{"id":101,"date":"2012-08-31T10:57:32","date_gmt":"2012-08-31T09:57:32","guid":{"rendered":"http:\/\/www.micklefieldlab.chemistry.manchester.ac.uk\/?page_id=101"},"modified":"2018-05-22T13:58:33","modified_gmt":"2018-05-22T12:58:33","slug":"dr-mark-thompson","status":"publish","type":"page","link":"https:\/\/www.micklefieldlab.chemistry.manchester.ac.uk\/?page_id=101","title":{"rendered":"Dr. Mark Thompson"},"content":{"rendered":"<p style=\"text-align: justify;\"><strong><a href=\"http:\/\/www.micklefieldlab.chemistry.manchester.ac.uk\/wp-content\/uploads\/2012\/08\/Mark-Thompson_website-picture-1.jpg\"><img loading=\"lazy\" decoding=\"async\" class=\"size-thumbnail wp-image-173 alignleft\" title=\"Mark Thompson_website picture (1)\" src=\"http:\/\/www.micklefieldlab.chemistry.manchester.ac.uk\/wp-content\/uploads\/2012\/08\/Mark-Thompson_website-picture-1-150x150.jpg\" alt=\"\" width=\"150\" height=\"150\" \/><\/a><\/strong><\/p>\n<p><strong>Mark Thompson<\/strong> obtained his BSc. in Biochemistry from the University of York in 2006 which included a year working in industry within the Pharmacokinetics Dynamics and Metabolism department at Pfizer. After graduation he remained at the University of York completing a PhD in Chemistry in 2009, investigating biocatalytic routes for the production of commercially desirable monoterpene alcohols. Following this, from 2010-2011 he worked on a Post-doctoral position at the University of Greifswald (Germany). During this time in the Department of Biotechnology &amp; Enzyme Catalysis, his research focussed on enzymes including Baeyer Villiger monooxygenases, esterases, and phenol oxidases. Work involved the targeted discovery of new biocatalysts and enhancement of catalytic properties via protein engineering, together with assay development and applied microbiology. After joining the Micklefield group in 2011 his current research interests are centred on the engineering of a number of different enzymes for improved commercial application.<\/p>\n<p><span style=\"text-decoration: underline;\">Publications:<\/span><\/p>\n<ul>\n<li><strong>Structure and Biocatalytic Scope of Coclaurine N-Methyltransferase.<\/strong> M. R. Bennett, <strong>M. L. Thompson<\/strong>, S. A. Shepherd, M. S. Dunstan, A. J. Herbert, D. R. M. Smith, V. A. Cronin, B. R. K. Menon, C. Levy &amp; J. Micklefield Angew. Chem. Int. Ed. <strong>2018<\/strong> in press. (<a href=\"http:\/\/dx.doi.org\/10.1002\/anie.201805060\">http:\/\/dx.doi.org\/10.1002\/anie.201805060<\/a>)<\/li>\n<li><strong>Effects of Active Site Modification and Quaternary Structure on the Regioselectivity of Catechol-<\/strong><strong><em>O<\/em><\/strong><strong>-Methyltransferase. <\/strong>B. J. C. Law, M. R. Bennett, <strong>M. L. Thompson<\/strong>, C. Levy, S. A. Shepherd, D. Leys, and J. Micklefield\u00a0<em>Angew. Chem. Int. Ed.\u00a0<\/em><strong>2016, <\/strong><em>55,<\/em><strong><em>\u00a0<\/em><\/strong>2683-2687. (<a href=\"http:\/\/dx.doi.org\/10.1002\/anie.201508287\">http:\/\/dx.doi.org\/10.1002\/anie.201508287<\/a>)<\/li>\n<li><strong>Extending the Biocatalytic Scope of Regiocomplementary Flavin-Dependent Halogenase Enzymes. <\/strong>S.A. Shepherd, C. Karthikeyan, J. Latham, A.