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Query: EC:1.4.1.2 (glutamate dehydrogenase)
 4,380 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Glucose-limited chemostat cultures of Escherichia coli, growing at dilution rates above 0.3/hr, continue to grow at the restricted rate after removal of glucose restriction. In a glycogenless strain, the specific rates of increase of mass, protein, and ribonucleic acid (RNA) were equal before and after supplementation with 0.05% glucose and did not increase detectably until after 30 to 60 min. The unrestricted specific growth rate was reached after two to three doublings of cell mass. Supplementation with glucose plus 20 amino acids, but not with glucose plus vitamins or ribosides, produced an immediate increase in the specific rates of mass and RNA synthesis followed by an increase in the specific rate of protein synthesis. In a wild-type strain, synthesis of protein and RNA continued at the restricted rate after glucose supplementation, but the specific rate of increase of mass immediately increased due to rapid synthesis of glycogen. At dilution rates less than 0.3/hr, the specific rates of increase of mass, protein, and RNA increased immediately after supplementation with glucose, but did not immediately attain the unrestricted growth. The results at dilution rates greater than 0.3/hr are interpreted to mean that the regulation of a number of enzymatic reactions is entirely through control of enzyme synthesis, without modulation of enzyme function. The levels of such enzymes are controlled so that operation with zero-order kinetics precisely meets the demands for balanced growth. It was shown that glutamic dehydrogenase and glutamic-oxalacetic transaminase are regulated in this manner.
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PMID:Metabolic regulation in glucose-limited chemostat cultures of Escherichia coli. 492 69

Buono, F. (Syracuse University, Syracuse, N.Y.), R. Testa, and D. G. Lundgren. Physiology of growth and sporulation in Bacillus cereus. I. Effect of glutamic and other amino acids. J. Bacteriol. 91:2291-2299. 1966.-Growth and sporulation were studied in Bacillus cereus by use of an active culture technique and a synthetic medium. A high level of glutamic acid (70 mm) was required for optimal growth and glucose oxidation followed by sporulation even though relatively little glutamic acid was consumed (14 mm). Optimal growth occurred with a combination of 14 mm glutamic acid and 56 mm (NH(4))(2)SO(4), aspartic acid, or alanine. Ornithine or arginine at 70 mm could replace glutamic acid in the synthetic medium without affecting the normal growth cycle. Glutamic acid was not replaced by any other amino acid, by (NH(4))(2)SO(4), or by a combination of either alpha-ketoglutarate or pyruvate plus (NH(4))(2)SO(4). Enzyme assays of cell-free extracts prepared from cells harvested at different times were used to study the metabolism of glutamic acid. Glutamic-oxaloacetic and glutamic-pyruvate transaminases were completely activated (or derepressed) during early stages of sporulation (period of 6 to 8 hr). Alanine dehydrogenase responded in a similar manner, but the levels of this enzyme were much higher throughout the culture cycle. Neither glutamic dehydrogenase nor alpha-ketoglutarate dehydrogenase was detected. Sporulation in a replacement salts medium was studied with cells harvested at different times from the synthetic medium. Cultures 2 to 6 hr old were unable to sporulate in the replacement salts medium unless glutamic acid (7.0 mm) was present. By the 6th hr, cells were in the early stages of sporulation, showing spore septa development. Cultures 8 hr old sporulated in the replacement salts medium. Other metabolic intermediates able to replace glutamic acid in the replacement salts medium were alanine, aspartic acid, and glutamine at equimolar concentrations. Also, ammonium ions in combination with pyruvic, oxaloacetic, alpha-ketoglutaric, or fumaric acid replaced glutamic acid. The likely role of these metabolites is discussed.
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PMID:Physiology of growth and sporulation in Bacillus cereus. I. Effect of glutamic and other amino acids. 495 15

Streptomycin slightly inhibited lactic and malic dehydrogenases of Bacillus subtilis, and inhibited isocitric dehydrogenase to about 60%. The formation of lactic dehydrogenase, glutamic dehydrogenase, alpha-alanine dehydrogenase, and succinic dehydrogenase was stimulated by the antibiotic at a concentration causing 50% inhibition of bacterial growth. Streptomycin had practically no influence on the formation of malic dehydrogenase, but the antibiotic produced 48% inhibition of the synthesis of isocitric dehydrogenase.
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PMID:Effect of streptomycin on some enzyme systems of Bacillus subtilis. 497 69

