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PubMed1976

The conversion of leucine to alpha-ketoisocaproic acid and its metabolic consequences for Escherichia coli K12.

The amino acid L-leucine serves as a good auxiliary nitrogen source for Escherichia coli K12, and in so doing is converted to alpha-ketoisocaproic acid which is excreted into the medium. L-Leucine does not serve as sole nitrogen source. Cells incubated with L-leucine as sole nitrogen source do not grow, although they do metabolize leucine, and accumulate ketoisocaproic acid in the medium. Where glycine is the only other nitrogen source, the presence of L-leucine greatly increases the growth rate even at concentrations so low that its contribution as nitrogen donor is unlikely to be important.

Ammonium Sulfate↗
PubMed1978

The microbial degradation of cyclohexanecarboxylic acid by a beta-oxidation pathway with simultaneous induction to the utilization of benzoate.

The metabolism of cyclohexanecarboxylic acid by a bacterium, designated PRL W19, follows a pathway involving beta-oxidation of coenzyme A intermediates analogous to the classical oxidation of fatty acids. The organism appears to have the property for the constitutive metabolism of caproic acid, and cell extracts contain high levels of the enzymes required for the functioning of the fatty acid cycle. However, the metabolism of cyclohexanecarboxylic acid requires induction by growth or incubation with an appropriate substrate. Extracts of induced cells contain several enzyme activities which are synthesized in response to the induction process. These enzymes include cyclohexanecarboxyl-CoA synthetase, cyclohexanecarboxyl-CoA dehydrogenase, 1-cyclohexenecarboxyl-CoA hydratase, and trans-2-hydroxycyclohexanecarboxyl-CoA dehydrogenase. A characteristics feature of this organism is that it becomes induced for the metabolism of benzoate and catechol during growth on cyclohexanecarboxylic acid, but benzoate does not appear to be an obligatory intermediate in the metabolism of cyclohexanecarboxylic acid.

3-Hydroxyacyl CoA Dehydrogenases↗
PubMed1982

Leucine dissimilation to isovaleric and isocaproic acids by cell suspensions of amino acid fermenting anaerobes: the Stickland reaction revisited.

Freshly compared cell suspensions of clostridia (Clostridium bifermentans, C. botulinum proteolytic type A, C. difficile, C. sordellii, and C. sporogenes) and Peptostreptococcus anaerobius converted leucine to isovaleric (iV) and isocaproic (iC) acids in the absence of other amino acids. The optimal pH for conversion was between 8 and 9 at 37 degrees C. The stoichiometry of reaction was compatible with that expected for the Stickland reaction, as the ratio of iV to iC was 1:2, the amount of CO2 produced was equivalent to that of iV, and ammonium ion concentrations were equal to the total C5 and C6 acids formed. The presence of alanine and valine (proton donors in the Stickland reaction) in incubations effectively increased the concentration of iC at the expense of iV production, implying that leucine acted there primarily as a proton acceptor. Glycine and proline (proton acceptors) stimulated both iV and iC production from leucine, but increases in iV concentrations were proportionately greater than for iC so that leucine was primarily a proton donor in the presence of proton acceptors. Glucose stimulated the conversion of leucine to volatile fatty acids but favoured iC production. Production of iC from leucine was inhibited by surface active compounds (cetyltrimethylammonium bromide and desoxycholate) as well as arsenite and iodoacetate. The redox dyes methyl viologen and phenosafranine inhibited iC production more severely than iV production, as did the nitroimidazole antimicrobial agent, metronidazole.

Amino Acids↗
PubMed1983

Subcellular location of enzymes involved in leucine dissimilation in Clostridium bifermentans.

Conversion of leucine to isovaleric (iV) and isocaproic (iC) acids by cell-free extracts of Clostridium bifermentans was demonstrated using two lysis procedures. Sonication resulted in an extract which had the enzymes to convert leucine to alpha-ketoisocaproic acid (alpha-kiC) and thence iV, but failed to produce iC. Extracts prepared by osmotic lysis, which contained intact membranes, could convert leucine to both iV and iC. The enzyme which converts leucine to alpha-kiC was solubilized during osmotic lysis, whereas the decarboxylase and leucine reductase system remained membrane bound. Osmotic lysis also released at least two small molecular weight, heat-stable, anionic components (3500 greater than molecular weight greater than or equal to 1000), which stimulated decarboxylase activity.

