SEARCH · PubMed Health

Results for “PROPANEDIOLS”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 163 records · Page 9Linked to original sources

PubMed1989

Similarity of Escherichia coli propanediol oxidoreductase (fucO product) and an unusual alcohol dehydrogenase from Zymomonas mobilis and Saccharomyces cerevisiae.

The gene that encodes 1,2-propanediol oxidoreductase (fucO) from Escherichia coli was sequenced. The reading frame specified a protein of 383 amino acids (including the N-terminal methionine), with an aggregate molecular weight of 40,642. The induction of fucO transcription, which occurred in the presence of fucose, was confirmed by Northern blot analysis. In E. coli, the primary fucO transcript was approximately 2.1 kilobases in length. The 5' end of the transcript began more than 0.7 kilobase upstream of the fucO start codon within or beyond the fucA gene. Propanediol oxidoreductase exhibited 41.7% identity with the iron-containing alcohol dehydrogenase II from Zymomonas mobilis and 39.5% identity with ADH4 from Saccharomyces cerevisiae. These three proteins did not share homology with either short-chain or long-chain zinc-containing alcohol dehydrogenase enzymes. We propose that these three unusual alcohol dehydrogenases define a new family of enzymes.

Alcohol Oxidoreductases↗

PubMed1995

Purification of 1,3-propanediol dehydrogenase from Citrobacter freundii and cloning, sequencing, and overexpression of the corresponding gene in Escherichia coli.

1,3-Propanediol dehydrogenase (EC 1.1.1.202) was purified to homogeneity from Citrobacter freundii grown anaerobically on glycerol in continuous culture. The enzyme is an octamer of a polypeptide of 43,400 Da. When tested as a dehydrogenase, the enzyme was most active with substrates containing two primary alcohol groups separated by one or two carbon atoms. In the physiological direction, 3-hydroxypropionaldehyde was the preferred substrate. The apparent Km values of the enzyme for 3-hydroxypropionaldehyde and NADH were 140 and 33 microM, respectively. The enzyme was inhibited by chelators of divalent cations but could be reactivated by the addition of Fe2+. The dhaT gene, encoding the 1,3-propanediol dehydrogenase, was cloned, and its nucleotide sequence (1,164 bp) was determined. The deduced dhaT gene product (387 amino acids, 41,324 Da) showed a high level of similarity to a novel family (type III) of alcohol dehydrogenases. The dhaT gene was overexpressed in Escherichia coli 274-fold by using the T7 RNA polymerase/promoter system.

Alcohol Dehydrogenase↗

PubMed1996

cobB function is required for catabolism of propionate in Salmonella typhimurium LT2: evidence for existence of a substitute function for CobB within the 1,2-propanediol utilization (pdu) operon.

The cobB function of Salmonella typhimurium LT2 was defined in vivo as an alternative activity for the nicotinic acid mononucleotide:5,6-dimethylbenzimidazole phosphoribosyltransferase enzyme (CobT), which is involved in the assembly of the nucleotide loop of cobalamin in this bacterium (J. R. Trzebiatowski, G. A. O'Toole, and J. C. Escalante-Semerena, J. Bacteriol. 176:3568-3575, 1994). In this paper we document that, independent of their inability to substitute for CobT function, cobB mutants are unable to use propionate as a carbon and energy source. A plasmid carrying only a wild-type copy of cobB complemented the cobalamin biosynthesis and propionate catabolism phenotypes of cobB mutants, indicating that a lack of CobB was responsible for both phenotypes. We demonstrate the existence of a function encoded by the 1,2-propanediol utilization (pdu) operon, which when induced by 1,2-propanediol compensated for the lack of CobB during propionate catabolism but failed to compensate for CobT in the assembly of the nucleotide loop of cobalamin in a cobB cobT double mutant.

Genes, Bacterial↗

PubMed2005

Crystal structure of an iron-dependent group III dehydrogenase that interconverts L-lactaldehyde and L-1,2-propanediol in Escherichia coli.

