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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)

Three isozymes of glutamate dehydrogenase (GDH) of Chlamydomonas reinhardtii, induced under different trophic and stress conditions, have been purified about 800-1000-fold to electrophoretic homogeneity. They are hexamers of Mr 266,000-269,000 as deduced from gel filtration and sedimentation coefficient data. GDH1 consisted of six identical subunits of 44 kDa each, whereas both GDH2 and GDH3 consisted of six similar-sized monomers (4 of 44 kDa and 2 of 46 kDa). Optimum pH for the three activities with each pyridine nucleotide was identical (8.5 with NADH; 7.7 with NADPH; and 9.0 with NAD+). The isozymes exhibited similar high optimum temperature values (60-62 degrees C) and isoelectric points (7.9-8.1). Activity was enhanced in vitro by Ca2+ ions and strongly inhibited by pyridoxal 5'-phosphate, KCN, o-phenanthroline and EDTA, and to a lesser extent by pHMB and methylacetimidate. In the aminating reaction the three isozymes were inhibited in a concentration-dependent process by both NADH and NADPH, with apparent Km values for NH4+ ranging from 13-53 mM; 0.36-1.85 mM for 2-oxoglutarate and 0.07-0.78 mM for NADH and NADPH. In the deaminating reaction apparent Km values ranged from 0.64-3.52 mM for L-glutamate and 0.20-0.32 for NAD+. In addition, the three isozymes exhibited a non-hyperbolic kinetics for NAD+ with negative cooperativity (n = 0.8).
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PMID:Purification and properties of three NAD(P)+ isozymes of L-glutamate dehydrogenase of Chlamydomonas reinhardtii. 154 Jun 36

The patterns of alanine dehydrogenase, glutamate dehydrogenase and malate dehydrogenase activity were studied during the normal vegetative cell cycle and during the processes of gametic differentiation and dedifferentiation in synchronized cultures of Chlamydomonas reinhardtii. During all three phases of growth and differentiation the synthesis of DNA was also measured. During gametic differentiation all three enzyme levels were suppressed compared to vegetative cells although DNA and cell number were comparable. During gametic dedifferentiation no DNA synthesis occurred during the first 24 h cycle and only a doubling during the second. It was not until the third cycle that a normal 4-fold increase in DNA was observed. Cell number followed a similar pattern. Although the levels of alanine dehydrogenase and malate dehydrogenase were uniformly low during the first cycle when glutamate dehydrogenase increased 4-fold, during the second cycle the patterns of these enzymes changed markedly. The enzymes did not attain levels characteristic of vegetative cells until the third cycle.
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PMID:Changes in enzyme activity during differentiation in Chlamydomonas reinhardtii. 738 47

The intracellular localization of the activity and synthesis of three isozymes of NAD(P)(+)-glutamate dehydrogenase from the unicellular green alga Chlamydomonas reinhardtii cw-92 has been established. Isozyme activities have been located within mitochondria by using differential centrifugation techniques and discontinuous Percoll gradient separations. Experiments with protein synthesis inhibitors cycloheximide, rifampicin, chloramphenicol, and actinomycin D, under dark and carbon starvation conditions, revealed that synthesis of the three isozymes was likely to occur in cytosol as precursor proteins that are then transported and processed inside the mitochondria.
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PMID:Intracellular Localization of Three l-Glutamate Dehydrogenase Isozymes from Chlamydomonas reinhardtii. 1665 61

The responses of the wild type strain and of the y-2 mutant strain of Chlamydomonas reinhardi to long term organotrophic growth were studied. It was shown that wild type can be cultured as an organotroph for at least a month with little decrease in chlorophyll content and no loss of viability. On the other hand, the mutant strain y-2 dies during such organotrophic growth, death beginning after 5 to 6 days in the dark. The kinetics of death indicate that the loss of 95% of the chlorophyll precedes death and that revertants to wild type overgrow such a culture. The results suggest that death of y-2 is correlated with the loss of chlorophyll rather than simple metabolic response to organotrophy and that the chloroplast or a chloroplast related factor may perform certain nonphotosynthetic functions in C. reinhardi. The activities of nicotine adenine dinucleotide and nicotine adenine dinucleotide phosphate dependent triose phosphate dehydrogenases were studied during long term organotrophic growth of y-2. It was found that the activities of these enzymes varied in a manner consistent with previous findings under these conditions. The activity of glutamic dehydrogenase was found to vary as a function of chlorophyll content in the mutant strain y-2.
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PMID:Responses of a Mutant Strain of Chlamydomonas reinhardi to Prolonged Organotrophic Growth. 1665 94