Caproates↗
PubMed1984

Impact of an oil field effluent on microbial activities in a Wyoming river.

The survival, functions, and physiological diversity of autochthonous sediment microbiota were examined in situ at five stations along the Little Popo Agie River, WY; one station above, one at, and three below a discharge point for oil wastewater from Union Oil Company's Dallas Field. Below the oil wastewater discharge point there were increases in electron-transport activity, carbon dioxide production, and microbial populations of heterotrophs, ammonifiers, hexadecane degraders, starch hydrolyzers, protein hydrolyzers, and sulfate reducers. At a station 1420 m below the discharge point, however, overall sediment microbial activities and all of the physiological groups of bacteria, except hexadecane-degrading microbiota, were at levels comparable with those at the control station above the discharge point. Similarly, mineralization of glucose, amino acids, hexanoic acid, and hexadecane was elevated at stations directly below the discharge point, but appeared to subside rapidly. Xenobiotic biodegradation potential of the sediments varied with the chemical and the sample location and was not directly related to oil residue levels in the sediment. Microorganisms thus appeared to maintain physiological diversity and increased in numbers and activity in a riverine environment that contained petroleum hydrocarbon concentrations known to be deleterious to freshwater fish and macrobenthic communities.

Alkanes↗
PubMedDate not supplied

Synthesis of two photoreactive heterobifunctional reagents derived from hexanoic acid.

The synthesis of two photoreactive heterobifunctional reagents derived from hexanoic acid is described. The compounds are succinimido 6-N-(4-azidobenzoyl)aminohexanoate (1c) and succinimido 6-mercapto-S-(4-azidothiophenyl)hexanoate (2c). Compound 1c was synthesized from benzyloxycarbonyl 4-aminobenzoic acid and 6-aminohexanoic acid benzyl ester. Compound 2c was obtained by disulfide exchange of dithiobis-4-aminobenzene with 6-mercaptohexanoic acid. The azido function was introduced by displacement of the corresponding diazonium salt and the active ester, by the mixed anhydride method. Both compounds were decomposed by ultraviolet irradiation. Phytohemagglutinin was modified by reaction with reagent 1c or 2c. Irradiation afforded polymeric lectin derivatives resulting from intermolecular cross-linking. Sodium dodecyl sulfate--polyacrylamide gel electrophoresis analyses revealed the presence of Coomasie-positive bands of molecular weight 33000, 67000, 120000, 144000, and higher. Polymeric structures resulting from irradiation of phytohemagglutinin modified with compound 2c were cleaved by reduction with 2-mercaptoethanol or with dithiothreitol. Phytohemagglutinin modified by reaction with compound 1c or 2c retained its ability to stimulate pig spleen lymphocytes in vitro. Whereas the lectin treated with reagent 2c was active as the unmodified protein, the lectin treated with compound 1c was more active than unmodified lectin at nearly all the concentrations tested.

Animals↗
PubMed1990

Oxidation of 2-oxoisocaproate and 2-oxoisovalerate by the perfused rat heart. Interactions with fatty acid oxidation.

The interactions between fatty acid oxidation and the oxidation of the 2-oxo acids of the branched chain amino acids were studied in the isolated Langendorff-perfused heart. 2-Oxoisocaproate inhibited the oxidation of oleate, but 2-oxoisovalerate and 2-oxo-3-methylvalerate did not. This difference was not attributable to the magnitude of the flux through the branched chain 2-oxo acid dehydrogenase, which was slightly higher with 2-oxoisovalerate than with 2-oxoisocaproate. Oxidation of 2-oxoisocaproate in the perfused heart was virtually complete, since more than 80% of the isovaleryl-CoA formed from 2-oxo[1-14C]isocaproate was further metabolized to CO2, as determined by comparing 14CO2 production from 2-oxo[14C(U)]isocaproate with that from the 1-14C-labelled compound. Only twice as much 14CO2 was produced from 2-oxo[14C(U)]isovalerate as from the 1-14C-labelled compound, indicating incomplete oxidation. This was confirmed by the accumulation in the perfusion medium of substantial quantities of labelled 3-hydroxyisobutyrate (an intermediate in the pathway of valine catabolism), when hearts were perfused with 2-oxo[14C(U)]isovalerate. The failure of 2-oxoisovalerate to inhibit fatty acid oxidation, then, can be attributed to the fact that its partial metabolism in the heart produces little ATP. We have previously shown that 3-hydroxyisobutyrate is a good gluconeogenic substrate in liver and kidney, and postulate that 3-hydroxyisobutyrate serves as an interorgan metabolite such that valine can serve as a glucogenic amino acid, even when its catabolism proceeds beyond the irreversible 2-oxo acid dehydrogenase in muscle.