Enzymatic techniques were used to study the metabolism of carbohydrates by ruminal bacteria. A direct relationship was observed between the proportions of acetate and propionate formed and the specific activities of the enzymes which participate in forming these acids. An inverse relationship between butyrate formation and butyrate-forming enzymes was observed. The relative activities of succinic dehydrogenase to fumaric reductase, nicotinamide adenine dinucleotide-linked glutamic dehydrogenase to nicotinamide adenine dinucleotide phosphate-linked glutamic dehydrogenase, and pyridine nucleotide-nonlinked lactic dehydrogenase to pyridine nucleotide-linked lactic dehydrogenase were affected by the level of concentrates in the diet. Lactyl coenzyme A dehydrase activity was below the limits of the assay technique in many samples from the alfalfa hay diet, and increased to relatively high levels when concentrates were fed. It is suggested that the enzymatic method will prove valuable for studying the contributions of individual microorganisms to the overall ruminal metabolism, and, with certain limitations, useful for estimating the relative contributions of alternate pathways.
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PMID:Enzymatic techniques for the study of pathways of carbohydrate utilization in the rumen. 595 Feb 50

Washed-cell preparations of Mycobacterium tuberculosis strain H37Ra and M. smegmatis 607 grown in Sauton's medium demonstrated a lag in glutamate oxidation. Washed-cell preparations of M. fortuitum and M. phlei oxidized glutamate immediately and in a linear fashion. Glutamate was oxidized without a lag by washed cells of M. tuberculosis H37Ra and M. smegmatis 607 harvested from a modified medium containing glutamate. Chloramphenicol inhibited the oxidation of glutamate by washed cells grown in the absence of glutamate. These findings suggested the induction of either an enzyme system for glutamate oxidation or a glutamate transport system. The activity of glutamic dehydrogenase was not significantly greater in extracts prepared from cells grown with glutamate. However, the initial rate of glutamate uptake by induced cells was three to four times higher than in noninduced cells. The induction of the glutamate transport system in M. tuberculosis H37Ra and M. smegmatis 607 was shown to parallel the induction of glutamate oxidation. After a 60-min lag, the inducible glutamate transport system appeared. Chloramphenicol prevented the induction of glutamate uptake, although the antibiotic had no effect on glutamate uptake by previously induced cells. Some of the properties of this glutamate uptake system are described.
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PMID:Inducible glutamate transport in Mycobacteria and its relation to glutamate oxidation. 602 4

In Neurospora crassa the assimilation of high and low concentrations of ammonium occurs by two different pathways. When the fungi are growing exponentially on ammonium excess, this compound is fixed by a glutamic dehydrogenase and an octameric glutamine synthetase (GS). The synthesis of this GS polypeptide (beta) is regulated by the nitrogen source present in excess; being higher on glutamate, intermediate on ammonium, and lower on glutamine. When N. crassa is growing in fed-batch ammonium-limited cultures a different polypeptide of GS (alpha), arranged as a tetramer, is synthesized. In both conditions synthesis in vivo correlates with the data obtained with an in vitro translation system primed with N. crassa RNA. This different expression of alpha and beta GS polypeptides was also observed when the cultures were shifted from excess to low nitrogen, and vice versa. By agarose gel electrophoresis in the presence of methylmercury hydroxide, some separation of different mRNAs that direct the in vitro synthesis of alpha and beta GS polypeptides has been accomplished. Data are presented that establish the operation of the tetrameric alpha GS and of glutamate synthase in the assimilation of ammonium in low concentration.
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PMID:Physiology of ammonium assimilation in Neurospora crassa. 612 Sep 27

