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PubMed1979

Pathways of energy metabolism required for phenotypic expression of nif+Kp genes in Escherichia coli.

In E. coli K12 (F'nif+Kp) hybrids, electron-transport-dependent phosphorylation is not necessary for anaerobic nitrogen fixation, and substrate level phosphorylation can provide sufficient ATP from glucose for nitrogenase activity. The fumarate-reduction system, however, is essential in these hybrids for the transfer of electrons to nitrogenase. This system is probably also involved in maintaining the membrane in the energized state, thereby allowing nitrogen fixation to occur. The nitrate-reduction system, which can energize the membrane like the fumarate-reduction system, is not necessary for nitrogenase activity in the E. coli K12(F'nif+Kp) hybrids. However, two nitrate reductase genes, chlA, and chlB, are essential for inhibition of nitrogen fixation by nitrate. Moreover, nitrate inhibits nitrogenase activity and this inhibition is most probably effected through a regulator factor coded by chlA and chlB.

Adenosine Triphosphate↗
PubMed1987

Reaction of argininosuccinase with bromomesaconic acid: role of an essential lysine in the active site.

We have undertaken studies on bovine liver argininosuccinase (L-argininosuccinate arginine-lyase, EC 4.3.2.1) with the active site-directed reagent bromo[U-14C]mesaconic acid, an analogue of fumaric acid. Reactivity, measured by enzyme inactivation, followed pseudo-first-order kinetics, and the rate increased with reagent concentration. Argininosuccinate completely protected the enzyme against inactivation, but neither arginine nor fumarate was protective. A plot of the degree of inactivation as a function of alkyl groups incorporated was extrapolated to 4 mol per mol of enzyme, or 1 mol per active site. After large-scale alkylation of the enzyme (and digestion with trypsin), two 14C-labeled tryptic peptides were isolated. These were chemically sequenced by the Edman method. The amino acid sequences proved to be identical with regions of the deduced amino acid sequences or argininosuccinases from human and yeast sources [O'Brien, W. E., McInnes, R., Kalumuck, K. & Adcock, M. (1986) Proc. Natl. Acad. Sci. USA 83, 7211-7215; Beacham, I. R., Schweitzer, B. W., Warrick, H. M. & Carbon, J. (1984) Gene 29, 271-279]. The 14C-labeled tryptic peptide in the active site region had the sequence Gly-Leu-Glu-Xaa-Ala-Gly-Leu-Leu-Thr-Lys; Xaa represents an unknown phenylthiohydantoin derivative detected in cycle 4. The corresponding amino acid was identified as lysine-51 on the basis of sequence similarity with human and yeast amino acid sequences in this region. The reaction of the enzyme with the alkylating agent and the specific protection against inactivation by argininosuccinate suggest that this lysine residue has an essential role in the binding of argininosuccinate to the enzyme and, consequently, is essential for catalysis.

Amino Acid Sequence↗
PubMedDate not supplied

A novel apparatus for the determination of solubility in pressurized metered dose inhalers.

The accurate solubility of salbutamol sulfate, budesonide, and formoterol fumarate dihydrate in hydrofluoroalkane propellant 134a at 25 degrees C for 24 h, are reported. The authors describe a novel reusable in-line pressurized solubility apparatus containing an integral filter holder and a continuous decrimpable valve for the determination of drug/excipients solubility in pressurized metered dose inhalers. The solubility was determined by high-performance liquid chromatography. Solubility of salbutamol sulfate was determined as being below the detection limits while budesonide and formoterol fumarate dihydrate solubility were 23.136 +/- 2.951 microg x g(-1) and 0.776 +/- 1.023 microg x g(-1), respectively (n = 3). This novel solubility apparatus offers an improved ease of use and potential higher analytical throughput.

Administration, Inhalation↗
PubMed1997

Retention and utilization of amino acids in piglets fed ad libitum or restrictively diets supplemented with organic acids.

