A common regulator for the operons encoding the enzymes involved in D-galactarate, D-glucarate, and D-glycerate utilization in Escherichia coli.

Genes for D-galactarate (gar) and D-glucarate (gud) metabolism in Escherichia coli are organized in three transcriptional units: garD, garPLRK, and gudPD. Two observations suggested a common regulator for the three operons. (i) Their expression was triggered by D-galactarate, D-glucarate, and D-glycerate.

Genetic analysis of a chromosomal region containing genes required for assimilation of allantoin nitrogen and linked glyoxylate metabolism in Escherichia coli.

Growth experiments with Escherichia coli have shown that this organism is able to use allantoin as a sole nitrogen source but not as a sole carbon source. Nitrogen assimilation from this compound was possible only under anaerobic conditions, in which all the enzyme activities involved in allantoin metabolism were detected. Of the nine genes encoding proteins required for allantoin degradation, only the one encoding glyoxylate carboligase (gcl), the first enzyme of the pathway leading to glycerate, had been identified and mapped at centisome 12 on the chromosome map.

Site-directed mutagenesis studies of the metal-binding center of the iron-dependent propanediol oxidoreductase from Escherichia coli.

The amino acid residues involved in the metal-binding site in the iron-containing dehydrogenase family were characterized by the site-directed mutagenesis of selected candidate residues of propanediol oxidoreductase from Escherichia coli. Based on the findings that mutations H263R, H267A and H277A resulted in iron-deficient propanediol oxidoreductases without catalytic activity, we identified three conserved His residues as iron ligands, which also bind zinc. The Cys362, a residue highly conserved among these dehydrogenases, was considered another possible ligand by comparison with the sequences of the medium-chain dehydrogenases.

Evolution of an Escherichia coli protein with increased resistance to oxidative stress.

L-1,2-Propanediol:NAD+ 1-oxidoreductase of Escherichia coli is encoded by the fucO gene, a member of the regulon specifying dissimilation of L-fucose. The enzyme normally functions during fermentative growth to regenerate NAD from NADH by reducing the metabolic intermediate L-lactaldehyde to propanediol which is excreted. During aerobic growth L-lactaldehyde is converted to L-lactate and thence to the central metabolite pyruvate.

Transcriptional regulation of the Escherichia coli rhaT gene.

Transcriptional regulation of the rhaT gene, one of the operons forming the rhamnose regulon in Escherichia coli, was studied by fusing its complete or deleted promoter to the reporter gene lacZ. Analysis of beta-galactosidase activities induced in these constructions grown under different conditions predicted the presence of two putative control elements: one for the RhaS regulatory protein and activating the gene not only by L-rhamnose but also by L-lyxose or L-mannose, the other for cAMP-catabolite repression protein and activating this gene in the absence of glucose. Anaerobiosis increased the promoter function two- to threefold with respect to the aerobic condition.

Stability studies and effect of the initial oleic acid concentration on lipase production by Candida rugosa.

The production of lipase by Candida rugosa in batch cultures was studied. The initial concentration of the carbon source employed, oleic acid, had an important effect on the final lipolytic activity levels. The maximum lipase/substrate yield and specific productivity obtained correspond to an initial oleic acid concentration of 2 g/l.

Efficient biodegradation of high-molecular-weight polyethylene glycols by pure cultures of Pseudomonas stutzeri.

Biodegradation of polyethylene glycols (PEGs) of up to 13,000 to 14,000 molecular weight has been shown to be performed by a river water bacterial isolate (strain JA1001) identified as Pseudomonas stutzeri. A pure culture of strain JA1001 grew on PEG 1000 or PEG 10000 at 0.2% (wt/vol) as a sole source of carbon and energy with a doubling time of 135 or 150 min, respectively.

Aerobic excretion of 1,2-propanediol by Salmonella typhimurium.

Salmonella typhimurium excreted the rhamnose fermentation product 1,2-propanediol not only under anaerobic conditions, but also under aerobic conditions. The absence of an aldehyde dehydrogenase enzymatic activity that oxidizes to lactate the lactaldehyde formed in the dissimilation of rhamnose raised the intracellular concentration of the aldehyde which was alternatively reduced to the excretable 1,2-propanediol by a residual propanediol oxidoreductase activity.

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 further metabolized, provided the culture was kept under anaerobic conditions. n-Propanol and propionate were found in the medium as end products of this process at concentrations one-half that of 1,2-propanediol.