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PubMed1980

Some synthetic phytotoxins structurally related to rhynchosporoside.

The (2-O)alpha-d-glucopyranoside of 1,2-propanediol and [U-(14)C]glucose were used as substrates in a reaction with almond beta-glucosidase, which resulted in the production of some (2-O)alpha-d-oligoglucosides of 1,2-propanediol. As its substrate, the beta-glucosidase preferred the glucoside isomer that rotates plane-polarized light to the right. Some of the glucosides produced in the enzymic reaction mixture possessed host selective toxin activity. It appears that the biological activity of the toxin is not dependent on the nature of the glycosidic linkage with the aglycone.

Journal Article↗
PubMed1990

Primary stimuli of icosanoid release inhibit arachidonoyl-CoA synthetase and lysophospholipid acyltransferase. Mechanism of action of hydrogen peroxide and methyl mercury in platelets.

Icosanoid formation in platelets depends on the concentration of free arachidonate that is mainly liberated from membrane phospholipids by phospholipase A2. The concentration of free arachidonate is also controlled by the activities of the reacylating enzymes arachidonoyl-CoA synthetase and lysophospholipid acyltransferase. In human platelet microsomes we determined the high enzyme activities of 5.9 nmol.min-1.(10(9) platelets)-1 for the arachidonoyl-CoA synthetase and 37 nmol.min-1.(10(9) platelets)-1 for the lysophospholipid acyltransferase. The activities of these reacylating enzymes were strongly reduced by hydrogen peroxide (H2O2) and methyl mercury that are primary stimuli of arachidonate release in intact platelets. H2O2 inhibited the arachidonoyl-CoA synthetase with an IC50 of 3.3 mmol/l without affecting the lysophospholipid acyltransferase. Sulfhydryl group protection by 3-mercapto-1,2-propanediol did not overcome the inhibition but glutathione prevented the inhibition of the arachidonoyl-CoA synthetase by H2O2. This suggests that glutathione by virtue of the glutathione peroxidase reduces H2O2 rather than that it protects free sulfhydryl groups of the arachidonoyl-CoA synthetase. Methyl mercury left the arachidonoyl-CoA synthetase activity unaffected but inhibited the lysophospholipid acyltransferase activity with an IC50 of 3.4 mumol/l. The inhibition is probably evoked by the blockade of sulfhydryl groups of the lysophospholipid acyltransferase because it disappeared when 3-mercapto-1,2-propanediol was added at a concentration higher than that of methyl mercury. Thrombin as a physiological full agonist, Ca2+ less than or equal to 1 mmol/l, the calcium ionophore A23187 and phorbol 12-myristate 13-acetate (TPA) and 1-oleoyl-2-acetylglycerol as model stimuli of protein kinase C neither influenced arachidonoyl-CoA synthetase nor lysophospholipid acyltransferase. It is concluded that the inhibitory effect of H2O2 and methyl mercury on the arachidonate-reacylating enzymes arachidonoyl-CoA synthetase or lysophospholipid acyltransferase, respectively, are responsible for their capacity to stimulate icosanoid release in intact cells. Thrombin and its intracellular messengers Ca2+ and diacylglycerol do not directly affect arachidonoyl-CoA synthetase and lysophospholipid acyltransferase.

Acyltransferases↗
PubMed1988

The effect of solvent extraction on the lipids of the stratum corneum in relation to observed immediate whitening of the skin.

Irritant contact dermatitis along with an increased transepidermal water loss can result from exposing the skin to solvents. A study of the interaction of various solvents with human stratum corneum was made using thin-layer chromatography. Comparison of 10 solvents (trichloroethylene, toluene, dimethylsulfoxide, n-hexane, 1,2-propanediol, carbon tetrachloride, methyl ethyl ketone, ethanol, acetone, distilled water) showed that 3 solvents (dimethylsulfoxide, 1,2 propanediol, distilled water) did not extract lipids from intact human stratum corneum. The findings are discussed in relation to the visual appearance of skin (whitening) after exposure to solvents.

Chromatography, Thin Layer↗
PubMed1979

Xylose, arabinose, and rhamnose fermentation by Bacteroides ruminicola.

