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oai:www.ideals.illinois.edu:2142/87888 2023-07-11 col_2142_5131 col_2142_14789 com_2142_5130 com_2142_14788 com_2142_8903

2006 Wilfred Van Der Donk Relyea, Heather Ann 2015-09-28T21:57:27Z 2015-09-28T21:57:27Z 10000-01-01 2006 The pH-rate profiles for active site mutants Lys76Ala, Glu266G1n, and Arg237Lys are also bell-shaped and the higher pKa of each is 8.4, which is also consistent with that observed for the pH dependence of sulfite inhibition for the wild type enzyme. Interestingly, the acidic limb of the Glu266Gln kcat/Km,HPt profile reveals a pKa of 7.2, which has been attributed to His292. A second variant, G1u266A1a, has a pH profile for kcat which is defined by a single pKa at 6.85 +/- 0.05 which also appears to be due to His292. The decrease in pKa for these mutants compared with the wild type indicates that a hydrogen bond exists between His292 and Glu266, and that interaction has been removed by replacing Glu266 with a neutral residue. Made available in DSpace on 2015-09-28T21:57:27Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3242970.pdf: 2971025 bytes, checksum: 168192ba6678e41248a63eaa9efc9abd (MD5) Previous issue date: 2006 Embargo set by: Seth Robbins for item 89169 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 111 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2006. http://hdl.handle.net/2142/87888 (MiAaPQ)AAI3242970 eng Chemistry, Biochemistry Kinetic Analysis and pH Dependence of the Phosphite Dehydrogenase Reaction text University of Illinois at Urbana-Champaign Dissertation Ph.D.