "structural enzymology". In this he addresses the enzymes, and their accessory domains, that are involved in the synthesis, modification and breakdown of carbohydrates. His chemical and structural insight into protein-carbohydrate interactions and his brilliant exploitation of advanced crystallographic methods provide the basis for understanding how the chemical and structural factors in the stereochemical pathway of the enzyme:substrate complex govern specificity and catalysis. His research is having an immense impact on carbohydrate chemistry and biology and biological catalysis generally.[33]

Davies was elected a Fellow of the Academy of Medical Sciences (FMedSci) in 2014, his nomination reads

Gideon Davies, who is Professor of Biological Chemistry at University of York, has made world-leading contributions to Biochemistry. He has made fundamental additions to our understanding of enzyme mechanism and carbohydrate biochemistry. As a direct result of his work into the conformation of sugars during turnover, he described the rational design of highly potent inhibitors of O-linked glucosamine modifying enzymes. These compounds are showing potential as treatments for Alzheimer's disease. Recently he has turned to study the human microbiota, which are now recognised to be an essential component of human health, and their carbohydrate metabolism is implicated in several disease states.[34]

He was awarded the John and Rita Cornforth Award of Royal Society of Chemistry in 2020[35] and the Queen's Anniversary Prize (to YSBL) in 2019[36] He was a Haworth Memorial Lectureship of Royal Society of Chemistry in 2018[37] and a Global Energy Award of Institution of Chemical Engineers winner in 2016.[38]

Personal life

[edit]

Davies married Valérie Marie-Andrée Ducros[39] in 1999 (div. 2021) and has two daughters.[6]