Animals↗
PubMed1978

Absence of Na+--H+ barrier function in mucosa of canine small bowel.

The study was designed to determine whether the special Na+--H+ barrier function of the gastric mucosa is present in the mucosa of the small bowel and whether a gastric mucosal barrier breaker (hexanoic acid) would accelerate the fluxes of sodium in duodenum-jejunum and ileum as in the stomach. The observations were made in healthy conscious dogs with Thiry-Vella fistulae of the small bowel or Heidenhain pouches of the gastric corpus. These barrier characteristics of the stomach were completely absent in the small intestine where bidirectional Na fluxes were 5--10 times greater than in the stomach and were not accelerated by hexanoic acid as they were in the stomach. A comparison was made between the rates of absorption of hexanoic acid, sodium hexanoate, and HCl from the pouches and fistulae. The lipid-soluble fatty acid was transported at all sites more rapidly than its water-soluble sodium salt. In the stomach and ileum the H+ of HCl and sodium hexanoate were absorbed at similar slow rates. The duodenal-jejunal mucosa, however, transported H+ at rates nearly identical to those of hexanoic acid. In our tests HCl was not neutralized in duodenal contents while large quantities were neutralized in the contents of ileum.

Animals↗
PubMed1980

The temperature dependence of ionic influences on contractile function in frog twitch muscle.

Alterations in the ionic composition of the medium produce striking changes in the potential-dependent contractile responses of skeletal muscles. This study was undertaken to examine the temperature dependence of some of these effects. The suppression of maximal K contractures of frog toe muscles in media lacking divalent cations was largely overcome by a sufficient increase in temperature. The restoration of K contractures by perchlorate in the absence of divalent cations was prevented by a sufficient decrease in temperature. The effect of perchlorate was to shift the temperature dependence of these contractures toward lower temperatures. The reduction in the amplitude of maximal K contractures in the absence of divalent cations was less marked after pretreatment with a reagent (trinitrobenzenesulfonate) that selectively modifies free amino groups, although the temperature dependence of these contractures was unchanged. The reduction in the amplitude of K contractures in the presence of an organic anion (hexanoate) was partially antagonized both by an increase in temperature or by a decrease in temperature, effects that resemble those observed in solutions in which the divalent cation concentration was reduced. In chloride solutions, the relation between [K]0 and K contractures was shifted toward lower [K]0 by an increase in temperature, whereas in perchlorate solutions increased temperature produced a shift in the opposite direction. The shift in this relation toward lower [K]0 at reduced temperature, and the accelerated time course of K contractures with an increase in temperature were similar in perchlorate and in chloride solutions. Thermodynamic analysis by Arrhenius plots indicated that the influence of divalent cations and perchlorate anions on K contractures may be the result of their effects on hydrational factors.

Animals↗
PubMed1997

Regulation of branched-chain ketoacid dehydrogenase flux by extracellular pH and glucocorticoids.

In muscles of rats with metabolic acidosis, branched-chain alpha-ketoacid dehydrogenase (BCKAD) activity is increased. Potential stimulatory signals include acidemia and/or glucocorticoids. It is unclear whether the signal(s) increases BCKAD activity by changing the activation state of the enzyme or by increasing the amount of enzyme. To separate the influences of extracellular pH and glucocorticoids on leucine catabolism, maximal BCKAD flux and the activation state (the ratio of basal to total flux) were measured in two cell types: 1) cells that do not express glucocorticoid receptors and 2) cells stably transfected to express glucocorticoid receptors. Acidification (pH 6.95) increased 1) the activation state from 67.2% at pH 7.4 to 82.8% at pH 6.95, 2) maximal BCKAD flux by 50%, and 3) the BCKAD subunit contents in both cell types (57, 410, and 270% for E2, E1 alpha, and E1 beta, respectively). Dexamethasone increased the BCKAD activation state from 67.2 to 82.3% in cells expressing glucocorticoid receptors, whereas dexamethasone plus acidification increased the activation state to 98%. The time course of stimulation by dexamethasone was slower than that by acidification. These results demonstrate that BCKAD is differentially regulated by extracellular pH and glucocorticoids.

3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)↗