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W B Dempsey

Publications and source records attributed to W B Dempsey.

49 records · Page 3Linked to original sources

Characterization of pyridoxine auxotrophs of Escherichia coli: serine and pdxF mutants.

At least six phenotypically distinct classes of mutants of Escherichia coli which require serine or pyridoxine or both can be isolated. Three of the six classes lack 3-phosphoserine-2-oxoglutarate aminotransferase. One of these classes contains WG5, a mutant previously characterized as containing the pdxF5 allele. The aminotransferase isolated from this mutant has been compared to that isolated from wild-type E. coli and found to have apparently normal affinity for pyridoxal 5'-phosphate, but reduced affinity for pyridoxamine 5'-phosphate.

Culture Media↗

Metabolism of alpha-aminoisobutyric acid by soil bacteria.

Eleven different bacteria, isolated by enrichment procedures on alpha-aminoisobutyric (AIB) as sole fixed nitrogen source, were examined for the mechanism by which they attacked the amino acid. All eleven organisms, including one which grew well on isopropylamine, converted AIB to acetone and CO(2) and showed an absolute dependence upon pyruvate for this reaction. No organism isolated degraded AIB to isopropylamine as the primary reaction. The data suggested that the usual mode of attack upon this amino acid is by an overall reaction comprised of two half reactions, one a decarboxylation-dependent transamination and the other a normal exchange transamination.

Acetone↗

Characterization of pyridoxine auxotrophs of Escherichia coli: P1 transduction.

Pyridoxine mutants of Escherichia coli B, previously divided into a minimum of six groups by cross-feeding tests, were characterized by transduction studies performed with phage P1bt. The results of these studies allowed division of pyridoxine mutants into five unlinked groups and set the minimum number of enzymes between pyridoxal phosphate and a metabolite common to other pathways at six or seven, with the probable maximum at ten. One group was shown to be linked to thr, leu, and pyrA.

Alleles↗

Isolation and characterization of pyridoxine auxotrophs of Escherichia coli.

Dempsey, Walter B. (University of Florida, Gainesville), and P. F. Pachler. Isolation and characterization of pyridoxine auxotrophs of Escherichia coli. J. Bacteriol. 91:642-645. 1966.-Pyridoxine auxotrophs of Escherichia coli B have been consistently produced by a modified penicillin enrichment method. This modified penicillin technique included a 6-hr growth period in the absence of any pyridoxine followed by a 2-hr treatment with penicillin at 1,000 units per ml. Penicillin was removed from these cultures by membrane filtration and the process was repeated. A minimum of three cycles was found necessary to isolate auxotrophs. Different phenotypes within the group of pyridoxine auxotrophs were distinguished by their responses to feeding with the various forms of pyridoxine, as well as by cross-feeding tests. Two auxotrophs were also differentiated by their frequency of reversion to prototrophy. Cross-feeding tests indicated that seven of the phenotypes fed in a linear sequence. These phenotypes had a very low frequency of reversion. The auxotrophs with a high frequency of reversion cross-fed in a linear sequence and fed the first five of the other seven auxotrophs. One of the auxotrophs isolated was a pyridoxal auxotroph.

Escherichia coli↗

Synthesis of Pyridoxine by a Pyridoxal Auxotroph of Escherichia coli.

Dempsey, Walter B. (University of Florida, Gainesville). Synthesis of pyridoxine by a pyridoxal auxotroph of Escherichia coli. J. Bacteriol. 92:333-337. 1966.-A pyridoxal auxotroph of Escherichia coli B produced pyridoxol and pyridoxol 5'-phosphate during starvation for pyridoxal. The identification of these compounds was made both by bioassay and by ion-exchange chromatography. Pyridoxol 5'-phosphate oxidase activity was absent in extracts of the auxotroph. The rate of synthesis of total pyridoxine by a pyridoxal-starved culture of this auxotroph was 6.0 x 10(-6) moles per mg per hr. Cellular content of pyridoxine was constant at 4.0 x 10(-10) moles/mg.

Journal Article↗