Metabolism and growth yields of Bacteroides ruminicola grown on d-xylose, l-arabinose, and l-rhamnose were studied. Growth yields were 62, 68, and 35.5 g (dry weight) per mol of carbohydrate fermented after correction for storage polysaccharide. Experiments with [1-(14)C]arabinose indicated that pentose was fermented by a pentose phosphate cycle plus glycolysis, with some indication of a minor phosphoketolase-type pathway. The product ratios from pentose were similar to those previously described for hexose. Rhamnose was fermented mainly to 1,2-propanediol, succinate, and acetate, although the latter was quantitatively less than expected. Estimates of adenosine 5'-triphosphate (ATP) molar growth yields could not be calculated with any certainty, as ATP generation by electron transport-linked phosphorylation cannot yet be assessed. If ATP were generated by substrate-level phosphorylation reactions alone, ATP molar growth yields for xylose, arabinose, and rhamnose would be 30, 28, and 35 g/mol. If calculations are based on an assumption that two ATP are generated by electron transport-linked phosphorylation per succinate, ATP molar growth yields become 15, 14, and 22 g/mol; if the assumption is also made that the pathway of lactaldehyde reduction is coupled to production of one ATP per 1,2-propanediol by electron transport-linked phosphorylation, the ATP molar growth yield for rhamnose fermentation becomes 14 g/mol. No preference can be expressed between these alternatives at present.

Adenosine Triphosphate↗
PubMed1988

Isolation and Characterization of a Thermophilic Bacterium Which Oxidizes Acetate in Syntrophic Association with a Methanogen and Which Grows Acetogenically on H(2)-CO(2).

We previously described a thermophilic (60 degrees C), syntrophic, two-membered culture which converted acetate to methane via a two-step mechanism in which acetate was oxidized to H(2) and CO(2). While the hydrogenotrophic methanogen Methanobacterium sp. strain THF in the biculture was readily isolated, we were unable to find a substrate that was suitable for isolation of the acetate-oxidizing member of the biculture. In this study, we found that the biculture grew on ethylene glycol, and an acetate-oxidizing, rod-shaped bacterium (AOR) was isolated from the biculture by dilution into medium containing ethylene glycol as the growth substrate. When the axenic culture of the AOR was recombined with a pure culture of Methanobacterium sp. strain THF, the reconstituted biculture grew on acetate and converted it to CH(4). The AOR used ethylene glycol, 1,2-propanediol, formate, pyruvate, glycine-betaine, and H(2)-CO(2) as growth substrates. Acetate was the major fermentation product detected from these substrates, except for 1,2-propanediol, which was converted to 1-propanol and propionate. N,N-Dimethylglycine was also formed from glycine-betaine. Acetate was formed in stoichiometric amounts during growth on H(2)-CO(2), demonstrating that the AOR is an acetogen. This reaction, which was carried out by the pure culture of the AOR in the presence of high partial pressures of H(2), was the reverse of the acetate oxidation reaction carried out by the AOR when hydrogen partial pressures were kept low by coculturing it with Methanobacterium sp. strain THF. The DNA base composition of the AOR was 47 mol% guanine plus cytosine, and no cytochromes were detected.

Journal Article↗
PubMed1992

Biodegradation of bisphenol A and other bisphenols by a gram-negative aerobic bacterium.

A novel bacterium designated strain MV1 was isolated from a sludge enrichment taken from the wastewater treatment plant at a plastics manufacturing facility and shown to degrade 2,2-bis(4-hydroxyphenyl)propane (4,4'-isopropylidenediphenol or bisphenol A). Strain MV1 is a gram-negative, aerobic bacillus that grows on bisphenol A as a sole source of carbon and energy. Total carbon analysis for bisphenol A degradation demonstrated that 60% of the carbon was mineralized to CO2, 20% was associated with the bacterial cells, and 20% was converted to soluble organic compounds. Metabolic intermediates detected in the culture medium during growth on bisphenol A were identified as 4-hydroxybenzoic acid, 4-hydroxyacetophenone, 2,2-bis(4-hydroxyphenyl)-1-propanol, and 2,3-bis(4-hydroxyphenyl)-1,2-propanediol. Most of the bisphenol A degraded by strain MV1 is cleaved in some way to form 4-hydroxybenzoic acid and 4-hydroxyacetophenone, which are subsequently mineralized or assimilated into cell carbon. In addition, about 20% of the bisphenol A is hydroxylated to form 2,2-bis(4-hydroxyphenyl)-1-propanol, which is slowly biotransformed to 2,3-bis(4-hydroxyphenyl)-1,2-propanediol. Cells that were grown on bisphenol A degraded a variety of bisphenol alkanes, hydroxylated benzoic acids, and hydroxylated acetophenones during resting-cell assays. Transmission electron microscopy of cells grown on bisphenol A revealed lipid storage granules and intracytoplasmic membranes.