The FucO protein, a member of the group III "iron-activated" dehydrogenases, catalyzes the interconversion between L-lactaldehyde and L-1,2-propanediol in Escherichia coli. The three-dimensional structure of FucO in a complex with NAD(+) was solved, and the presence of iron in the crystals was confirmed by X-ray fluorescence. The FucO structure presented here is the first structure for a member of the group III bacterial dehydrogenases shown experimentally to contain iron. FucO forms a dimer, in which each monomer folds into an alpha/beta dinucleotide-binding N-terminal domain and an all-alpha-helix C-terminal domain that are separated by a deep cleft. The dimer is formed by the swapping (between monomers) of the first chain of the beta-sheet. The binding site for Fe(2+) is located at the face of the cleft formed by the C-terminal domain, where the metal ion is tetrahedrally coordinated by three histidine residues (His200, His263, and His277) and an aspartate residue (Asp196). The glycine-rich turn formed by residues 96 to 98 and the following alpha-helix is part of the NAD(+) recognition locus common in dehydrogenases. Site-directed mutagenesis and enzyme kinetic assays were performed to assess the role of different residues in metal, cofactor, and substrate binding. In contrast to previous assumptions, the essential His267 residue does not interact with the metal ion. Asp39 appears to be the key residue for discriminating against NADP(+). Modeling L-1,2-propanediol in the active center resulted in a close approach of the C-1 hydroxyl of the substrate to C-4 of the nicotinamide ring, implying that there is a typical metal-dependent dehydrogenation catalytic mechanism.

Aldehydes↗

PubMed1984

Counteractive effects of propionate or 1,2-propanediol against hypoglycemia and ketonemia of tributyrin-treated cows.

We administered tributyrin (500 ml), tributyrin (500 ml) plus magnesium propionate (400 g), tributyrin (500 ml) plus sodium propionate (400 g), or tributyrin (500 ml) plus 1,2-propanediol (400 ml) as a single dose into rumens of lactating cows and then measured in blood the plasma concentrations of glucose, acetoacetate, 3-hydroxybutyrate, free fatty acids, and insulin as a function of time. Tributyrin administration caused hypoglycemia and hyperketonemia similar to the ketotic condition in less than 3 h and was a negative correlation of --.88 between glucose and ketone concentrations in blood plasma. Administration of either magnesium propionate, sodium propionate, or 1,2-propanediol could counteract the hypoglycemia and hyperketonemia induced by tributyrin administration without significantly changing the insulin response. Of the two propionate compounds, magnesium propionate was more effective than sodium propionate for alleviating hypoglycemia and hyperketonemia.

3-Hydroxybutyric Acid↗

PubMed1976

The influence of propanediol-1,3 on the development of the legs, wings and lower beak of the chick embryo.

In seven series of 31-34 chick embryos each, the influence of the position of the egg during incubation and of the administration of 0.05 ml propanediol-1,3 on the 5th day of incubation on the development and growth of the limbs and beak were studied. Isotonic saline injected embryos served as controls. The embryos were sacrificed at the age of 15 days. Incubation of the egg in a vertical position, with the air chamber pointing upward, proved to result in a slight, through significant reduction in the length of the limbs and beak. Propanediol was highly toxic if injected in the immediate vicinity of the embryo. If injected at some distance from the embryo, either into the air chamber or into the yolk, the agent proved to be teratogenic: measurements showed a considerable retardation of the longitudinal growth of the limbs and beak, the latter being a parrot beak in 60 per cent of the cases, whereas both the tibia and the metatarsals were, moreover, bent posteriorward. Histological studies of the tibia showed an underdevelopment of the periosteal bone collar and, at the angle of the bone, a replacement of the posterior part of this collar by endochondral bone trabeculae. The abnormalities observed are dissimilar to those demonstrated in hereditary congenital chondrodystrophy and in micromelic conditions induced by insulin or sulfonamides.

Animals↗

PubMed2000

Conformational features of reduced and disulfide intact forms of hen egg white lysozyme in aqueous solution in presence of 3-chloro-1, 2-propanediol and dioxane: implications for protein folding intermediates.

Conformational features of reduced and disulfide intact hen egg white lysozyme in aqueous 1,4-dioxane and 3-chloro-1, 2-propanediol solutions have been examined using circular dichroism and fluorescence spectroscopy. We find that in presence of 1, 4-dioxane, reduced lysozyme assumes a relatively compact conformational form with secondary structure closer to native state and no tertiary structure as judged by peptide and aromatic CD spectra and ANS binding studies monitored by fluorescence. Further, in presence of 40% (v/v) 3-chloro-1, 2-propanediol, disulfide intact lysozyme (DI-lysozyme) assumes a conformational form with native like secondary structure and no tertiary structure akin to a molten globule state. We correlate our results to kinetic hydrogen- deuterium exchange NMR results of the refolding of lysozyme available in literature and suggest that the conformational forms observed in our study could be models for kinetic intermediates in the refolding of lysozyme.

Animals↗

PubMed1988

[Enhancement of the combination of F-actin and alpha-actinin association in the presence of 1,2-propanediol].