In a metabolic trial 4 groups of 8 piglets of 5 kg weight each were kept individually for 45 days (final weight 23 kg) and fed a practical diet. At the beginning of the experiment the body amino acid contents of an additional group of 8 piglets were determined by carcass analysis, and at the end of the experiment the body amino acid contents of the 4 test group piglets (A = control fed ad libitum, B and C = supplement of 1.5% fumaric acid fed ad libitum or restrictively, D = supplement of 1.5% citric acid fed ad libitum) were also analysed. The amino acid retention during the experimental period was determined by difference. The supplements of fumaric or citric acid did not influence the amount of the amino acid retention. The quotient of amino acid retention to amino acid consumed or the "productive amino acid value" was calculated and the maintenance requirements of essential amino acids for piglets were used to estimate the productive amino acid value for both retention and maintenance. The mean amino acid retention amounted to about 56 g/d, i.e. 3.49 g/kg W0.75.d of essential amino acids. The essential amino acid requirements for maintenance was 2.0 g, i.e. 0.29 g/kg W0.75.d, showing a variation of 4% (Leu) to 20% (Met+Cys) when related to the amount of the corresponding amino acid retention. With regard to the amino acid pattern for retention of the nutritionally most important amino acids, the following ratios were found: Lys, 100 (6.27 g/16 g N): Met+Cys, 48 (3.03 g): Thr, 56 (3.49 g): Trp, 13 (0.80 g). The productive amino acid values ranged from 40% (Trp), 55% (Thr), 66% (Met) to 80% (Lys). Under the conditions investigated, neither the supplements of organic acids nor the feed restriction influenced the amino acid utilization.

Amino Acids↗
PubMed2003

Film coated pellets containing verapamil hydrochloride: enhanced dissolution into neutral medium.

Weakly basic drugs, such as verapamil hydrochloride, that are poorly soluble in neutral/alkaline medium may have poor oral bioavailability due to reduced solubility in the small intestine and colon. Film coated pellets were prepared using two strategies to enhance drug release at high pH values. Firstly, pellets were coated with Eudragit RS/hydroxypropyl methylcellulose acetate succinate (HMAS) mixtures in proportions of 10:1 and 10:3, respectively. The enteric polymer, HMAS, would dissolve in medium at pH > 6 creating pores through the insoluble Eudragit RS membrane to increase drug release. Secondly, an acidic environment was created within the core by the inclusion of fumaric acid at concentrations of 5 and 10% in order to increase drug solubility. Both strategies enhanced drug release into neutral medium in dissolution studies using the pH change method to simulate GIT transit. Dissolution profiles of samples tested in pH 1.2 for 12 hr were compared with those using the pH change method (pH 1.2 for first 1.5 hr, pH raised to 6.8 for remaining 10.5 hr) using the area under the dissolution curve (AUC), the dissolution half-life (t50%), and the amount of drug released in 3 hr (A3hr) values. Both strategies enhanced drug release into neutral medium although the strategy using HMAS in the film was more effective. The formulation least affected by pH change was a combination of the two strategies, i.e., pellets containing 5% fumaric acid coated with Eudragit RS 12% w/w and HMAS 1.2% w/w.

Acrylic Resins↗
PubMed1990

Enzyme electrophoresis as an alternative method for separating the sympatric Leishmania vectors Phlebotomus papatasi and Phlebotomus langeroni (Diptera: Psychodidae).

Trials were conducted to determine the accuracy of separating the sympatric sand fly species Phlebotomus papatasi (Scopoli) and P. langeroni Nitzulescu by means of cellulose acetate enzyme electrophoresis. Malic enzyme, phosphoglucomutase, 6-phosphogluconate dehydrogenase, and fumarate hydratase were each evaluated in laboratory-reared and field-collected populations of the two species. Each of the four enzyme-based identifications was highly sensitive (greater than 97%) and specific (greater than 93%). Identifications based upon fumarate hydratase were in perfect agreement with morphological identifications, and evidence was obtained which indicates that this enzyme may be the most stable of the four enzymes tested. The application of enzyme-based vector identification is discussed in relation to classical and novel survey procedures for Leishmania promastigote detection in sand flies.

