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Gerlt, John A. Haller, Toomas 2015-09-25T22:27:50Z 2015-09-25T22:27:50Z 10000-01-01 2001 2001 The E113Q mutant exhibited significantly larger isotope effect for both kcat and kcat/Km than wild-type, suggesting differences in reaction mechanism between wild type and E113Q. Although experimental difficulties encountered did not allow quantitative studies of stereochemistry of the MMDC reaction, the reaction catalyzed by wild-type MMDC proceeds with retention of configuration using (S)-methylmalonyl-CoA as a substrate, and with inversion of configuration using (R)-methylmalonyl-CoA as a substrate. H66F catalyzed the MMDC reaction with at least partial racemization. I postulated that His66 is important in retaining structure of the active site. Made available in DSpace on 2015-09-25T22:27:50Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3023070.pdf: 9796868 bytes, checksum: a1905793dc00dee2c26cbf098e5da6c4 (MD5) Previous issue date: 2001 Embargo set by: Seth Robbins for item 86057 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 192 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2001. http://hdl.handle.net/2142/84776 (MiAaPQ)AAI3023070 eng Biology, Microbiology Methylmalonyl -Coa Decarboxylase (Ygfg) for Escherichia Coli: A New Activity for the Crotonase Superfamily text Biochemistry Biochemistry University of Illinois at Urbana-Champaign Dissertation Ph.D.