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PubMed1972

Regulation of nitrate reductase in Neurospora crassa: regulation of transcription and translation.

A technique employing cycloheximide and actinomycin D has been used for the separation of transcription and translation during the induction of nitrate reductase in Neurospora crassa. Nitrate reductase is found to be synthesized in low efficiency when nitrate is not provided during both transcription and translation. Nitrate reductase synthesis is enhanced by nitrate. Nitrate is found to induce nitrate reductase by enhancing the increase of the capacity to synthesize nitrate reductase, and ammonia is found to repress nitrate reductase, by inhibiting the induced increase of the capacity to make the enzyme, or by making it unstable in vivo, or both. The effect of ammonia is partially reversed by nitrate. The addition of ammonium tartrate or the removal of nitrate during translation of the induced capacity to synthesize nitrate reductase is found to result in the inactivation of nitrate reductase in vivo. A low level of nitrate in the medium is found to be sufficient for enhancing the induced increase of the capacity to synthesize nitrate reductase, but a higher level of nitrate is required to stabilize the enzyme after its formation. The induced capacity to synthesize nitrate reductase is relatively stable in the presence or absence of nitrate, but not in the presence of ammonia.

Ammonia↗
PubMed1981

Properties of the Bacillus licheniformis A5 glutamine synthetase purified from cells grown in the presence of ammonia or nitrate.

The glutamine synthetase from Bacillus licheniformis A5 was purified by using a combination of polyethylene glycol precipitation and chromatography on Bio-Gel A 1.5m. The resulting preparation was judged to be homogeneous by the criteria of polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate, equilibrium analytical ultracentrifugation, and electron microscopic analysis. The enzyme is a dodecamer with a molecular weight of approximately 616,000, and its subunit molecular weight is 51,000. Under optimal assay conditions (pH 6.6, 37 degrees C) apparent Km values for glutamate, ammonia, and manganese.adenosine 5'-triphosphate (1:1 ratio) were 3.6, 0.4, and 0.9 mM, respectively. Glutamine synthetase activity was inhibited approximately 50% by the addition of 5 mM glutamine, alanine, glycine, serine, alpha-ketoglutarate, carbamyl phosphate, adenosine 5'-diphosphate, or inosine 5'-triphosphate to the standard glutamine synthetase assay system, whereas 5 mM adenosine 5'-monophosphate or pyrophosphate caused approximately 90% inhibition of enzyme activity. Phosphorylribosyl pyrophosphate at 5 mM enhanced activity approximately 60%. We were unable to detect any physical or kinetic differences in the properties of the enzyme when it was purified from cells grown in the presence of ammonia or nitrate as sole nitrogen source. The data indicate that B. licheniformis A5 contains one species of glutamine synthetase whose catalytic activity is not regulated by a covalent modification system.

Amino Acids↗
PubMed1983

Effect of microbiological hydrolysis of urea on the nitrification process.

The aim of this study was to determine the causes of previously observed inhibition of stage II of nitrification in nitrifying activated sludge treating industrial wastewaters containing ammonium, urea and nitrates. Experiments made with both industrial wastewaters and synthetic medium containing equivalent concentrations of nitrogen compounds demonstrated that the factor limiting the activity of nitrobacteria is microbiological hydrolysis of urea, the causative agent probably being free ammonia released in the course of this hydrolysis.

Bacteria↗
PubMed1988

Growth and macromolecular content of the dimorphic fungus Aureobasidium pullulans and the effect of hydroxyurea and other inhibitors.

The growth kinetics and the macromolecular content of the yeast and ethanol-induced hyphal forms of Aureobasidium pullulans were studied. During the morphological transition from yeasts to hyphae, both the protein and RNA content decreased significantly, the mycelial form containing only 76% of the amount of protein in the yeasts, and 38% of the RNA. The DNA was the only component tested whose level increased during the transition. Among several compounds inhibiting macromolecular synthesis, only hydroxyurea showed a remarkable effect on the morphology of A. pullulans, inducing the mycelial morphology. The macromolecular composition of hydroxyurea-treated cultures changed with time in a way similar to that of the ethanol-Tween 80-ammonia medium, and to that of carbon-starved cultures, without ethanol or glucose.

Culture Media↗
PubMed1985

Trace elements in chemical evolution. II: Synthesis of amino acids under simulated primitive earth conditions in the presence of trace elements.

Electric discharge experiments have been performed in a plausible primitive earth atmosphere consisting of methane, nitrogen, and water over an aqueous phase of an ammonia-ammonium buffer solution. In some experiments, ions of metal elements, calcium, magnesium, zinc, iron and molybdenum were introduced. Gas phase products and amino acids in the liquid phase were analyzed by gas chromatography. With trace metal ions, less organic compounds in the gas phase and larger amounts of amino acids were obtained than without them. The results have shown the possible importance of trace elements in chemical evolution and the origin of life on the earth.

