Biosynthetic pathways in Oxalobacter formigenes
dc.contributor.advisor | Milton J. Allison | |
dc.contributor.advisor | Alan A. DiSpirito | |
dc.contributor.author | Cornick, Nancy | |
dc.contributor.department | Veterinary Microbiology and Preventive Medicine | |
dc.date | 2018-08-23T00:10:34.000 | |
dc.date.accessioned | 2020-06-30T07:08:31Z | |
dc.date.available | 2020-06-30T07:08:31Z | |
dc.date.copyright | Sun Jan 01 00:00:00 UTC 1995 | |
dc.date.issued | 1995 | |
dc.description.abstract | <p>Oxalate is the only substrate that supports the growth of the gram negative anaerobe, Oxalobacter formigenes. Oxalate is decarboxylated to formate plus CO[subscript]2. A small amount of acetate (0.5-1 mM) is required for biosynthetic reactions. Oxalate is reduced and assimilated into cell biomass by aerobic oxalate-degrading bacteria using either the glycerate pathway or the serine pathway. Oxalate is reduced to 3P-glycerate and assimilated as a C[subscript]3 unit. We detected the enzymatic activities of glycerate pathway but not those of the serine pathway in cell-free extracts of O. formigenes;Four potential sources of carbon for cell biomass are available to O. formigenes, oxalate, acetate, formate and CO[subscript]2. We grew the organism in [superscript]14 C labeled carbon sources and determined the contribution of each of these sources to cell carbon. O. formigenes derived at least 54% of its cell carbon from oxalate and at least 7% from acetate. The only other carbon source utilized was CO[subscript]3. Formate was not incorporated to a significant extent. Carbon from [superscript]14 C-oxalate and [superscript]14 CO[subscript]3 was detected in amino acids derived from [alpha]-ketoglutarate, oxaloacetate, pyruvate, 3P-glycerate and in the aromatic amino acids. Amino acids derived from [alpha]-ketoglutarate, oxaloacetate and pyruvate contained carbon derived from [superscript]14 C-acetate;When O. formigenes was grown on [superscript]13 C-labeled oxalate, acetate or CO[subscript]3,the labeling patterns of the amino acids were consistent with their formation through common biosynthetic pathways. [superscript]13 C from oxalate was detected in the majority of the carbons from all of the amino acids. Approximately 60% of the acetate was incorporated as a C[subscript]2 unit into four amino acids (glutamate, proline, arginine and leucine). The other 40% of the acetate was split and was detected in amino acids derived from oxaloacetate and pyruvate;Enzymatic activities detected in cell-free extracts included: glutamate dehydrogenase, phosphoenolpyruvate carboxylase, pyruvate carboxylase, citrate synthase and isocitrate dehydrogenase. These findings support the [superscript]14 C and [superscript]13 C data which indicate that O. formigenes assimilates acetate into protein using the first third of the TCA pathway and that C[subscript]4 units are formed from C[subscript]3 units by carboxylation of pyruvate or PEP.</p> | |
dc.format.mimetype | application/pdf | |
dc.identifier | archive/lib.dr.iastate.edu/rtd/10893/ | |
dc.identifier.articleid | 11892 | |
dc.identifier.contextkey | 6423314 | |
dc.identifier.doi | https://doi.org/10.31274/rtd-180813-11245 | |
dc.identifier.s3bucket | isulib-bepress-aws-west | |
dc.identifier.submissionpath | rtd/10893 | |
dc.identifier.uri | https://dr.lib.iastate.edu/handle/20.500.12876/64089 | |
dc.language.iso | en | |
dc.source.bitstream | archive/lib.dr.iastate.edu/rtd/10893/r_9531729.pdf|||Fri Jan 14 18:30:04 UTC 2022 | |
dc.subject.disciplines | Biochemistry | |
dc.subject.disciplines | Microbiology | |
dc.subject.keywords | Microbiology | |
dc.subject.keywords | immunology and preventive medicine | |
dc.subject.keywords | Microbiology | |
dc.title | Biosynthetic pathways in Oxalobacter formigenes | |
dc.type | article | |
dc.type.genre | dissertation | |
dspace.entity.type | Publication | |
relation.isAuthorOfPublication | a89b8fad-4329-4bb1-bbcd-c1d3b324f0f7 | |
relation.isOrgUnitOfPublication | 16f8e472-b1cd-4d8f-b016-09e96dbc4d83 | |
thesis.degree.level | dissertation | |
thesis.degree.name | Doctor of Philosophy |
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