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University of Illinois at Urbana-Champaign
Studies on the Mechanism of the Pyruvate Oxidase Flavoprotein of Escherichia Coli (Rapid Kinetics, Biochemical Software, Lipid-Activated Enzyme)
Abstract
dc:descriptionThe pyruvate oxidase flavoprotein catalyzes the oxidative decarboxylation of pyruvate to acetate and carbon dioxide. Flavin adenine dinucleotide and thiamin pyrophosphate are cofactors. The enzymatic activity of the purfied flavoprotein is very low in the absence of lipids. Following reduction by substrate, lipids and many other other amphiphilic substances bind to a high affinity site on the flavoenzyme and stimulate the activity about 25 fold. The enzyme can also be activated by controlled proteolysis of the reduced flavoenzyme, which destroys the high affinity lipid site.
Degree
thesis:*- Name thesis:degree_name
- Ph.D.
- Level thesis:degree_level
- Dissertation
- Discipline thesis:degree_discipline
- Chemistry
- Grantor
- University of Illinois at Urbana-Champaign
- Year dc:date
- 2014
Author and committee
dc:creator, dc:contributor.*- Author dc:creator
-
- Mather, Michael Wayne
Subjects
dc:subject × 1Identifiers
dc:identifier.*- Identifier
- (UMI)AAI8422129
- OAI identifier oai:identifier
- oai:www.ideals.illinois.edu:2142/70255