The ammonium assimilatory enzymes glutamine synthetase (EC 6.3.1.2) and glutamate dehydrogenase (EC 1.4.1.3) were investigated for a possible role in the regulation of asparaginase (EC 3.5.1.1) in a Chlamydomonas species isolated from a marine environment. Cells grown under nitrogen limitation (0.1 millimolar NH(4) (+), NO(3) (-), or l-asparagine) possessed 6 times the asparaginase activity and approximately one-half the protein of cells grown at high nitrogen levels (1.5 to 2.5 millimolar). Biosynthetic glutamine synthetase activity was 1.5 to 1.8 times greater in nitrogen-limited cells than cells grown at high levels of the three nitrogen sources.Conversely, glutamate dehydrogenase (both NADH- and NADPH-dependent activities) was greatest in cells grown at high levels of asparagine or ammonium, while nitrate-grown cells possessed little activity at all concentrations employed. For all three nitrogen sources, glutamate dehydrogenase activity was correlated to the residual ammonium concentration of the media after growth (r = 0.88 and 0.94 for NADH- and NADPH-dependent activities, respectively).These results suggest that glutamate dehydrogenase is regulated in response to ambient ammonium levels via a mechanism distinct from asparaginase or glutamine synthetase. Glutamine synthetase and asparaginase, apparently repressed by high levels of all three nitrogen sources, are perhaps regulated by a common mechanism responding to intracellular nitrogen depletion, as evidenced by low cellular protein content.
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PMID:Regulation of asparaginase, glutamine synthetase, and glutamate dehydrogenase in response to medium nitrogen concentrations in a euryhaline chlamydomonas species. 1666 9

Two hours after the addition of l-methionine-dl-sulfoximine to the cell suspension, glutamine synthetase activity was inhibited by more than 90% in air-grown Chlamydomonas reinhardii. Cells continued to take up NH(3) from the medium provided that the concentration of dissolved CO(2) was high (equilibrated with 4% CO(2) in air). This NH(3) uptake, about 30% of the control, is discussed in terms of glutamate dehydrogenase activity. Without CO(2), or with a low CO(2) level, a NH(3) excretion was observed, the rate of which depended on the actual concentration of the dissolved CO(2). Experiments with (15)NH(3) demonstrated that no NH(3) uptake was masked by this excretion and inversely that no excretion occurred during the uptake in the conditions where it took place. Furthermore, the NH(3) excretion observed in the absence of CO(2) increased when O(2) concentration rose to 15% and was inhibited when 10 millimolar isonicotinic acid hydrazide was supplied to the algal suspension. Thus, NH(3) excretion in the presence of l-methionine-dl-sulfoximine seems to be related to a photorespiratory process inasmuch as it presents the same properties with regard to the O(2) and the isonicotinic acid hydrazide effects. These results favor the hypothesis that NH(3) produced in the medium originates from the glycine to serine reaction. On the other hand, partial inhibition (50%) of photosynthesis by l-methionine-dl-sulfoximine was attributed to uncoupling between electron transfer and photophosphorylation due to NH(3) accumulation into the cell.
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PMID:Ammonia exchange and photorespiration in chlamydomonas. 1666 24

The specific activities of nitrate reductase, nitrite reductase, glutamine synthetase, glutamate synthase, and glutamate dehydrogenase were determined in intact protoplasts and intact chloroplasts from Chlamydomonas reinhardtii. After correction for contamination, the data were used to calculate the portion of each enzyme in the algal chloroplast. The chloroplast of C. reinhardtii contained all enzyme activities for nitrogen assimilation, except nitrate reductase, which could not be detected in this organelle. Glutamate synthase (NADH- and ferredoxin-dependent) and glutamate dehydrogenase were located exclusively in the chloroplast, while for nitrite reductase and glutamine synthetase an extraplastidic activity of about 20 and 60%, respectively, was measured. Cells grown on ammonium, instead of nitrate as nitrogen source, had a higher total cellular activity of the NADH-dependent glutamate synthase (+95%) and glutamate dehydrogenase (+33%) but less activity of glutamine synthetase (-10%). No activity of nitrate reductase could be detected in ammonium-grown cells. The distribution of nitrogen-assimilating enzymes among the chloroplast and the rest of the cell did not differ significantly between nitrate-grown and ammonium-grown cells. Only the plastidic portion of the glutamine synthetase increased to about 80% in cells grown on ammonium (compared to about 40% in cells grown on nitrate).
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PMID:Localization of Nitrogen-Assimilating Enzymes in the Chloroplast of Chlamydomonas reinhardtii. 1666 9