References

[edit]
  1. ^ a b Davies, Gideon John (2007). Published work submitted for the degree of D.Sc (DSc thesis). University of Bristol.
  2. ^ a b c Gideon Davies publications indexed by Google Scholar Edit this at Wikidata
  3. ^ a b Vocadlo, D. J.; Davies, G. J.; Laine, R; Withers, S. G. (2001). "Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate" (PDF). Nature. 412 (6849): 835–8. Bibcode:2001Natur.412..835V. doi:10.1038/35090602. PMID 11518970. S2CID 205020153.
  4. ^ a b Professor Gideon Davies, FMedSci, FRS Biography, University of York [dead link]
  5. ^ a b Gloster, Tracey Maureen (2005). Transition state mimicry in glycoside hydrolysis (PhD thesis). The University of York. OCLC 1063339504. EThOS uk.bl.ethos.533533.
  6. ^ a b c Anon (2014). "Davies, Prof. Gideon John". Who's Who (online Oxford University Press ed.). A & C Black. doi:10.1093/ww/9780199540884.013.U251693. (Subscription or UK public library membership required.)
  7. ^ a b Gideon Davies publications indexed by the Scopus bibliographic database. (subscription required)
  8. ^ a b Gideon Davies publications from Europe PubMed Central
  9. ^ Davies, Gideon John (1990). Phosphoglycerate kinase from Bacillus stearothermophilus (PhD thesis). University of Bristol.
  10. ^ a b c d www.york.ac.uk/chemistry/staff/academic/d-g/gdavies/ Edit this at Wikidata
  11. ^ "Gideon Davies". royalsociety.org. Archived from the original on 28 June 2018. Retrieved 14 June 2017.
  12. ^ "Leading scientists awarded Royal Society Research Professorships". royalsociety.org. Retrieved 14 June 2017.
  13. ^ Henrissat, B.; Davies, G. (1997). "Structural and sequence-based classification of glycoside hydrolases". Current Opinion in Structural Biology. 7 (5): 637–44. doi:10.1016/S0959-440X(97)80072-3. PMID 9345621.
  14. ^ Davies, G.; Henrissat, B. (1995). "Structures and mechanisms of glycosyl hydrolases". Structure. 3 (9): 853–9. doi:10.1016/S0969-2126(01)00220-9. PMID 8535779.
  15. ^ Agirre, Jon; Davies, Gideon; Wilson, Keith; Cowtan, Kevin (2015). "Carbohydrate anomalies in the PDB" (PDF). Nature Chemical Biology. 11 (5): 303. doi:10.1038/nchembio.1798. PMID 25885951.
  16. ^ Agirre, Jon; Iglesias-Fernández, Javier; Rovira, Carme; Davies, Gideon J; Wilson, Keith S; Cowtan, Kevin D (2015). "Privateer: software for the conformational validation of carbohydrate structures" (PDF). Nature Structural & Molecular Biology. 22 (11): 833–834. doi:10.1038/nsmb.3115. PMID 26581513. S2CID 33800088.
  17. ^ Agirre, Jon; Davies, Gideon J; Wilson, Keith S; Cowtan, Kevin D (June 2017). "Carbohydrate structure: the rocky road to automation" (PDF). Current Opinion in Structural Biology. Carbohydrates: A feast of structural glycobiology • Sequences and topology: Computational studies of protein-protein interactions. 44: 39–47. doi:10.1016/j.sbi.2016.11.011. PMID 27940408.
  18. ^ Vocadlo, D. J.; Davies, G. J.; Laine, R.; Withers, S. G. (23 August 2001). "Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate" (PDF). Nature. 412 (6849): 835–838. Bibcode:2001Natur.412..835V. doi:10.1038/35090602. ISSN 0028-0836. PMID 11518970. S2CID 205020153.
  19. ^ Ducros, Valérie M.-A.; Zechel, David L.; Murshudov, Garib N.; Gilbert, Harry J.; Szabó, Lóránd; Stoll, Dominik; Withers, Stephen G.; Davies, Gideon J. (2 August 2002). "Substrate distortion by a beta-mannanase: snapshots of the Michaelis and covalent-intermediate complexes suggest a B(2,5) conformation for the transition state". Angewandte Chemie International Edition in English. 41 (15): 2824–2827. doi:10.1002/1521-3773(20020802)41:15<2824::AID-ANIE2824>3.0.CO;2-G. ISSN 1433-7851. PMID 12203498.
  20. ^ Coutinho, Pedro M.; Deleury, Emeline; Davies, Gideon J.; Henrissat, Bernard (25 April 2003). "An evolving hierarchical family classification for glycosyltransferases". Journal of Molecular Biology. 328 (2): 307–317. doi:10.1016/s0022-2836(03)00307-3. ISSN 0022-2836. PMID 12691742.