-W. Struck, <strong>M. L. Thompson<\/strong>, B. Menon, C. Levy, D. Leys and J. Micklefield\u00a0<em>Chemical Science<\/em>\u00a0<strong>2015\u00a0<\/strong><em>6, <\/em>3454-3460<strong>\u00a0<\/strong>(<a href=\"http:\/\/pubs.rsc.org\/en\/Content\/ArticleLanding\/2015\/SC\/C5SC00913H#!divAbstract\">http:\/\/dx.doi.org\/10.1039\/C5SC00913H<\/a>)<\/li>\n<li><strong>Enzymatic Enantioselective Decarboxylative Protonation of Heteroaryl Malonates.\u00a0<\/strong>R. Lewin, M. Goodall, <strong>M.L. Thompson<\/strong>,\u00a0J. Leigh, M. Breuer, K. Baldenius and J. Micklefield\u00a0<em>Chem. Eur. J.,<\/em>\u00a0<strong>2015,<\/strong>\u00a0<em>17<\/em>, 6557-6563. DOI:\u00a0<a href=\"http:\/\/www.chemeurope.com\/en\/publications\/781296\/enzymatic-enantioselective-decarboxylative-protonation-of-heteroaryl-malonates.html\">10.1002\/chem.201406014<\/a><\/li>\n<li><strong>Enzymatic Carboxylation and Decarboxylation.\u00a0<\/strong>R. Lewin,\u00a0<strong>M. Thompson<\/strong> and J Micklefield\u00a0<em>Science of Synthesis: Biocatalysis in Organic Synthesis,<\/em>\u00a0<strong>2014<\/strong>, 2, 133-157.<\/li>\n<li><strong>S-Adenosyl-Methionine-Dependent Methyltransferases: Highly Versatile Enzymes in Biocatalysis, Biosynthesis and Other Biotechnological Applications.\u00a0<\/strong>A.-W. Struck, <strong>M.L. Thompson<\/strong>, L.S. Wong, and J. Micklefield\u00a0<em>ChemBioChem<\/em>\u00a0<strong>2012<\/strong><em>, 13,<\/em>\u00a02642-2655 (<a href=\"http:\/\/onlinelibrary.wiley.com\/doi\/10.1002\/cbic.201200556\/abstract\">http:\/\/dx.doi.org\/10.1002\/cbic.201200556<\/a>)<\/li>\n<li><strong>Use of \u201csmall but smart\u201d libraries to enhance the enantioselectivity of an esterase from Bacillus stearothermophilus towards tetrahydrofuran-3-yl acetate.\u00a0<\/strong>A. Nobili, M.G. Gall, I.V. Pavlidis, <strong>M.L. Thompson<\/strong>, M. Schmidt, U.T. Bornscheuer <em>FEBS Journal,<\/em>\u00a0<strong>2013,<\/strong> 280, 3084-3093.<\/li>\n<li><strong>Investigating the effects of metals on phenol oxidase-producing nitrogen-fixing Azotobacter chroococcum.<\/strong>\u00a0S. Herter, M. Schmidt, <strong>M.L. Thompson<\/strong>, A. Mikolasch, F. Schauer. <em>Journal of Basic Microbiology,<\/em><strong> 2012<\/strong>, 52, 1-9<\/li>\n<li><strong>A high-throughput assay method to quantify Baeyer-Villiger monooxygenase activity.\u00a0<\/strong>S. Sass, M. Kadow, K. Geitner, <strong>M.L. Thompson<\/strong>, L. Talmann, D. Bottcher, M. Schmidt, U.T. Bornscheuer. <em>Tetrahedron,\u00a0<\/em><strong>2012,<\/strong> 68, 7570-7580.<\/li>\n<li><strong>Study of enzymatic properties of phenol oxidase from nitrogen-fixing Azotobacter chroococcum.\u00a0<\/strong>S. Herter, M. Schmidt, <strong>M.L. Thompson<\/strong>, A. Mikolasch, F. Schauer. <em>Applied Microbiology and Biotechnology Express,<\/em>\u00a0<strong>2011<\/strong>, 1, 14.<\/li>\n<li><strong>Identification of novel esterases for the synthesis of sterically demanding chiral alcohols by sequence-structure guided genome mining.