Animals↗
PubMed1990

Transport of tri- and dicarboxylic acids across the intestinal brush border membrane of calves.

Transport of tri- and dicarboxylic acids across the intestinal brush border membrane was investigated using citrate and fumarate as transport substrates. The experiments were performed with brush border membrane vesicles isolated from calf proximal jejunum. Citrate and fumarate uptake by the brush border membrane vesicles occurred by a common Na(+)-dependent transport mechanism that appears to be specific for tri- and dicarboxylates. The protonated forms of citrate (citrate-(1) and citrate-(2] seem to be much better transported than the trivalent form, as indicated by the strong stimulation of citrate uptake at an extravesicular pH of 5.6 compared to that at pH 7.8. Furthermore, citrate transport across the intestinal brush border membrane appears to be mediated by an electroneutral process.

Animals↗
PubMed1978

Mechanisms of desorption and adsorption of liver cytosolic fumarase to cellular membranous components.

The cytosolic fumarase [EC 4.2.1.2[ of rat liver was bound, after dialysis, to the microsomal membrane in vitro. Binding of the enzyme was dependent on pH, and was facilitated in the pH range below 7.5. The binding reaction was completely inhibited by 0.5 mM fumarate, aurintricarboxylate or colchicine. The bound fumarase was released from the membrane by the substrates, isocitrate, citrate or 2,3-diphosphoglycerate at low concentrations. Desorption of the enzyme by metabolites was also dependent on pH, and was more rapid in the alkaline pH range. The enzyme desorption curves were sigmoidal, and kinetic studies suggested a biphasic cooperative mechanism for the action of the metabolites. The apparent desorption constants (concentrations necessary for 50% desorption of the enzyme) estimated at pH 7.3 for isocitrate, 2,3-diphosphoglycerate, L-malate, oxalacetate, fumarate, citrate, succinate, and KCl were 0.073, 0.074, 0.22, 0.39, 0.56, 2.9, and 19 mM, respectively. The bound fumarase showed little enzymatic activity, and its Km and Vmax values were fivefold and 31%, respectively, of those of the free enzyme.

Adsorption↗
PubMed1978

Hydrogen-dependent growth of Escherichia coli in anaerobic respiration and the presence of hydrogenases with different functions.

E. coli K10 was found to grow anaerobically on molecular hydrogen by reducing nitrate, fumarate, and trimethylamine N-oxide when peptone was added to the culture medium. Molar growth yields based on consumed hydrogen estimated from the amounts of reduction products were all 7.8 g cells/mol, suggesting that 1 mol of ATP was produced in the oxidation of 1 mol of hydrogen. Hydrogenase activity measured in terms of hydrogen evolution was several times higher in cells grown on glucose than in cells grown on hydrogen in the presence of fumarate and trimethylamine N-oxide, while hydrogenase activity measured in terms of hydrogen uptake was unchanged in both cases. The ratio of hydrogenase activities measured in terms of hydrogen uptake and evolution was also high in the extract and centrifugal fractions from cells grown in hydrogen. The soluble fraction and trypsin digest of the precipitate at 100,000 X g were subjected to polyacrylamide disc gel electrophoresis and hydrogenase bands were stained by reduction of benzyl viologen with hydrogen and by oxidation of reduced methyl viologen. The resulting patterns suggest that multiple forms of hydrogenase are present and that the amounts of forms functioning in hydrogen evolution were greatly decresed in cells grown on hydrogen in the presence of acceptors.

Anaerobiosis↗
PubMed2005

The effects of various organic acids on phytate phosphorus utilization in chicks.