The influence of 1,2-propanediol on the G-actin/F-actin equilibrium has been studied previously. We report here its effect on the crosslinking of actin filaments by alpha-actinin. Capillary viscometry experiments indicate a marked increase in the viscosity of F-actin/alpha-actinin solutions in the presence of this solvent, with a rise of the gel point temperature. Gel electrophoresis obtained after high-speed sedimentation of these proteins showed an enhancement of the alpha-actinin/actin filaments association. Propanediol-induced perturbations of interactions between microfilaments and actin-binding proteins might help explain the variability of its cryoprotective efficiency for the preservation of various cells.

Actinin↗

PubMed1987

The measurement of 1,2-propanediol, D, L-2,3-butanediol and meso-2,3-butanediol in controls and alcoholic cirrhotics.

Plasma 1,2-propanediol, D,L,-2,3-butanediol and 2,3-meso-butanediol were measured in 29 patients with biopsy proven alcoholic cirrhosis and 10 control subjects, none of whom had measurable blood alcohol levels. None of these compounds were present in control subjects at level above 5 nmol/ml. Seventeen (59%) of 29 serum samples drawn from patients with alcoholic cirrhosis contained 1,2-propanediol in concentrations above 5 nmol/ml (range less than 5.0 nmol/ml-35.4 nmol/ml, median 5.6), 8 (28%) of 29 samples contained D,L-2,3-butanediol in concentrations above 5.0 nmol/ml (range less than 5.0 nmol/ml-211 nmol/ml) and 7 (25%) of 29 samples contained meso-2,3-butanediol in concentrations above 5.0 nmol/ml (range less than 5.0-63.4 nmol/ml). In alcohol abstinent patients with alcoholic cirrhosis elevated serum 2,3-butanediol is due neither to ingestion of diols from undistilled alcoholic beverages nor is it likely to arise directly from the metabolic products of ethanol. In future studies on the origin of 2,3-butanediol in alcoholic patients biopsy evidence of the degree of associated liver damage should be obtained.

Alcoholism↗

PubMed1983

[Biochemical indices of erythrocytes cryopreserved with protection by 1,2-propanediol and glycerin].

Based on the data concerning the content of ATP, 2,3-DFG, K+, and Na+ in depreserved red cells stored at 4 degrees C in resuspending media TsNIIGPK 8b and 8v it has been established that blood preserved under protection of 1,2-propanediol is comparable with that preserved under glycerin protection as regards its quality and is even better from the standpoint of some other indicators. Medium TsNIIGPK 8v may be used as resuspending medium for blood exposed to low temperature preservation under protection of 1,2-propanediol.

Adenosine Triphosphate↗

PubMed1980

[On the biosynthesis of glyceride- and phosphoglyceride analogues from monoglyceride analogue 2-(linoleoylamino)-1,3-propanediol in rats (author's transl)].

From L-serine 2-(linoleoylamino)-1,3-propanediol, a monoglyceride analogue, was synthesized and characterized by thin-layer and gas chromatography, infra red spectroscopy and mass spectrometry. After oral application to rats there was an accumulation, almost exclusively in the liver, of triglyceride, diglyceride, phosphatidylcholine and phosphatidylethanolamine analogues with amide-bound linoleic acid. Small amounts of triglyceride analogues could also be detected in the adipose tissue. The analogues were chromatographically isolated using in addition enzymatic and non-enzymatic hydrolysis procedures. Results disclosed that the amide-bound fatty acid of 2-(linoleoylamino)-1,3-propanediol can be absorbed and metabolized intact. Phosphoglyceride analogues are probably formed by the CDP-choline and CDP-ethanolamine pathway fromdiglyceride analogues. Phosphatidylcholine and its analogues disclosed a similar composition of the 1-O-acyl fatty acids. Apparently analogues have in vivo similar substrate properties to hydrolases and acyltransferases as their natural counterparts.

Animals↗

PubMed1994

Metal-catalyzed oxidation of Fe2+ dehydrogenases. Consensus target sequence between propanediol oxidoreductase of Escherichia coli and alcohol dehydrogenase II of Zymomonas mobilis.

