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University of Illinois at Urbana-Champaign
Methylmalonyl -Coa Decarboxylase (Ygfg) for Escherichia Coli: A New Activity for the Crotonase Superfamily
Abstract
dc:descriptionThe 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.
Degree
thesis:*- Name thesis:degree_name
- Ph.D.
- Level thesis:degree_level
- Dissertation
- Discipline thesis:degree_discipline
- Biochemistry
- Grantor
- University of Illinois at Urbana-Champaign
- Year dc:date
- 2015
Author and committee
dc:creator, dc:contributor.*- Author dc:creator
-
- Haller, Toomas
- Contributors dc:contributor
-
- Gerlt, John A.
Subjects
dc:subject × 1Rights
- Language dc:language
- eng
Identifiers
dc:identifier.*- Identifier
- (MiAaPQ)AAI3023070
- OAI identifier oai:identifier
- oai:www.ideals.illinois.edu:2142/84776