Previous research from our laboratory has shown that citric acid improves phytate P utilization in chicks fed a P-deficient corn-soybean meal diet. The current study was conducted to determine if other organic acids also are effective, with an emphasis on gluconic acid. Four experiments were conducted in which 4 replicate groups of 5 crossbred chicks (New Hampshire x Columbian) were fed a P-deficient diet (0.16% nonphyate P) from 8 to 22 d of age. In Experiment 1, chick weight gain and tibia ash were significantly increased (P < 0.05) by 1.5 and 3% sodium gluconate (NaGlu), 1.5% calcium gluconate (CaGlu), 1.5 and 3% glucono-delta-lactone, and 1% 2-hydroxy-4-methylthio butanoic acid (Alimet). In experiment 2, tibia ash was significantly increased (P < 0.05) by 2% NaGlu, CaGlu, and citric acid in chicks fed the P-deficient diet but not in chicks fed a 0.45% nonphytate P diet, indicating that the organic acid responses were due to increased P utilization. In experiments 3 and 4, tibia ash was significantly increased by 3% NaGlu and 3% citric acid, but not by 3% fumaric acid or 0.025, 0.05 and 0.1% EDTA. The results of this study showed that NaGlu, CaGlu, glucono-delta-lactone, Alimet, and citric acid, but not fumaric acid or EDTA, improved phytate P utilization in chicks fed a corn-soybean meal diet.

Animals↗
PubMed2000

Cerebral metabolism of lactate in vivo: evidence for neuronal pyruvate carboxylation.

The cerebral metabolism of lactate was investigated. Awake mice received [3-13C]lactate or [1-13C]glucose intravenously, and brain and blood extracts were analyzed by 13C nuclear magnetic resonance spectroscopy. The cerebral uptake and metabolism of [3-13C]lactate was 50% that of [1-13C]glucose. [3-13C]Lactate was almost exclusively metabolized by neurons and hardly at all by glia, as revealed by the 13C labeling of glutamate, gamma-aminobutyric acid and glutamine. Injection of [3-13C]lactate led to extensive formation of [2-13C]lactate, which was not seen with [1-13C]glucose, nor has it been seen in previous studies with [2-13C]acetate. This formation probably reflected reversible carboxylation of [3-13C]pyruvate to malate and equilibration with fumarate, because inhibition of succinate dehydrogenase with nitropropionic acid did not block it. Of the [3-13C]lactate that reached the brain, 20% underwent this reaction, which probably involved neuronal mitochondrial malic enzyme. The activities of mitochondrial malic enzyme, fumarase, and lactate dehydrogenase were high enough to account for the formation of [2-13C]lactate in neurons. Neuronal pyruvate carboxylation was confirmed by the higher specific activity of glutamate than of glutamine after intrastriatal injection of [1-14C]pyruvate into anesthetized mice. This procedure also demonstrated equilibration of malate, formed through pyruvate carboxylation, with fumarate. The demonstration of neuronal pyruvate carboxylation demands reconsideration of the metabolic interrelationship between neurons and glia.

Animals↗
PubMed2000

Denitrovibrio acetiphilus, a novel genus and species of dissimilatory nitrate-reducing bacterium isolated from an oil reservoir model column.

A novel dissimilatory, nitrate-reducing bacterium, designated strain N2460T, was isolated from an oil reservoir model column. Strain N2460T is a mesophilic, obligately anaerobic, marine, gram-negative bacterium. The cells are vibrio-shaped and motile by a bipolar flagellum. Strain N2460T reduces nitrate to ammonia in a mineral medium supplied by acetate. The presence of a 2-oxoglutarate dehydrogenase activity indicates that acetate is oxidized via the citric acid cycle. No growth is obtained on formate, higher fatty acids, malate, fumarate, benzoate, alcohols, sugar, yeast extract, crude oil, alkanes, proline, hydrogen, sulfur or thiosulfate with nitrate as electron acceptor. Oxygen, sulfate, thiosulfate and sulfur are not utilized as alternative electron acceptors. Strain N2460T grows fermentatively on fumarate, but not on pyruvate. The G+C content of the DNA is 42.6 mol%. 16S rRNA gene analysis shows that strain N2460T belongs to the Bacteria and that the closest relative is 'Geovibrio ferrireducens' (sequence similarity 86.9%). On the basis of phylogenetic as well as phenotypic data, it is proposed that strain N2460T represents the type strain of a new genus and species, Denitrovibrio acetiphilus gen. nov., sp. nov.

