Anabolic incorporation of oxalate by Oxalobacter formigenes
Article Abstract:
Oxalobacter formigenes uses the glycerate pathway to assimilate carbon from oxalate. Cell free lysates of O. formigenes, grown anaerobically in the presence of oxalates, showed enzymatic activities of the enzymes of the glycerate pathway, like oxalyl coenzyme A reductase, glyoxylate carboligase, tartronic semialdehyde reductase, glycerate kinase, and glyoxylate dehydrogenase. Enzyme activities of serine-glyoxylate aminotransferase, an enzyme characteristic of the serine pathway, are not detected. The carbon assimilated from oxalate is reduced to 3-phosphoglycerate prior to entering common biosynthetic pathways.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1996
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Purification of two nitrate reductases from Xanthomonas maltophila grown in aerobic cultures
Article Abstract:
An investigation was conducted to elucidate the nitrate reductase (NR) system of Xanthomonas maltophila, which can aerobically convert nitrate tonitrite, but is unable to anaerobically respire on nitrate. Membrane fraction analysis and enzyme assays showed that X. maltophila produces two nitrate reductases, designated NR-I and NR-II. Characterization of these NRs showed that NR-I contains cytochrome b and oxidizes menaquinol. NR-II has smaller alpha- and beta-subunits, and has lower contents of iron and molybdenum.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1992
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Microbial transformation of benzocyclobutene to benzocyclobutene-1-ol and benzocyclobutene-1-one
Article Abstract:
Intact cells of Pseudomonas fluorescens 127-68 XVII, which contains the naphthalene dioxygenase system, were used to study the oxidation of benzocyclobutene (BCB). Gas chromatographic analysis of oxidation products showed the consistent presence of two metabolites with similar polarities and boiling points. Further characterization of these products identified them as BCB-1-ol, which represents the initial oxidation product of BCB, and BCB-1-one, the product of dehydrogenation of BCB-1-ol.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1992
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