Benzhydryl Compounds↗
PubMed1996

Physiologic Mechanisms Involved in Accumulation of 3-Hydroxypropionaldehyde during Fermentation of Glycerol by Enterobacter agglomerans.

When grown in 700 mM glycerol within the pH range 6.0 to 7.5, anaerobic pH-regulated cultures of Enterobacter agglomerans exhibited an extracellular accumulation of 3-hydroxypropionaldehyde (3-HPA). This phenomenon, which causes fermentation cessation, occurred earlier when pH was low. In contrast, substrate consumption was complete at pH 8. Levels of glycerol-catabolizing enzymes, i.e., glycerol dehydrogenase and dihydroxyacetone kinase for the oxidative route and glycerol dehydratase and 1,3-propanediol dehydrogenase for the reductive route, as well as the nucleotide pools were determined periodically in the pH 7- and pH 8-regulated cultures. A NAD/NADH ratio of 1.7 was correlated with the beginning of the production of the inhibitory metabolite. Further accumulation was dependent on the ratio of glycerol dehydratase activity to 1,3-propanediol dehydrogenase activity. For a ratio higher than 1, 3-HPA was produced until fermentation ceased, which occurred for the pH 7-regulated culture. At pH 8, a value below 1 was noticed and 3-HPA accumulation was transient, while the NAD/NADH ratio decreased. The low rate of glycerol dissimilation following the appearance of 3-HPA in the culture medium was attributed to the strong inhibitory effect exerted by 3-HPA on glycerol dehydrogenase activity.

Journal Article↗
PubMed1996

Properties of Allyl Alcohol-Resistant Mutants of Clostridium butyricum Grown on Glycerol.

Mutants of Clostridium butyricum E5 exhibiting resistance to allyl alcohol which produced the same quantities of 1,3-propanediol as the wild-type strain but more acetate than butyrate were isolated. The acetate-butyrate formation plays a major function in the regulation of the internal redox balance. Allyl alcohol resistance can be attributed not to the loss of 1,3-propanediol dehydrogenase but to a shift in the reductive properties of the enzyme. The data support the view that cellular regulation is modified to avoid intracellular accumulation of 3-hydroxypropionaldehyde.

Journal Article↗
PubMed2006

Whole-genome transcription profiling reveals genes up-regulated by growth on fucose in the human gut bacterium "Roseburia inulinivorans".

"Roseburia inulinivorans" is an anaerobic polysaccharide-utilizing firmicute bacterium from the human colon that was identified as a producer of butyric acid during growth on glucose, starch, or inulin. R. inulinivorans A2-194 is also able to grow on the host-derived sugar fucose, following a lag period, producing propionate and propanol as additional fermentation products. A shotgun genomic microarray was constructed and used to investigate the switch in gene expression that is involved in changing from glucose to fucose utilization. This revealed a set of genes coding for fucose utilization, propanediol utilization, and the formation of propionate and propanol that are up-regulated during growth on fucose. These include homologues of genes that are implicated in polyhedral body formation in Salmonella enterica. Dehydration of the intermediate 1,2-propanediol involves an enzyme belonging to the new B12-independent glycerol dehydratase family, in contrast to S. enterica, which relies on a B12-dependent enzyme. A typical gram-positive agr-type quorum-sensing system was also up-regulated in R. inulinivorans during growth on fucose. Despite the lack of genome sequence information for this commensal bacterium, microarray analysis has provided a powerful tool for obtaining new information on its metabolic capabilities.

Bacteria, Anaerobic↗
PubMed1987

Loss of aldehyde dehydrogenase in an Escherichia coli mutant selected for growth on the rare sugar L-galactose.