Acetates↗
PubMed1982

Growth of Streptococcus faecalis var. zymogenes on glycerol: the effect of aerobic and anaerobic growth in the presence and absence of haematin on enzyme synthesis.

Streptococcus faecalis var. zymogenes was grown aerobically and anaerobically in the presence and absence of haematin, with glycerol as the carbon and energy source. Aerobic growth was stimulated by the inclusion of haematin in the medium but fumarate had no effect on growth. The bacterium was unable to grow anaerobically on glycerol unless fumarate was present; haematin had no effect on growth. NADH oxidase activity, which catalysed the oxidation of NADH + H+ to form H2O rather than H2O2, was found in the soluble fraction and was induced by aerobic growth but partially repressed when haematin was present in the medium. In contrast, a particulate NADH oxidase, which was sensitive to inhibition by antimycin A and 2-heptyl-4-hydroxyquinoline N-oxide, was induced by aerobic growth in the presence of haematin. NADH peroxidase was massively induced by aerobic growth, whereas more lactate dehydrogenase activity was found in anaerobically grown bacteria. Catalase was formed only during aerobic growth in the presence of haematin.

Aerobiosis↗
PubMed1991

Cloning, sequencing, and mutational analysis of the Bradyrhizobium japonicum fumC-like gene: evidence for the existence of two different fumarases.

The Bradyrhizobium japonicum fumarase gene (fumC-like) was cloned and sequenced, and a fumC deletion mutant was constructed. This mutant had a Nod+ Fix+ phenotype in symbiosis with the host plant, soybean, and growth in minimal medium with fumarate as sole carbon source was also not affected. The cloned B. japonicum fumC gene fully complemented an Escherichia coli Fum- mutant, strain JH400, for growth in minimal medium with fumarate. The predicted amino acid sequence of the FumC protein showed strong similarity to the E. coli FumC protein, Bacillus subtilis CitG protein, Saccharomyces cerevisiae Fum1 protein, and the mammalian fumarases. The B. japonicum FumC protein accounted for about 40% of the total fumarase activity in aerobically grown cells. The remaining 60% was ascribed to a temperature-labile fumarase. These data suggest that B. japonicum possesses two different fumarase isoenzymes, one of which is encoded by fumC. Besides E. coli, which has three fumarases, B. japonicum is thus the second bacterium for which there is genetic evidence for the existence of more than one fumarase.

Amino Acid Sequence↗
PubMed1975

Keto acid metabolism in Desulfovibrio.

Four strains of Desulfovibrio each excreted pyruvate to a constant level during growth; it was re-absorbed when the substrate (lactate) was exhausted. Malate, succinate, fumarate and malonate also accumulated during growth. One of the strains (Hildenborough) excreted alpha-ketoglutarate as well as pyruvate when incubated in nitrogen-free medium; the former was re-absorbed on addition of NH4Cl. In a low-lactate nitrogen-free medium, strain Hildenborough rapidly re-absorbed the pyruvate initially excreted, but did not re-absorb the alpha-ketoglutarate. Arsenite (I mM) prevented the accumulation of alpha-ketoglutarate; I mM-malonate did not affect the accumulation of keto acids. Isocitrate dehydrogenase activity (NAD-specific) in all strains was lower than NADP-specific glutamate dehydrogenase activity. Alpha-Ketoglutarate dehydrogenase could not be detected in any strain. NADPH oxidase activity was demonstrated. This and previous work indicate that a tricarboxylic acid pathway from citrate to alpha-ketoglutarate exists in Desulfovibrio spp., and that succinate can be synthesized via malate and fumarate; however, an intact tricarboxylic acid cycle is evidently not present. The findings are compared with observations on biosynthetic pathways in clostridia, obligate lithotrophs, phototrophs, and methylotrophs, and various facultative bacteria.

