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Title:Methylmalonyl -Coa Decarboxylase (Ygfg) for Escherichia Coli: A New Activity for the Crotonase Superfamily
Author(s):Haller, Toomas
Doctoral Committee Chair(s):Gerlt, John A.
Department / Program:Biochemistry
Discipline:Biochemistry
Degree Granting Institution:University of Illinois at Urbana-Champaign
Degree:Ph.D.
Genre:Dissertation
Subject(s):Biology, Microbiology
Abstract: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.
Issue Date:2001
Type:Text
Language:English
Description:192 p.
Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2001.
URI:http://hdl.handle.net/2142/84776
Other Identifier(s):(MiAaPQ)AAI3023070
Date Available in IDEALS:2015-09-25
Date Deposited:2001


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