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Genetic analysis of a chromosomal region containing genes required for assimilation of allantoin nitrogen and linked glyoxylate metabolism in Escherichia coli.
A systematic analysis of the gene cluster was undertaken to identify genes involved in allantoin utilization, and the products of these genes were overexpressed and shown to have the predicted corresponding enzyme activities. Expand
The gene yjcG, cotranscribed with the gene acs, encodes an acetate permease in Escherichia coli.
The time course of [1,2-(14)C]acetate uptake and the results of a concentration kinetics analysis performed with cells expressing ActP or cells deficient in ActP supported the the hypothesis that this carrier is an acetate transporter and suggested that there may be another transport system for this monocarboxylate. Expand
Crystal structure of an iron-dependent group III dehydrogenase that interconverts L-lactaldehyde and L-1,2-propanediol in Escherichia coli.
The FucO structure presented here is the first structure for a member of the group III bacterial dehydrogenases shown experimentally to contain iron, and Asp39 appears to be the key residue for discriminating against NADP(+). Expand
Role of secreted glyceraldehyde-3-phosphate dehydrogenase in the infection mechanism of enterohemorrhagic and enteropathogenic Escherichia coli: interaction of the extracellular enzyme with human
Observations indicate that exported GAPDH may act as a virulence factor which could contribute to EHEC and EPEC pathogenesis. Expand
glc locus of Escherichia coli: characterization of genes encoding the subunits of glycolate oxidase and the glc regulator protein.
The locus glc (min 64.5), associated with the glycolate utilization trait in Escherichia coli, is known to contain glcB, encoding malate synthase G, and the gene(s) needed for Glycolate oxidase activity, and five additional genes: glcC and in the other direction glcD,glcE, glcF, and glcG followed by glcb, may encode the glc regulator protein. Expand
Anaerobic metabolism of the L-rhamnose fermentation product 1,2-propanediol in Salmonella typhimurium.
When grown anaerobically on L-rhamnose, Salmonella typhimurium excreted 1,2-propanediol as a fermentation product. Upon exhaustion of the methyl pentose, 1,2-propanediol was recaptured and furtherExpand
Fermentation mechanism of fucose and rhamnose in Salmonella typhimurium and Klebsiella pneumoniae.
The detection of an equimolar amount of 1,2-propanediol was detected in the medium when Salmonella typhimurium or Klebsiella pneumoniae fermented L-fucose or L-rhamnose, indicating that L- fucose and L- rhamnosed fermentation takes place in these species by 1, 2-pro panediol production and excretion. Expand
L-lyxose metabolism employs the L-rhamnose pathway in mutant cells of Escherichia coli adapted to grow on L-lyxose.
The mutated rhamnulose kinase, mapped in the rha locus, enabled the growth of the mutant cells on L-lyxose, and the glycolaldehyde generated in the cleavage of L-xylulose 1-phosphate by the rhamNulose-1-ph phosphate aldolase was oxidized by lactaldehyde dehydrogenase to glycolate, a compound normally utilized by E. coli. Expand
Proteomic analysis of outer membrane vesicles from the probiotic strain Escherichia coli Nissle 1917
This study describes the first global OMV proteome of a probiotic strain and provides evidence that probiotic‐derived OMVs contain proteins that can target these vesicles to the host and mediate their beneficial effects on intestinal function. Expand
Dual role of LldR in regulation of the lldPRD operon, involved in L-lactate metabolism in Escherichia coli.
Results were consistent with the hypothesis that LldR has a dual role, acting as a repressor or an activator of lldPRD, and it is proposed that in the absence of L-lactate, L AldR binds to both O1 and O2, probably leading to DNA looping and the repression of transcription. Expand