Amino Acids↗
PubMed1969

Role of ammonium ion in the biosynthesis of beta-nitropropionic acid.

The metabolism of inorganic nitrogen compounds was studied in extracts of Penicillium atrovenetum which had been grown under conditions in which beta-nitropropionic acid (BNP) synthesis varied from 0 to 12.5 mumoles per ml. None of the extracts was able to oxidize ammonium ion or nitrite. An enzyme was detected which catalyzed the oxidation of hydroxylamine with cytochrome c as the electron acceptor. The activity of this enzyme was not related to the ability of the organism to produce BNP. Nitrate and nitrite reductase activities were detected only in P. atrovenetum cultures grown on nitrate as a nitrogen source. These results indicated that BNP synthesis is probably not directly associated with the metabolism of inorganic nitrogen compounds and that an organic pathway for the formation of the nitro group is more likely. The activities of certain enzymes related to the metabolism of aspartic acid were investigated. Aspartate ammonia-lyase activity could not be detected in P. atrovenetum extracts. Aspartate aminotransferase and glutamate dehydrogenase activities were found in the extracts but were highest in the cultures which did not produce BNP. beta-Nitroacrylic acid reductase activity was highest in extracts of cultures which were actively synthesizing BNP.

Aspartate Aminotransferases↗
PubMed2004

Mechanisms of ammonia activation and ammonium ion inhibition of quinoprotein methanol dehydrogenase: a computational approach.

The mechanism of methanol oxidation by quinoprotein methanol dehydrogenase (MDH.PQQ) in combination with methanol (MDH.PQQ.methanol) involves Glu-171--CO2(-) general base removal of the hydroxyl proton of methanol in concert with hydride equivalent transfer to the >C5=O quinone carbon of pyrroloquinoline quinone (PQQ) and rearrangement to hydroquinone (PQQH2) with release of formaldehyde. Molecular dynamics (MD) studies of the structures of MDH.PQQ.methanol in the presence of activator NH3 and inhibitor NH4(+) have been carried out. In the MD structure of MDH.PQQ.methanol.NH3, the hydrated NH3 resides at a distance of approximately 24 A away from methanol and the ortho-quinone portion of PQQ. As such, influence of NH3 on the oxidation reaction is not probable. We find that NH4(+) competes with the substrate by hydrogen-bonding to Glu-171CO2(-) such that the MDH.PQQ.methanol.NH4(+) complex is not reactive. Ammonia readily forms imines with quinone. Imines are present in solution as neutral (>C5=NH) and protonated (>C5=NH2(+)) species. MD simulations establish that the >C5=NH2(+) derivative of MDH.PQQ(NH2(+).methanol structure is unreactive because of the nonproductive means of methanol binding. The structure obtained by the MD simulations with the neutral >C5=NH imine of MDH.PQQ(NH).methanol structure is similar to the reactive MDH.PQQ.methanol complex. This active site geometry allows for catalysis of hydride equivalent transfer to the >C5=NH of PQQ(NH) by concerted Glu-171CO(2)(-) general-base removal of the H-OCH3 proton and Arg-324H+ general-acid proton transfer to the imine nitrogen. Enzyme-bound <C5(H)NH2 derivative of PQQ [PQQ(NH)] and CH(2)O product are formed.

Alcohol Oxidoreductases↗
PubMed1989

The physiology of L-methionine catabolism to the secondary metabolite ethylene by Escherichia coli.

Catabolism of L-methionine by Escherichia coli strain B SPAO led to the formation of ethylene as a secondary metabolite (ethylenogenesis). Methionine was initially deaminated by a transamination reaction to the 2-oxo acid 2-oxo-4-methylthiobutyric acid (KMBA) which was then converted to ethylene. The utilization of L-methionine as an additional nitrogen source was investigated by examining ethylene synthesis under different nitrogen supply conditions. Ethylene formation in batch culture was unaffected by the concentration of the precursor L-methionine in the medium although increasing concentrations of NH4Cl resulted in progressively less ethylene formation. Cultures grown without L-methionine did not produce ethylene but were able to synthesize ethylene when L-methionine or KMBA was provided. Addition of L-tyrosine to batch cultures reduced the yield of ethylene after 42 h by 54%. Under these conditions the maximum transient level of KMBA was reduced by 32% and occurred later compared to when L-methionine was the only amino acid supplement. Continuous cultures grown under ammonia limitation produced both ethylene and KMBA. In contrast, when glucose was limiting, neither of these metabolites were produced. Cells harvested from continuous cultures grown under glucose or ammonia limitation were able to synthesize ethylene from either L-methionine or KMBA although their capacity for ethylene synthesis (ethylenogenic capacity) was optimal under ammonia limitation (C:N ratio = 20).

Ammonium Chloride↗