\u00a0<\/strong>G.S. Nguyen, <strong>M.L. Thompson<\/strong>, G. Grogan, U.T. Bornscheuer, R. Kourist. <em>Journal of Molecular Catalysis B: Enzymatic,<\/em>\u00a0<strong>2011<\/strong><em>, 70<\/em>, 88-94.<\/li>\n<li><strong>A new phenol oxidase produced during melanogenesis and encystment stage in the nitrogen-fixing soil bacterium Azotobacter chroococcum.\u00a0<\/strong>S. Herter, M. Schmidt, <strong>M.L. Thompson<\/strong>, A. Mikolasch, F. Schauer. <em>Applied Microbiology and Biotechnology,<\/em>\u00a0<strong>2011<\/strong><em>, 90<\/em>, 1037-1049.<\/li>\n<li><strong>Comparative analysis of tertiary alcohol esterase activity in bacterial strains isolated from enrichment cultures and from screening strain libraries.\u00a0<\/strong>S. Herter, G.S. Nguyen, <strong>M.L. Thompson<\/strong>, F. Steffen-Munsberg, F. Schauer, U.T. Bornscheuer, R. Kourist. <em>Applied Microbiology and Biotechnology,<\/em>\u00a0<strong>2011<\/strong><em>, 90<\/em>, 929-939.<\/li>\n<li><strong>Biotransformation of \u03b2-myrcene to geraniol by a strain of Rhodococcus erythropolis isolated by selective enrichment from hop plants. M.L. Thompson<\/strong>, R. Marriott, A. Dowle, G. Grogan. <em>Applied Microbiology and Biotechnology,<\/em>\u00a0<strong>2010<\/strong><em>, 85<\/em>, 721-730.<\/li>\n<\/ul>\n","protected":false},"excerpt":{"rendered":"<p>Mark Thompson obtained his BSc. in Biochemistry from the University of York in 2006 which included a year working in industry within the Pharmacokinetics Dynamics and Metabolism department at Pfizer. After graduation he remained at the University of York completing &hellip; <a href=\"https:\/\/www.micklefieldlab.chemistry.manchester.ac.uk\/?page_id=101\">Continue reading <span class=\"meta-nav\">&rarr;<\/span><\/a><\/p>\n","protected":false},"author":1,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"open","template":"","meta":{"footnotes":""},"class_list":["post-101","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/www.micklefieldlab.chemistry.manchester.ac.uk\/index.php?rest_route=\/wp\/v2\/pages\/101","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/www.micklefieldlab.chemistry.manchester.ac.uk\/index.php?rest_route=\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/www.micklefieldlab.chemistry.manchester.ac.uk\/index.php?rest_route=\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/www.micklefieldlab.chemistry.manchester.ac.uk\/index.php?rest_route=\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"https:\/\/www.micklefieldlab.chemistry.manchester.ac.uk\/index.php?rest_route=%2Fwp%2Fv2%2Fcomments&post=101"}],"version-history":[{"count":17,"href":"https:\/\/www.micklefieldlab.chemistry.manchester.ac.uk\/index.php?rest_route=\/wp\/v2\/pages\/101\/revisions"}],"predecessor-version":[{"id":1020,"href":"https:\/\/www.micklefieldlab.chemistry.manchester.ac.uk\/index.php?rest_route=\/wp\/v2\/pages\/101\/revisions\/1020"}],"wp:attachment":[{"href":"https:\/\/www.micklefieldlab.chemistry.manchester.ac.uk\/index.php?rest_route=%2Fwp%2Fv2%2Fmedia&parent=101"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}