Escherichia coli K-12 converts L-fucose to dihydroxyacetone phosphate (C-1 to C-3) and L-lactaldehyde (C-4 to C-6) by a pathway specified by the fuc regulon. Aerobically, L-lactaldehyde serves as a carbon and energy source by the action of an aldehyde dehydrogenase of broad specificity; the product, L-lactate, is then converted to pyruvate. Anaerobically, L-lactaldehyde serves as an electron acceptor to regenerate NAD from NADH by the action of an oxidoreductase; the reduced product, L-12-propanediol, is excreted. A strain selected for growth on L-galactose (a structural analog of L-fucose) acquired a broadened inducer specificity because of an altered fucR gene encoding the activator protein for the fuc regulon (Y. Zhu and E. C. C. Lin, J. Mol. Evol. 23:259-266, 1986). In this study, a second mutation that abolished aldehyde dehydrogenase activity was discovered. The L-fucose pathway converts L-galactose to dihydroxyacetone phosphate and L-glyceraldehyde. Aldehyde dehydrogenase then converts L-glyceraldehyde to L-glycerate, which is toxic. Loss of the dehydrogenase averts the toxicity during growth on L-galactose, but reduces by one-half the aerobic growth yield on L-fucose. When mutant cells induced in the L-fucose system were incubated with radioactive L-fucose, accumulation of radioactivity occurred if the substrate was labeled at C-1 but not if it was labeled C-6. Complete aerobic utilization of carbons 4 through 6 of L-fucose depends not only on an adequate activity of aldehyde dehydrogenase to trap L-lactaldehyde as its anionic acid but also on the lack of L-1,2-propanediol oxidoreductase activity, which converts L-lactaldehyde to a readily excreted alcohol.

Aerobiosis↗
PubMed1987

NAD-linked aldehyde dehydrogenase for aerobic utilization of L-fucose and L-rhamnose by Escherichia coli.

Mutant analysis revealed that complete utilization of L-fucose and L-rhamnose by Escherichia coli requires the activity of a common NAD-linked aldehyde dehydrogenase which converts L-lactaldehyde to L-lactate. Mutations affecting this activity mapped to the ald locus at min 31, well apart from the fuc genes (min 60) encoding the trunk pathway for L-fucose dissimilation (as well as L-1,2-propanediol oxidoreductase) and the rha genes (min 88) encoding the trunk pathway for L-rhamnose dissimilation. Mutants that grow on L-1,2-propanediol as a carbon and energy source also depend on the ald gene product for the conversion of L-lactaldehyde to L-lactate.

Aldehyde Dehydrogenase↗
PubMed1988

A mutant crp allele that differentially activates the operons of the fuc regulon in Escherichia coli.

L-Fucose is used by Escherichia coli through an inducible pathway mediated by a fucP-encoded permease, a fucI-encoded isomerase, a fucK-encoded kinase, and a fucA-encoded aldolase. The adolase catalyzes the formation of dihydroxyacetone phosphate and L-lactaldehyde. Anaerobically, lactaldehyde is converted by a fucO-encoded oxidoreductase to L-1,2-propanediol, which is excreted. The fuc genes belong to a regulon comprising four linked operons: fucO, fucA, fucPIK, and fucR. The positive regulator encoded by fucR responds to fuculose 1-phosphate as the effector. Mutants serially selected for aerobic growth on propanediol became constitutive in fucO and fucA [fucO(Con) fucA(Con)], but noninducible in fucPIK [fucPIK(Non)]. An external suppressor mutation that restored growth on fucose caused constitutive expression of fucPIK. Results from this study indicate that this suppressor mutation occurred in crp, which encodes the cyclic AMP-binding (or receptor) protein. When the suppressor allele (crp-201) was transduced into wild-type strains, the recipient became fucose negative and fucose sensitive (with glycerol as the carbon and energy source) because of impaired expression of fucA. The fucPIK operon became hyperinducible. The growth rate on maltose was significantly reduced, but growth on L-rhamnose, D-galactose, L-arabinose, glycerol, or glycerol 3-phosphate was close to normal. Lysogenization of fuc+ crp-201 cells by a lambda bacteriophage bearing crp+ restored normal growth ability on fucose. In contrast, lysogenization of [fucO(Con)fucA(Con)fucPIK(Non)crp-201] cells by the same phage retarded their growth on fucose.