  21. ^ Yuzwa, Scott A; Macauley, Matthew S; Heinonen, Julia E; Shan, Xiaoyang; Dennis, Rebecca J; He, Yuan; Whitworth, Garrett E; Stubbs, Keith A; McEachern, Ernest J (2008). "A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo". Nature Chemical Biology. 4 (8): 483–490. doi:10.1038/nchembio.96. PMID 18587388.
  22. ^ Wu, Liang; Viola, Cristina M; Brzozowski, Andrzej M; Davies, Gideon J (2015). "Structural characterization of human heparanase reveals insights into substrate recognition". Nature Structural & Molecular Biology. 22 (12): 1016–1022. doi:10.1038/nsmb.3136. PMC 5008439. PMID 26575439.
  23. ^ Roth, Christian; Chan, Sherry; Offen, Wendy A; Hemsworth, Glyn R; Willems, Lianne I; King, Dustin T; Varghese, Vimal; Britton, Robert; Vocadlo, David J (2017). "Structural and functional insight into human O-GlcNAcase". Nature Chemical Biology. 13 (6): 610–612. doi:10.1038/nchembio.2358. PMC 5438047. PMID 28346405.
  24. ^ Yin, DeLu (Tyler); Urresti, Saioa; Lafond, Mickael; Johnston, Esther M.; Derikvand, Fatemeh; Ciano, Luisa; Berrin, Jean-Guy; Henrissat, Bernard; Walton, Paul H. (18 December 2015). "Structure-function characterization reveals new catalytic diversity in the galactose oxidase and glyoxal oxidase family". Nature Communications. 6: 10197. Bibcode:2015NatCo...610197Y. doi:10.1038/ncomms10197. PMC 4703870. PMID 26680532.
  25. ^ Quinlan, R. Jason; Sweeney, Matt D.; Leggio, Leila Lo; Otten, Harm; Poulsen, Jens-Christian N.; Johansen, Katja Salomon; Krogh, Kristian B. R. M.; Jørgensen, Christian Isak; Tovborg, Morten (13 September 2011). "Insights into the oxidative degradation of cellulose by a copper metalloenzyme that exploits biomass components". Proceedings of the National Academy of Sciences. 108 (37): 15079–15084. Bibcode:2011PNAS..10815079Q. doi:10.1073/pnas.1105776108. ISSN 0027-8424. PMC 3174640. PMID 21876164.
  26. ^ Frandsen, Kristian E H; Simmons, Thomas J; Dupree, Paul; Poulsen, Jens-Christian N; Hemsworth, Glyn R; Ciano, Luisa; Johnston, Esther M; Tovborg, Morten; Johansen, Katja S (2016). "The molecular basis of polysaccharide cleavage by lytic polysaccharide monooxygenases". Nature Chemical Biology. 12 (4): 298–303. doi:10.1038/nchembio.2029. PMC 4817220. PMID 26928935.
  27. ^ Larsbrink, Johan; Rogers, Theresa E.; Hemsworth, Glyn R.; McKee, Lauren S.; Tauzin, Alexandra S.; Spadiut, Oliver; Klinter, Stefan; Pudlo, Nicholas A.; Urs, Karthik (2014). "A discrete genetic locus confers xyloglucan metabolism in select human gut Bacteroidetes". Nature. 506 (7489): 498–502. Bibcode:2014Natur.506..498L. doi:10.1038/nature12907. PMC 4282169. PMID 24463512.
  28. ^ Cuskin, Fiona; Lowe, Elisabeth C.; Temple, Max J.; Zhu, Yanping; Cameron, Elizabeth A.; Pudlo, Nicholas A.; Porter, Nathan T.; Urs, Karthik; Thompson, Andrew J. (2015). "Human gut Bacteroidetes can utilize yeast mannan through a selfish mechanism". Nature. 517 (7533): 165–169. Bibcode:2015Natur.517..165C. doi:10.1038/nature13995. PMC 4978465. PMID 25567280.
  29. ^ UK Government research grants awarded to Gideon Davies Archived 26 October 2014 at the Wayback Machine, via Research Councils UK
  30. ^ "Professor Paul Walton - About staff, University of York".
  31. ^ "Home". ico.chemistry.unimelb.edu.au.
  32. ^ "The GlaxoSmithKline Award".
  33. ^ "Professor Gideon John Davies FRS". London: The Royal Society. Archived from the original on 23 November 2015.
  34. ^ "Professor Gideon Davies FRS FMedSci". London: The Academy of Medical Sciences. Archived from the original on 26 October 2014.
  35. ^ "Archive".
  36. ^ "Putting proteins at the forefront of industrial biotechnology and new drug approaches".
  37. ^ "Carbohydrate Group".
  38. ^ "Global Awards - Past winners - IChemE".
  39. ^ Ducros, V. R.; Brzozowski, A. M.; Wilson, K. S.; Brown, S. H.; Østergaard, P.; Schneider, P.; Yaver, D. S.; Pedersen, A. H.; Davies, G. J. (1998). "Crystal structure of the type-2 Cu depleted laccase from Coprinus dnereus at 2.2 Å resolution". Nature Structural Biology. 5 (4): 310–316. doi:10.1038/nsb0498-310. PMID 9546223. S2CID 8642348.
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