Abstract
Oxalate is the only substrate that supports the growth of Oxalobacter formigenes, an anaerobic, gram negative rod that inhabits the intestinal tract of many mammals. Oxalate is decarboxylated to formate and CO2 in a nearly 1:1 ratio but some carbon from oxalate is also used for cell synthesis. Two pathways for assimilation of oxalate (the glycerate pathway and the serine pathway) have been described in aerobic bacteria. We found that cell-free lysates of O. formigenes contained the following enzymatic activities: oxalyl-CoA reductase, glyoxylate carboligase, tartronic semialdehyde reductase, glycerate kinase, hydroxypyruvate reductase and glyoxylate dehydrogenase. No evidence for serine-giyoxylate aminotransferase found. These results support the concept that 0. formigenes assimilates carbon from oxalate using the glycerate pathway and that the serine pathway is not functional.
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