Alleles↗
PubMed1995

Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols.

A bacterial strain that can utilize several kinds of alcohols as its sole carbon and energy sources was isolated from soil and tentatively identified as Pseudomonas putida HK5. Three distinct dye-linked alcohol dehydrogenases (ADHs), each of which contained the prosthetic group pyrroloquinoline quinone (PQQ), were formed in the soluble fractions of this strain grown on different alcohols. ADH I was formed most abundantly in the cells grown on ethanol and was similar to the quinoprotein ADH reported for P. putida (H. Görisch and M. Rupp, Antonie Leeuwenhoek 56:35-45, 1989) except for its isoelectric point. The other two ADHs, ADH IIB and ADH IIG, were formed separately in the cells grown on 1-butanol and 1,2-propanediol, respectively. Both of these enzymes contained heme c in addition to PQQ and functioned as quinohemoprotein dehydrogenases. Potassium ferricyanide was an available electron acceptor for ADHs IIB and IIG but not for ADH I. The molecular weights were estimated to be 69,000 for ADH IIB and 72,000 for ADH IIG, and both enzymes were shown to be monomers. Antibodies raised against each of the purified ADHs could distinguish the ADHs from one another. Immunoblot analysis showed that ADH I was detected in cells grown on each alcohol tested, but ethanol was the most effective inducer. ADH IIB was formed in the cells grown on alcohols of medium chain length and also on 1,3-butanediol. Induction of ADH IIG was restricted to 1,2-propanediol or glycerol, of which the former alcohol was more effective. These results from immunoblot analysis correlated well with the substrate specificities of the respective enzymes. Thus, three distinct quinoprotein ADHs were shown to be synthesized by a single bacterium under different growth conditions.

1-Butanol↗
PubMed2004

Evidence that a B12-adenosyl transferase is encoded within the ethanolamine operon of Salmonella enterica.

Adenosylcobalamin (Ado-B12) is both the cofactor and inducer of ethanolamine ammonia lyase (EA-lyase), a catabolic enzyme for ethanolamine. De novo synthesis of Ado-B12 by Salmonella enterica occurs only under anaerobic conditions. Therefore, aerobic growth on ethanolamine requires import of Ado-B12 or a precursor (CN-B12 or OH-B12) that can be adenosylated internally. Several known enzymes adenosylate corrinoids. The CobA enzyme transfers adenosine from ATP to a biosynthetic intermediate in de novo B12 synthesis and to imported CN-B12, OH-B12, or Cbi (a B12 precursor). The PduO adenosyl transferase is encoded in an operon (pdu) for cobalamin-dependent propanediol degradation and is induced by propanediol. Evidence is presented here that a third transferase (EutT) is encoded within the operon for ethanolamine utilization (eut). Surprisingly, these three transferases share no apparent sequence similarity. CobA produces sufficient Ado-B12 to initiate eut operon induction and to serve as a cofactor for EA-lyase when B12 levels are high. Once the eut operon is induced, the EutT transferase supplies more Ado-B12 during the period of high demand. Another protein encoded in the operon (EutA) protects EA-lyase from inhibition by CN-B12 but does so without adenosylation of this corrinoid.

Alkyl and Aryl Transferases↗
PubMed1997

Evidence for a phloretin-sensitive glycerol transport mechanism in the perfused rat liver.

Glycerol, water, and urea transport were studied in the perfused rat liver. When hypertonic glycerol (100 mM) was infused into the perfused rat liver, rapid equilibration of glycerol between the extracellular and intracellular space occurred and only small effects of osmotic water fluxes on liver mass and extracellular ion concentrations were observed. However, when phloretin (0.2 mmol/l) was present, addition (or removal) of glycerol (100 mmol/l) induced within seconds a marked and transient decrease (or increase) of both liver mass and effluent Na+ and K+ concentrations, suggestive of transient osmotic water shifts out of and/or into the cells. These effects were observed with glycerol but not with infusion of 1,2-propanediol, 1,3-propanediol, or ethanediol (100 mmol/l). Calculation of permeability coefficients for hepatocytes in the perfused rat liver revealed that in the absence of a transmembrane glycerol concentration gradient the glycerol permeability was decreased from 0.146 +/- 0.005 (n = 14) to 0.055 +/- 0.016 microm/s (n = 4) in the presence of phloretin (200 microM). Water permeability was not affected by phloretin [0.146 +/- 0.005 under control conditions (n = 12) vs. 0.157 +/- 0.006 microm/s (n = 4) in the presence of phloretin]. Urea permeability was 0.131 +/- 0.008 microm/s (n = 5) and decreased to 0.061 +/- 0.003 microm/s in the presence ofphloretin. Glycerol and water permeability were inhibited in the presence of hypertonic glucose (200 mM) by 47 and 27%, respectively, but urea permeability was not affected by glucose.

