Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0038187 (starvation)
 24,951 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Regulation of the expression of the histidase coded by hutk of Klebsiella aerogenes in Salmonella typhimurium and in Escherichia coli and of the expression of the histidase coded by huts of S. typhimurium in E. coli was investigated. The hutk histidase was found to be sensitive to catabolite repression in K. aerogenes and in E. coli, but insensitive to catabolite repression in S. typhimurium; huts histidase has previously been shown to be catabolite sensitive in all three organisms. The expression of both hutk and huts histidase in E. coli was activated by nitrogen starvation. Apparently, the glutamine synthetase of E. coli may activate the formation of some glutamate- and ammonia-producing enzymes.
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PMID:Regulation of histidase synthesis in intergeneric hybrids of enteric bacteria. 0 26

1. Slices of duodenum and jejunum produce ammonia from glutamine in vitro. 2. Ammoniagenesis does not increase in response to acidosis or potassium deficiency, two conditions known to cause enhanced ammoniagenesis in the kidney. 3. Gut contains glutaminase 1 as well as gamma-glutamyl transpeptidase. 4. These enzymes do not show any increase during starvation.
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PMID:Ammonia production by the small intestine of the rat. 0 12

Anthranilate synthase of Agmenellum quadruplicatum, a unicellular species of blue-green bacteria, consists of two nonidentical subunits. A 72,000 dalton protein has aminase activity but is incapable of reaction with glutamine (amidotransferase) unless a second protein (18,000 molecular weight) is present. The small subunit was first detected through its ability to complement a partially purified aminase subunit from Bacillus subtilis to produce a hybrid complex capable of amidotransferase function. Conditions for the function of the heterologous complex were less stringent than for the homologous A. quadruplicatum complex. A reducing agent such as dithiothreitol stabilizes the A. quadruplicatum aminase subunit and is obligatory for amidotransferase function. L-Tryptophan feedback inhibits both the aminase and amidotransferase reactions of anthranilate synthase; Ki values of 6 X 10(-8) M for the amidotransferase activity and 2 X 10(-6) M for the aminase activity were obtained. The Km value calculated for ammonia (2.2 mM) was more favorable than the Km value glutamine (13 mM). Likewise, the Vmax of anthranilate synthase was greater with ammonia than with glutamine. Starvation of a tryptophan auxotroph results in a threefold derepression of the aminase subunit, but no corresponding increase in the small 18,000 M subunit occurs. While microbial anthranilate synthase complexes are remarkably similar overall, the relatively good aminase activity of the A. quadruplicatum enzyme may be of physiological significance in nature.
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PMID:An anthranilate synthase of the extreme aminase type in a species of blue-green bacteria (algae). 10 18

Two different inactivators of nitrate reductase have been found in cell free preparations of Neurospora. The first (Inactivator I) is very active at pH 9, is inhibited by disodium ethylene diamine tetraacetate (EDTA) and is present in all mycelia incubated under all conditions tested; the second (Inactivator II) is very active at pH 5, is repressed by ammonia or by a metabolic product of ammonia and derepressed by nitrogen starvation, cannot be derepressed by nitrogen starvation in strain nit-2, in which a number of "ammonia-represible" enzymes are permanently repressed, and is sensitive to phenyl methyl sulfonyl fluoride. Crude extracts of mycelia contain inhibitor(s) of both inactivators.
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PMID:Demonstration in vitro of two intracellular inactivators of nitrate reductase from Neurospora. 14 14

When washed spleen slices from fed rats are incubated with 3 mm-[U-14C]glucose, the rate of glucose utilization (46.2 mumol/h per g dry wt.) is sufficient to account, theoretically, for 80% of the O2 consumption. Measurement of net lactate production, however, and the fate of the radioactive carbon, indicates that the contribution of glucose to the respiratory fuel of the tissue is only 25-30% whereas 60-70% of the glucose utilized is converted into lactate. At saturating glucose concentrations (above 5 mm) its contribution to the respiratory fuel of the slice is increased to a maximum value of 34-39%. Only 2% of the glucose utilized is metabolized via the oxidative steps of the pentose phosphate pathway. Starvation for 72 h marginally increases both the rate of glucose utilization (by 21%) and its net contribution to the respiratory fuel (by 29%). Insulin, glucagon, adrenaline and adenosine 3':5'-cyclic monophosphate have no significant effect on either the rate of glucose utilization or on the pattern of radioactive isotope distribution. The uptake of glucose is increased by only 20%, whereas the production of lactate doubles when slices are incubated under anaerobic conditions. In assessing the suitability of spleen slices for metabolic studies, the only serious major perturbation, compared with the freeze-clamped organ, is an elevated mitochondrial [NAD+]/[NADH] ratio (connected with increased endogenous NH3 production) that is partially restored to normal values on incubation with glucose. Equal proportions of erythrocytes and leucocytes are found in the washed spleen slice. Metabolic contributions of the constituent cell populations in the washed slice are calculated and it is concluded that lymphocytes account for the major part of the glycolytic metabolism (80-90%), whereas the contribution of erythrocytes is insignificant.
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PMID:Regulation of carbohydrate metabolism in lymphoid tissue. Quantitative aspects of [U-14C]glucose oxidation by rat spleen slices. 17 88

