University of Illinois at Urbana-Champaign
Metabolism of Gallic Acid by Eubacterium Oxidoreducens
Abstract
dc:descriptionGallate was decarboxylated by cell extracts of Eubacterium oxidoreducens with pyrogallol as the only detectable product. A phloro-glucinol reductase catalyzed the conversion of phloroglucinol to dihydrophloroglucinol, using NADPH as the source of electrons. Extracts of cells grown on gallate and formate contained formate dehydrogenase (EC 1.2.1.43) and hydrogenase (EC 1.88.99.1), which were both NADP-linked. These results suggest that the oxidation of formate or H$\sb2$ may be indirectly linked to the reduction of phloroglucinol. A dihydrophloroglucinolase was present, which hydrolyzed dihydrophloroglucinol to 3-hydroxy-5-oxohexanoate. This six-carbon ring cleavage product presumably can be broken down by a series of reactions similar to β-oxidation. These reactions cleaved the six carbon acid to 3-hydroxybutyryl-CoA yielding acetate and butyrate as end products. A number of key enzymes involved in β-oxidation and substrate level phosphorylation were demonstrated in cell extracts.
Degree
thesis:*- Name thesis:degree_name
- Ph.D.
- Level thesis:degree_level
- Dissertation
- Discipline thesis:degree_discipline
- Dairy Science
- Grantor
- University of Illinois at Urbana-Champaign
- Year dc:date
- 2014
Author and committee
dc:creator, dc:contributor.*- Author dc:creator
-
- Krumholz, Lee Richard
Subjects
dc:subject × 1Identifiers
dc:identifier.*- Identifier
- (UMI)AAI8823176
- OAI identifier oai:identifier
- oai:www.ideals.illinois.edu:2142/71736