{"id":16,"date":"2012-11-20T19:29:39","date_gmt":"2012-11-20T19:29:39","guid":{"rendered":"http:\/\/pages.charlotte.edu\/john-risley\/?page_id=16"},"modified":"2013-04-08T18:45:42","modified_gmt":"2013-04-08T18:45:42","slug":"risley-group-home-page","status":"publish","type":"page","link":"https:\/\/pages.charlotte.edu\/john-risley\/risley-group-home-page\/","title":{"rendered":"Risley Group Home Page"},"content":{"rendered":"

John M. Risley – Professor<\/h3>\n\n\n\n\n\n\n\n\n
Areas of research:<\/td>\nKinetic and physical studies of the lysosomal enzyme glycosylasparaginase. The\u00a018<\/sup>O isotope shift in NMR.<\/td>\n<\/tr>\n
Undergraduate institution:<\/td>\nBall State University, Muncie, Indiana<\/td>\n<\/tr>\n
Graduate institution:<\/td>\nPurdue University, West Lafayette, Indiana<\/td>\n<\/tr>\n
Postdoctoral experience:<\/td>\nPurdue University, West Lafayette, Indiana<\/td>\n<\/tr>\n
Phone number:<\/td>\n(704) 687-4844<\/td>\n<\/tr>\n
E-mail:<\/td>\njmrisley@uncc.edu<\/a><\/td>\n<\/tr>\n<\/tbody>\n<\/table>\n

 <\/p>\n

I. Studies of Glycosylasparaginase, an Enzyme Associated with a Lysosomal Storage Disease<\/h3>\n

The catabolism of glycoproteins to the constituent amino acids and monosaccharides involves many different enzymes. While the enzymes that hydrolyze the peptide bonds in the polypeptide chain to amino acids show a generally broad activity toward different amino acid side chains, the enzymes that hydrolyze the bonds between the sugars in the carbohydrate moieties of glycoproteins generally have a high degree of specificity. A key enzyme in the catabolism of N-linked carbohydrate moieties is glycosylasparaginase, which hydrolyzes the amide bond between asparagine and N-acetylglucosamine to give aspartic acid and 1-amino-N-acetylglucosamine as shown below.<\/p>\n

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\nA decrease in activity of this enzyme gives rise to aspartylglucosaminuria, an inherited lysosomal storage disease, that leads to mental retardation and a shortened life span as the metabolite accumulates in cells, tissues, and body fluids. There is no cure for the disorder. Not very much is known about the physical or kinetic properties of the enzyme. Mutations that give rise to the disorder have been elucidated and a crystal structure for the enzyme has been recently published. My lab is studying the physical and kinetic properties of the enzyme. Since so little is known about the protein, the fundamental properties that can be studied are quite numerous. We synthesize potential substrate analogues for the enzyme, inhibitors, possible suicide substrates, and transition-state analogues and study their properties with the enzyme. We are also using molecular modeling of the enzyme in order to study various properties.<\/p>\n

II. The\u00a018<\/sup>O Isotope Shift in NMR.<\/h3>\n

NMR spectroscopy is a very important analytical tool in chemistry. It is used in almost all areas of chemistry, including analytical, biochemistry, inorganic, organic, and physical chemistry. One small area, and specialization, of study in NMR is the effect of isotopes on NMR active nuclei. Oxygen has three naturally-occurring isotopes,\u00a016<\/sup>O,\u00a017<\/sup>O and\u00a018<\/sup>O;\u00a016<\/sup>O is the most abundant at 99+%. Two NMR-active nuclei that are in important oxygen-containing compounds are\u00a013<\/sup>C and\u00a031<\/sup>P. The NMR signals of\u00a013<\/sup>C and31<\/sup>P have slightly different chemical shifts when bonded to\u00a016<\/sup>O and\u00a018<\/sup>O; the differences are very small – a few ppb (parts per billion) – but can be readily detected when the NMR spectrometer is correctly set up. We are using these\u00a018<\/sup>O isotope shifts in\u00a013<\/sup>C NMR and\u00a031<\/sup>P NMR to study reactions and properties of molecules.<\/p>\n","protected":false},"excerpt":{"rendered":"

John M. Risley – Professor Areas of research: Kinetic and physical studies of the lysosomal enzyme glycosylasparaginase. The\u00a018O isotope shift in NMR. Undergraduate institution: Ball State University, Muncie, Indiana Graduate institution: Purdue University, West Lafayette, Indiana Postdoctoral experience: Purdue University, West Lafayette, Indiana Phone number: (704) 687-4844 E-mail: jmrisley@uncc.edu   I. Studies of Glycosylasparaginase, an […]<\/p>\n","protected":false},"author":582,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"open","template":"","meta":{"jetpack_post_was_ever_published":false,"footnotes":""},"class_list":["post-16","page","type-page","status-publish","hentry"],"jetpack_shortlink":"https:\/\/wp.me\/P2UMQA-g","jetpack_sharing_enabled":true,"_links":{"self":[{"href":"https:\/\/pages.charlotte.edu\/john-risley\/wp-json\/wp\/v2\/pages\/16","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/pages.charlotte.edu\/john-risley\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/pages.charlotte.edu\/john-risley\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/pages.charlotte.edu\/john-risley\/wp-json\/wp\/v2\/users\/582"}],"replies":[{"embeddable":true,"href":"https:\/\/pages.charlotte.edu\/john-risley\/wp-json\/wp\/v2\/comments?post=16"}],"version-history":[{"count":5,"href":"https:\/\/pages.charlotte.edu\/john-risley\/wp-json\/wp\/v2\/pages\/16\/revisions"}],"predecessor-version":[{"id":32,"href":"https:\/\/pages.charlotte.edu\/john-risley\/wp-json\/wp\/v2\/pages\/16\/revisions\/32"}],"wp:attachment":[{"href":"https:\/\/pages.charlotte.edu\/john-risley\/wp-json\/wp\/v2\/media?parent=16"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}