The phenotype of certain mutations in pyrA, the gene encoding carbamylphosphate synthetase (CPSase), is expressed only in the presence od exogenous arginine. In unsupplemented media, synthesis of carbamylphosphate and growth was almost normal; in arginine-containing media, synthesis of carbamylphosphate stopped, as did growth, as a consequence of starvation for pyrimidine. Genetic and biochemical evidence suggests that arginine exerts this inhibition by repressing the synthesis of ornithine carbamyltransferase (OTCase), the intracellular presence of which is required for assembly of the unequal subunits and proper functioning of the mutant CPSase. After the addition of arginine to a culture of the mutant, CPSase activity (glutamine dependent) characteristic of the intact holoenzyme progressively decreased, whereas activity (ammonia dependent) characteristic of the free large (alpha) subunit increased. Extracts of mutant cells contain free small (beta) subunits, as demonstrated directly by in vitro complementation using purified alpha subunits from wild type. The mutant enzyme from cultures grown in the presence of arginine had a markedly decreased affinity for adenosine 5'-triphosphate. Mutations in argR that cause depressed synthesis of OTCase suppressed the phenotype, and a certain mutation in argI, the gene encoding OTCase, enhanced it. In vitro experiments using purified enzyme confirm the stimulatory effect of OTCase on the activity of mutant CPSase.
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PMID:Arginine-sensitive phenotype of mutations in pyrA of Salmonella typhimurium: role of ornithine carbamyltransferase in the assembly of mutant carbamylphosphate synthetase. 18 93

Methylamine (methylammonium ion) entered Saccharomyces cerevisiae X2180-A by means of a specific active transport system. Methylamine uptake was pH dependent (maximum rate between pH 6.0 and 6.5) and temperature dependent (increasing up to 35 C) and required the presence of a fermentable or oxidizable energy source in the growth medium. At 23 C the vmax for methylamine transport was similar 17 nmol/min per mg of cells (dry weight) and the apparent Km was 220 muM. The transport system exhibited maximal activity in ammonia-grown cells and was repressed 60 to 70 percent when glutamine or asparagine was added to the growth medium. There was no significant derepression of the transport system during nitrogen starvation. Ammonia (ammonium ion) was a strong competitive inhibitor of methylamine uptake, whereas other amines inhibited to a much lesser extent. Mutants selected on the basis of their reduced ability to transport methylamine (Mea-R) simultaneously exhibited a decreased ability to transport ammonia.
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PMID:Methylamine and ammonia transport in Saccharomyces cerevisiae. 23 81

During recent studies conducted with suspensions of three strains of Saccharomyces cerevisiae, it was observed that ammonia was rapidly liberated when L-asparagine was added to the medium. Subsequent investigation has revealed that these strains of S. cerevisiae have an externally active asparaginase as well as an internally active one. The appearance of the external asparaginase is stimulated by nitrogen starvation, requires an available energy source, and is prevented by cycloheximide. The internal enzyme appears to be constitutive. The external activity is relatively insensitive to para-hydroxymercuribenzoate inhibition, whereas the internal activity is highly inhibited by this compound.
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PMID:L-Asparaginase of Saccharomyces cerevisiae: an extracellular Enzyme. 23 36

The effects of starvation on the acid-base status of the rat and on the glucoeogenic and ammoniagenic capacity of rat renal-cortical slices were examined. Starvation for 48 or 72 hr did not affect acid-base status, and urinary ammonia production did not change. Kidney cortical slices from starved as compared to fed rats showed increased gluconeogenic capacity when incubated with the substrated pyruvate, succinate, fumarate, malate, 2-oxyoglutarate, glutamine and glutamate. Renal cortical tissue from starved rats also had increased activity of the gluconeogenic enzyme phosphoenolpyruvate carboxykinase. Renal cortical slices from starved rats did not differ from those from fed rats in the ability to produce ammonia from glutamine or glutamate, nor was there any difference inhe activity of glutaminase between these groups. These results show that renal gluconeogenic capacity is increased in starved rats in the absence of systemic acidosis, and starvation does not lead to an increase in urinary ammonia excretion or renal ammoniagenic capacity.
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PMID:Effect of starvation on renal metabolism in the rat. 24 54

1. The levels of the individual free amino acids, K, Na and water present in parietal muscle were measured in fish starved for periods of 3-115 days. 2. The Na and water content progressively increased relative to dry weight of tissue during the starvation period whereas an initial increase in the K content up to 67 days was followed by a decrease to near the normal fed level by 115 days. The ammonia content remained essentially stable over the same period. 3. The essential free amino acid content tended to follow the muscle sodium pattern while the non-essential amino acids and taurine gave results somewhat similar to those of potassium. 4. The net result of these changes is that the Na, K and total free amino acid concentration is maintained within fairly narrow limits relative to the tissue water content during 11-67 days of the starvation period under the experimental conditions used.
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PMID:The effects of starvation on the sodium, potassium, water and free amino acid content of parietal muscle from Agonus cataphractus. 31 60


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