Aconitate Hydratase↗
PubMed2004

Shewanella profunda sp. nov., isolated from deep marine sediment of the Nankai Trough.

A novel piezotolerant, mesophilic, facultatively anaerobic, organotrophic, polarly flagellated bacterium (strain LT13a(T)) was isolated from a deep sediment layer in the Nankai Trough (Leg 190, Ocean Drilling Program) off the coast of Japan. This organism used a wide range of organic substrates as sole carbon and energy sources: pyruvate, glutamate, succinate, fumarate, lactate, citrate, peptone and tryptone. Oxygen, nitrate, fumarate, ferric iron and cystine were used as electron acceptors. Maximal growth rates were observed at a hydrostatic pressure of 10 MPa. Hydrostatic pressure for growth was in the range 0.1-50 MPa. Predominant cellular fatty acids were 16 : 1omega7c, 15 : 0 iso, 16 : 0 and 13 : 0 iso. The G+C content of the DNA was 44.9 mol%. On the basis of 16S rRNA gene sequences, strain LT13a(T) was shown to belong to the gamma-Proteobacteria, being closely related to Shewanella putrefaciens (98 %), Shewanella oneidensis (97 %) and Shewanella baltica (96 %). Levels of DNA homology between strain LT13a(T) and S. putrefaciens, S. oneidensis and S. baltica were <20 %, indicating that strain LT13a(T) represents a novel species. Genetic evidence and phenotypic characteristics showed that isolate LT13a(T) constitutes a novel species of the genus Shewanella. Because of the deep origin of the strain, the name Shewanella profunda sp. nov. is proposed, with LT13a(T) (=DSM 15900(T)=JCM 12080(T)) as the type strain.

Anaerobiosis↗
PubMed2006

Desulfuromonas svalbardensis sp. nov. and Desulfuromusa ferrireducens sp. nov., psychrophilic, Fe(III)-reducing bacteria isolated from Arctic sediments, Svalbard.

Two psychrophilic, Gram-negative, rod-shaped, motile bacteria (strains 112T and 102T) that conserved energy from dissimilatory Fe(III) reduction concomitant with acetate oxidation were isolated from permanently cold Arctic marine sediments. Both strains grew at temperatures down to -2 degrees C, with respective temperature optima of 14 degrees C and 14-17 degrees C for strains 112T and 102T. The isolated strains reduced Fe(III) using common fermentation products such as acetate, lactate, propionate, formate or hydrogen as electron donors, and they also grew with fumarate as the sole substrate. As alternatives to Fe(III), they reduced fumarate, S0 and Mn(IV). Based on 16S rRNA gene sequence similarity, strain 112T was most closely related to Desulfuromonas acetoxidans (97.0 %) and Desulfuromonas thiophila NZ27T (95.5 %), and strain 102T to Malonomonas rubra Gra Mal 1T (96.3 %) and Desulfuromusa succinoxidans GylacT (95.9 %) within the Deltaproteobacteria. Strains 112T and 102T therefore represent novel species, for which the names Desulfuromonas svalbardensis sp. nov. (type strain 112T=DSM 16958T=JCM 12927T) and Desulfuromusa ferrireducens sp. nov. (type strain 102T=DSM 16956T=JCM 12926T) are proposed.

Acetic Acid↗
PubMed1980

Tetracycline transport in Bacteroides fragilis.

In susceptible strain of Bacteroides fragilis, tetracycline uptake is biphasic. The initial phase is independent of adenosine 5'-triphosphate synthesis, which is coupled to fumarate reduction; this phase is not altered by expression of tetracycline resistance genes in a resistant strain. The second phase appears to occur by active transport, since it is largely reduced by rotenone, an inhibitor of electron transport to fumarate; moreover, this phase is under negative control of the tetracycline resistance gene.

Bacteroides fragilis↗