The serum activities of monoamine oxidase (MAO), gamma-glutamyl transferase (GGT) and glutamic dehydrogenase (GDH) enzymes were measured in 25 patients with Schistosoma mansoni infection (Group I), 26 patients with schistosomal hepatosplenomegaly and ascites (Group II) and 21 normal controls. The activities of these enzymes were compared with those of serum aspartate aminotransferase (AST), alanine aminotransferase (ALT) and alkaline phosphatase (ALP). The mean levels of MAO, GGT and GDH of Group I were not significantly different from controls. The mean levels of MAO and GGT in Group II, however, were significantly different from corresponding mean levels of Group I and the controls at P less than .001. Changes in the mean level of GDH and ALT were not significant. By contrast, the levels of AST and ALP in both groups showed significant elevation over control levels at P less than .001. These results indicate that estimation of the two enzymes MAO and GGT may aid in the biochemical differentiation of the stages of schistosomiasis and their associated hepatic complications.
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PMID:Serum enzyme tests in hepatosplenic schistosomiasis. 612 67

Glutamate dehydrogenase activity was determined in mitochondrial preparations from rat ventral prostate and rat kidney. Kinetic parameters of the ventral prostate enzyme were comparable to those for the kidney enzyme. Glutamate dehydrogenase activity in the direction of glutamate oxidative deamination was inhibited by alpha-ketoglutarate. However, the characteristics of alpha-ketoglutarate inhibition indicated that glutamate oxidation via glutamate dehydrogenase can occur at in vivo prostatic alpha-ketoglutarate levels. These results suggest that glutamate dehydrogenase activity in prostate may provide a continuous source of alpha-ketoglutarate for aspartate transamination to oxalacetate and ultimate citrate synthesis. In addition prostate mitochondria are able to couple the glutamic dehydrogenase reaction to aspartate aminotransferase. Under these conditions aspartate in the presence of glutamate and acetyl coenzyme A will result in a net synthesis of citrate. Consequently we propose an aspartate-glutamate pathway for citrate synthesis in prostate.
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PMID:Glutamate dehydrogenase and a proposed glutamate-aspartate pathway for citrate synthesis in rat ventral prostate. 615 Jan 22

The accumulations by axoplasmic transport of selected enzyme activities proximal and distal to a ligature placed on the sciatic nerve were monitored in rats exposed in utero to maternal antibodies to nerve growth factor (NGF) and in control rats. Littermates of the animals exposed to anti-NGF were shown elsewhere to have had a 70% reduction in the number of sensory neurons in dorsal root ganglia and a 90% reduction in number of neurons in superior cervical (sympathetic) ganglion. The accumulation of F(-)-sensitive acid phosphatase activity was depressed 75% both proximal and distal to the tie. Accumulation of F(-)-resistant acid phosphatase activity was depressed nearly 50% proximal to the tie. Distal accumulation of this activity did not occur in either group of rats. Accumulation of acetylcholinesterase activity was depressed 30%. Distal accumulation of the activities of beta-glucuronidase and hexokinase was depressed 50%. In the lumbar dorsal root ganglia, dry weight was reduced 40%, and the activities of peroxide-sensitive, F(-)-resistant acid phosphatase and of the mitochondrial enzymes hexokinase, glutamic dehydrogenase, glutamic-oxalacetic transaminase, and NAD-dependent isocitric dehydrogenase were all reduced a little more, 45--50% per ganglion. However, the activities of the lysosomal enzymes, F(-)-sensitive acid phosphatase and beta-glucuronidase, of the peroxide-resistant, F(-)-resistant acid phosphatase, and of the mitochondrial enzyme glutaminase were all reduced about 60% per ganglion. The results of these measurements were interpreted to suggest that much, and perhaps all, of the F(-)-sensitive acid phosphatase activity in motion in peripheral nerve in rat is confined to sensory axons.
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PMID:Transported enzymes in sciatic nerve and sensory ganglia of rats exposed to maternal antibodies against nerve growth factor. 616 7

The paper is concerned with the effect antibrain antiserum may exert on the activity of succinic dehydrogenase, glutamic dehydrogenase, cytochrome oxidase, and peroxidase. By means of quantitative cytochemistry and electron microscopy it was demonstrated that activity of succinic dehydrogenase activity or cytochrome oxidase increased in the cortex and hypothalamus following the injection of anti-cortex or anti-hypothalamic serum. There were no changes of glutamic dehydrogenase and peroxidase found. Nonspecific alterations of neuronal fine structures were observed in both the cortex and the hypothalamus of rabbits treated with antiserum.
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PMID:The influence of antibrain antibodies on the level of enzyme activity and ultrastructure of brain. 626 73


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