Animals↗
PubMed1994

Use of scaling theory to relate measurements of lung endothelial barrier permeability.

This work examined the relationships between lung microvascular permeability-surface area products (PS) for small solutes in animals of different size and for columns of endothelial-covered microcarrier beads. We assembled PS data (humans, sheep, lambs, and rabbits) for labeled sucrose, mannitol, urea, 1,2-propanediol, 1,3-propanediol, and 1,4-butanediol. In addition, PS for cell columns using sucrose, mannitol, and sodium fluorescein were evaluated. A new mathematical model for the analysis of cell columns that accounts for transit time variations was derived and compared with models neglecting this variation. Allometric relationships between PS and body weight or exchange surface (S) were examined. Permeability relative to diffusivity (P/D) correlated inversely with S for all animals. In addition, P/D for the cell columns fell near this regression line. The results suggest either that permeability for hydrophilic tracers is higher for smaller animals or that the indicator-dilution measurement is a fractal process dependent on scale. Furthermore, the P/D-S correlations may help relate cell column experiments to animal studies.

Animals↗
PubMed2001

In vitro and in vivo activity of 1-O-hexadecylpropanediol-3-phospho-ganciclovir and 1-O-hexadecylpropanediol-3-phospho-penciclovir in cytomegalovirus and herpes simplex virus infections.

Human cytomegalovirus (HCMV) and herpes simplex virus (HSV) can cause a wide variety of clinical manifestations in man. Ganciclovir (GCV) is effective against HCMV infection when administered by the intravenous route and may be used orally in large doses for prophylaxis of HCMV infections in organ transplantation patients and in AIDS patients. In previous studies with acyclovir (ACV), we found that covalent attachment of an alkyl glycerol phosphate moiety greatly increased oral bioavailability and increased antiviral activity against hepatitis B virus. Adducts of ACV with alkyl propanediol phosphate were more active than the alkyl glycerol phosphate analogue in vitro in 2.2.15 cells, which constitutively produce hepatitis B virus. To see if this strategy would work for two other poorly absorbed nucleoside analogues, we synthesized 1-O-hexadecylpropanediol-3-phospho-GCV (HDP-P-GCV) and 1-O-hexadecyl-propanediol-3-phospho-penciclovir (HDP-P-PCV), and evaluated the in vitro antiviral activity, selectivity and oral antiviral activity of both compounds versus GCV or PCV in mice infected with HSV-1 or HDP-P-GCV versus murine cytomegalovirus (MCMV). HDP-P-GCV is orally active in both MCMV and HSV-1 infection in mice with antiviral activity equivalent to (HSV-1) or greater than oral GCV (MCMV). Oral HDP-P-PCV was more active than PCV orally versus intranasal HSV-1 infection in mice.

Administration, Oral↗
PubMed1996

Modification of a glassy carbon electrode with diols for the suppression of electrode fouling in biological fluids.

The surface of a glassy carbon (GC) electrode was modified covalently with ethyleneglycol, diethyleneglycol, 1,2-propanediol, and 1,3-propanediol by electrochemical oxidation in order to suppress the electrode fouling originating from non-specific adsorption of serum proteins. Human serum albumin (HSA) was adsorbed significantly on the surface of a bare GC electrode, which was monitored by cyclic voltammetry in the presence of Fe(CN)6(4)-/Fe(CN)6(3)-ions. In contrast, the diol-modified GC electrodes were scarcely fouled in HSA solution and even in human serum. The results were explained reasonably based on the hydrophilic nature of the diol-modified GC surface.

Adsorption↗