We have studied two enzymes of a newly described family of dehydrogenases with high sequence homology, 1,2-propanediol oxidoreductase of Escherichia coli and alcohol dehydrogenase II of Zymomonas mobilis. These enzymes perform their metabolic role under anaerobic conditions; in the presence of oxygen, they show a very similar inactivation pattern by a metal-catalyzed oxidation system. Titration of histidine residues with diethyl pyrocarbonate showed one histidine residue less in the oxidized enzymes. Comparison of subtilisin peptide maps of active and inactivated enzymes showed a difference in one histidine-containing peptide, the sequence of which is YNTPH277GVAN for propanediol oxidoreductase and YNLPH277GV for alcohol dehydrogenase II. This histidine residue lies 10 residues away from a proposed metal-binding site, H263XXXH267, necessary to explain a site-specific free radical mechanism. The three histidine residues here described are strictly conserved in all enzymes of this family. In this report we propose that histidine 277 is a target for oxidation by a metal-catalyzed oxidation system and that this modification leads to the irreversible inactivation of both enzymes.

Alcohol Dehydrogenase↗

PubMed1997

Effects of glycerol-1,2-dimethylsuccinate and propanediol-1,2-dimethylsuccinate on insulin release and protein biosynthesis in islets of Goto-Kakizaki rats.

Selected esters of succinic acid are currently under investigation as possible insulinotropic tools in the treatment of non-insulin-dependent diabetes mellitus. Novel esters with high insulinotropic efficiency were recently synthesized. The present study concerns the effects of two of these novel esters, namely glycerol-1,2-dimethylsuccinate (2.5 mM) and propanediol-1,2-dimethylsuccinate (1.0 mM), upon the release of insulin and the de novo biosynthesis of peptides in islets from hereditarily diabetic Goto-Kakizaki rats. Whereas D-glucose (2.8 to 16.7 mM) caused a concentration-related stimulation of insulin release in the islets of the diabetic rats, the two esters of succinic acid only increased modestly, and often not significantly, insulin secretion. Nevertheless, they both markedly increased the incorporation of L-[4-3H]phenylalanine into trichloroacetic acid-precipitable material in islets deprived of any other exogenous nutrient. These findings indicate that, at variance with all pharmaceutical agents presently used or proposed as insulin secretagogues in the treatment of type 2 diabetes, glycerol-1,2-dimethylsuccinate and propanediol-1,2-dimethylsuccinate, considered as islet cell nutrients, display, in addition to their insulinotropic action, the property of stimulating biosynthetic activity in the endocrine pancreas of animals affected by this disease.

Animals↗

PubMed2006

Coupling of enantioselective biooxidation of DL-1,2-propanediol and bioreduction of pinacolone via regeneration cycle of coenzyme.

Enantioselective biotransformation of DL-1,2-propanediol to D-2-hydroxypropanic acid was first reported by the authors. In the biooxidation process, there were some by-product formed and thus influenced the e.e. value and output of the acid. Restricting oxygen in the reaction system and offering additional proton receptor to the system displayed approving effect. The latter method constructed regeneration cycle system of coenzyme. In the article, the bioreduction of pinacolone was coupled to the enantioselective oxidation. Yield of the acid was increased by 36% and e.e. value of the product approached 99%.

Biotransformation↗

PubMed2003

Protein content of polyhedral organelles involved in coenzyme B12-dependent degradation of 1,2-propanediol in Salmonella enterica serovar Typhimurium LT2.

Salmonella enterica forms polyhedral organelles during coenzyme B(12)-dependent growth on 1,2-propanediol (1,2-PD). Previously, these organelles were shown to consist of a protein shell partly composed of the PduA protein, the majority of the cell's B(12)-dependent diol dehydratase, and additional unidentified proteins. In this report, the polyhedral organelles involved in B(12)-dependent 1,2-PD degradation by S. enterica were purified by a combination of detergent extraction and differential and density gradient centrifugation. The course of the purification was monitored by electron microscopy and gel electrophoresis, as well as enzymatic assay of B(12)-dependent diol dehydratase. Following one- and two-dimensional gel electrophoresis of purified organelles, the identities and relative abundance of their constituent proteins were determined by N-terminal sequencing, protein mass fingerprinting, Western blotting, and densitometry. These analyses indicated that the organelles consisted of at least 15 proteins, including PduABB'CDEGHJKOPTU and one unidentified protein. Seven of the proteins identified (PduABB'JKTU) have some sequence similarity to the shell proteins of carboxysomes (a polyhedral organelle involved in autotrophic CO(2) fixation), suggesting that the S. enterica organelles and carboxysomes have a related multiprotein shell. In addition, S. enterica organelles contained four enzymes: B(12)-dependent diol dehydratase, its putative reactivating factor, aldehyde dehydrogenase, and ATP cob(I)alamin adenosyltransferase. This complement of enzymes indicates that the primary catalytic function of the S. enterica organelles is the conversion of 1,2-PD to propionyl coenzyme A (which is consistent with our prior proposal that the S. enterica organelles function to minimize aldehyde toxicity during growth on 1,2-PD). The possibility that similar protein-bound organelles may be more widespread in nature than currently recognized is discussed.

