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oai:www.ideals.illinois.edu:2142/84902 2023-07-11 col_2142_5131 col_2142_14795 com_2142_5130 com_2142_14794 com_2142_14793 com_2142_8903

Gerlt, John A. Wieczorek, Stacey Jean 2015-09-25T22:28:25Z 2015-09-25T22:28:25Z 10000-01-01 1999 1999 The crystal structure of GalD indicates that His 185 may serve as a general acid catalyst to facilitate the departure of the 3-OH leaving group and/or stereospecifically protonate the product in the subsequent tautomerization reaction. The function of His 185 was investigated by comparing the kinetics of wild type, H285N, E310Q, H185Q and H185N GalD mutants, using both D-galactonate and 3-fluoro-3-deoxy-galactonate (F-Gal) as substrates. The kcat values for all the mutants decreased with D-galactonate, but only the kcat values for H185Q and H185N were relatively unaffected with F-Gal. Solvent deuterium incorporation studies with H185Q and H185N indicated that deuterium is stereospecifically protonated at the pro-S position. Thus, His 185 is involved in the beta-elimination of 3-OH but does not protonate the product in the subsequent tautomerization reaction. Made available in DSpace on 2015-09-25T22:28:25Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 9921753.pdf: 5463079 bytes, checksum: 8032e7e916648e941f4069e1d8f9edd2 (MD5) Previous issue date: 1999 Embargo set by: Seth Robbins for item 86183 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs U of I Only 151 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1999. http://hdl.handle.net/2142/84902 (MiAaPQ)AAI9921753 eng Chemistry, Organic Galactonate Dehydratase: Exploring the Frontiers of the Enolase Superfamily text Biochemistry Biochemistry University of Illinois at Urbana-Champaign Dissertation Ph.D.