Publications

 

Publications

  1. O’Neill, EC; Pergolizzi, G; Stevenson, CEM, Lawson, DM; Nepogodiev, SA and Field, RA. ” Cellodextrin phosphorylase from Ruminiclostridium thermocellum: X-ray crystal structure and substrate specificity analysis.” Carbohydr. Res., 2017, S0008-6215(17)30359-2. DOI:10.1016/j.carres.2017.07.005.
  2. Field, R; Pergolizzi, G; Kuhaudomlarp, S and Kalita, E. “Glycan phosphorylases in multi-enzyme synthetic processes.” Protein Pept. Lett., 2017. DOI:10.2174/0929866524666170811125109.
  3. Both, P; Riese,M; Gray, C. J; Huang, K; Pallister. E. G; Kosov, I; Conway, L. P; Voglmeir, J and Flitsch, S. L. “Development and application of a highly α2,6-selective pseudosialidase.” ChemRxiv, 31.08.2017.
  4. Gray C. J; Thomas B, Upton R, Migas L. G, Eyers C. E, Barran P. E and Flitsch S. L. “Applications of ion mobility mass spectrometry for high throughput, high resolution glycan analysis.” Biochimica et Biophysica Acta (BBA) – GENERAL SUBJECTS. DOI: 10.1016/J.BBAGEN.2016.02.003
  5. P. Both, H. Busch, P. Kelly, F. G. Mutti, N. J. Turner, S. L. Flitsch, Sabine J. “Whole-Cell Biocatalysts for Stereoselective C-H Amination Reactions”. Angewandte Chemie-Internatioal Edition., 55; 1511 – 1513. DOI: 10.1002/anie.201510028
  6. van Munster, J.M., Thomas, B., Riese, M., Davis, A.L., Gray, C.J., Archer, D.B, & Flitsch, S.L. “Application of carbohydrate arrays coupled with mass spectrometry to detect activity of plant-polysaccharide degradative enzymes from the fungus Aspergillus niger.” Sci. Rep. DOI:10.1038/srep43117
  7. Schindler, B., Barnes, L., Renois, G., Gray, C., Chambert, S. Fort, S., Flitsch, S.L., Loison, C.,  Allouche, A-R. and Compagnon, I. “Anomeric memory of the glycosidic bond upon fragmentation and its consequences for carbohydrate sequencing.” Nat. Commun. DOI: 10.1038/s41467-017-01179-y
  8. Kuhaudomlarp, S., Patron N.J., Henrissat, B., Rejzek, M., Saalbach, G., and Field, R.A. “Identification of Euglena gracilis β-1,3-glucan phosphorylase and establishment of a new glycoside hydrolase (GH) family GH149.” JBC DOI: 10.1074/jbc.RA117.000936
  9. Craven, F.L., Silva, J., Segarra-Maset, M.D., Huang, K., Both, P., Gough, J.E., Flitsch, S.L., Webb, S.J. “One-pot’sequential enzymatic modification of synthetic glycolipids in vesicle membranes” Chem. Comm. DOI: 10.1039/C7CC09148F
  10. Huang, K., Parmeggiani, F., Pallister, E., Huang, C-J., Liu, F-F., Li, Q., Birmingham, W.R., Both, P., Thomas, B., Liu, L., Voglmeir, J., and Flitsch, S.L. “Characterisation of a Bacterial Galactokinase with High Activity and Broad Substrate Tolerance for Chemoenzymatic Synthesis of 6-Aminogalactose-1-Phosphate and Analogues.” ChemBioChem DOI: 10.1002/cbic.201700477
  11. Song, H. B.; He, M.; Cai, Z. P. Huang, K.; Flitsch, S. L.; Liu, L.; Voglmeir, J. “UDP-Glucose 4-Epimerase and b-1-4-Galactosyltransferase from the Oyster Magallana gigas as Valuable Biocatalysts for the production of galactosylated products.” International J. Mol. Sci. DOI: 10.3390/ijms19061600
  12. Both, P., Riese, M., Gray, C.J., Huang, K., Pallister, E.G., Kosov, I., Conway, L.P., Voglmeir, J., Flisch, S.L. “Applications of a highly α2, 6-selective pseudosialidase.” Glycobiology DOI: 10.1093/glycob/cwy016
  13. Kuhaudomlarp S., Walpole S., Stevenson C. E. M., Nepogodiev S. A., Lawson D. M., Angulo J., Field R. A. “Unravelling the Specificity of Laminaribiose Phosphorylase from Paenibacillus sp. YM-1 towards Donor Substrates Glucose/Mannose 1-Phosphate by Using X-ray Crystallography and Saturation Transfer Difference NMR Spectroscopy.” ChemBioChem DOI: 10.1002/cbic.201800260
  14. Gray, C.; Flitsch S. L. Methods for the High Resolution Analysis of Glycoconjugates. In ‘Coupling and Decoupling of Diverse Molecular Units in Glycosciences’, pp225-267. Springer International Publishing, Z.J. Witczak and R. Bielski Eds. DOI: 10.1007/978-3-319-65587-1
  15. Briliute, J.; Urbanowicz, P. A.; Luis, A. S.; Basle, A.; Paterson, N.; Rebello, O.; Hendel, J.; Ndeh, D. A.; Lowe, E. C.; Martens, E. C.; Spencer, D. I. R.; Bolam, D. N.; Crouch L. I. Complex N-glycan breakdown by gut Bacteroides involves an extensive enzymatic apparatus encoded by multiple co-regulated genetic loci. Nat Microbiol. DOI: 10.1038/s41564-019-0466-x
  16. Kuhaudomlarp, S.; Pergolizzi, G.; Patron, N. J.; Henrissat, B.; Field, R. A. Unraveling the subtleties of β-(1→3)-glucan phosphorylase specificity in the GH94, GH149 and GH161 glycoside hydrolase families,  J. Biol. Chem. DOI: 10.1074/jbc.RA119.007712
  17. de Andrade, P.; Munoz, J.; Pergolizzi, G.; Gabrielli, V.; Nepogodiev, S.; Luga, D.; Fabian, L.; Nigmatullin, R.; Johns, M. A.; Harniman, R.; Eichhorn, S. J.; Angulo, J.; Khimyak, Yaroslav, Field, R. Bottom-up Chemoenzymatic Synthesis Towards Novel Fluorinated Cellulose-like Materials, ChemRxiv, 2020. Link to paper
  18. Singh, R. P.; Pergolizzi, G.; Nepogodiev, S. A.; de Andrade, P.; Kuhaudomlarp, S.; Field, R. A. Preparative and Kinetic Analysis of β-1,4- and β-1,3-Glucan Phosphorylases Informs Access to Human Milk Oligosaccharide Fragments and Analogues Thereof. ChemBioChem, 2020, 7, 1043-1049. DOI: 10.1002/cbic.201900440
  19. Wu, H.; Rebello, O.; Crost, E. H.; Owen, C. D.; Walpole, S.; Bennati-Granier, C.; Ndeh, D.; Monaco, S.; Hicks, T.; Colvile, A.; Urbanowicz, P. A.; Walsh, M. A.; Angulo, A.; Spencer, D. I. R.; Juge, N. Fucosidases from the human gut symbiont Ruminococcus gnavus.  Cell. Mol. Life Sci. 2020. DOI: 10.1007/s00018-020-03514-x