Amino Acid Sequence↗

PubMed1999

Surface characterization, protein adsorption, and initial cell-surface reactions on glutathione and 3-mercapto-1,2,-propanediol immobilized to gold.

Monolayers of glutathione (GSH) and 3-mercapto-1,2-propanediol (MG) on gold were tested for their bioreactivity by assessing the degree of inflammatory reaction as manifested by the adherence and activation of platelets and white blood cells (wbc) after exposure to blood ex vivo. Surface composition was characterized by XPS, and noncontact optical profilometry was used to determine surface roughness. The thickness and composition of the adsorbed protein layers were measured by ellipsometry/antibody techniques in vitro. Cell adhesion and activation were quantified by acridine orange staining, fluorescein-diacetate staining, and by specific antibodies against cell membrane antigens. Distinct differences among the surfaces were observed relative to the amounts and composition of adsorbed plasma proteins and the adhesion and activation of platelets (CD62P-exposure) and wbc (CD11b/CD18-exposure). GSH surfaces, which adsorbed the least amount of plasma protein, caused the least adherence and activation of platelets (CD62P), followed by the highest activation of wbc (CD11b/18). The MG surfaces caused a rapid recruitment and activation of platelets (CD62P), followed by a lower activation of wbc (CD11b/18). Thus it appears that measurements of the initial adsorption of plasma protein from anticoagulated plasma and of the adhesion and activation of platelets after 8 min of exposure to whole blood cannot be used to predict accurately the adhesion and activation behavior of inflammatory cells after longer periods (2 h) of exposure on different surfaces.

Adsorption↗

PubMed1989

Parthenogenetic activation of unfertilized mouse oocytes by exposure to 1,2-propanediol is influenced by temperature, oocyte age, and cumulus removal.

Cumulus-intact and -denuded unfertilized oocytes from two mouse strains were exposed to 1.5 M ethanol (EtOH) or two cryoprotectant solutions, 1.5 M propanediol (PROH) or 1.5 M dimethylsulfoxide (DMSO), for 4.5 min at 27 degrees C, and the proportion of activating or degenerating oocytes studied. Exposure to DMSO did not significantly increase activation above that of oocytes not exposed to DMSO. Treatment of oocytes in PROH resulted in the activation of up to 87% of viable oocytes. This was significantly higher (P less than .01) than in control oocytes and comparable to the rate of activation after treatment with EtOH (59-96% activation). In solutions at 1 degree C, 47% of control oocytes were activated, which was not significantly different from the rate of activation in EtOH (36%) or PROH (50%) at 1 degree C. Following treatment with PROH, up to 87% of oocytes degenerated within a period of 6 h in vitro. The age of the oocytes (h post hCG) and the time of cumulus removal with the enzyme hyaluronidase, relative to the time of exposure to the chemicals, influenced the level of degeneration in most groups. Significantly fewer oocytes degenerated when cumulus cells were removed before treatment (0-31%) than when the cumulus was left intact throughout the treatment and 6 h culture period (10-87%). Exposure to PROH at 1 degree C reduced oocyte degeneration to 5%. We conclude that PROH causes significantly greater losses of oocytes as a result of parthenogenetic activation and degeneration than of exposure to DMSO.

Animals↗

PubMed1994

Human corneal endothelial tolerance to glycerol, dimethylsulfoxide, 1,2-propanediol, and 2,3-butanediol.

We exposed human corneas to various concentrations of four cryoprotectants by one of two methods: a gradual increase to the final concentration (ramp method) and a series of steps to the final concentration (step method). Endothelial damage was manifest as a decrease in the number of endothelial cells per unit area. The highest concentrations that did not cause a loss of endothelial cells by the ramp and step methods, respectively, were 4.3 and 2.0 M glycerol, 2.0 and 4.3 M dimethylsulfoxide, 2.0 and 3.0 M 1,2-propanediol, and 2.0 and 2.5 M 2,3-butanediol. The ramp method achieved higher final concentrations with the more slowly permeating glycerol, but required low toxicity. The step method achieved higher final concentrations with the more toxic cryoprotectants by limiting the exposure time, but required more rapid permeation. None of the four cryoprotectants was tolerated at concentrations sufficient for vitrification at practical cooling and warming rates.

Adolescent↗