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drug development
although AtGDH1 is insensitive to MPD in activity assays, several (+/-)-2-methyl-2,4-pentanediol (MPD) binding sites with conserved sequence are identified and the observation of druggable sites opens a potential for non-competitive herbicide design
energy production
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a bio-anode using L-glutamate as the fuel is constructed. To oxidize L-glutamate at the anode, glutamate dehydrogenase, derived from Pyrobaculum islandicum, and proline dehydrogenase derived from Pyrococcus horikoshii, are immobilized for a two-enzyme conjugate enzymatic and redox reaction. To achieve an efficient enzyme reaction and electron transfer, the immobilization ratio of proline dehydrogenase to glutamate dehydrogenase is controlled by varying the molar ratios of dithiobis succinimidyl undecanoate and nitrilotriacetic acid dihydrochloride
agriculture
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GDH genes involved in leaf senescence are also a component of the plant defence response during plantpathogen interaction, GDH behaves like a non-specific stress-related gene
agriculture
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plays some role in triticale plants defence against effects of different types of environmental stresses
agriculture
a high-copy number of the GDH2-encoded NADH-specific glutamate dehydrogenase gene stimulates growth at 15°C, while overexpression of NADPH-specific GDH1 has detrimental effects. Total cellular NAD levels are a limiting factor for growth at low temperature in Saccharomyces cerevisiae. Increasing NADH oxidation by overexpression of GDH2 may help to avoid perturbations in the redox metabolism induced by a higher fermentative/oxidative balance at low temperature. Overexpression of GDH2 increases notably the cold growth in the wine yeast strain QA23 in both standard growth medium and synthetic grape must
analysis
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evaluation of the C.Diff Quik Chek Complete Assay which tests for the presence of both glutamate dehydrogenase and toxins A and B. The assay allows 88% of specimens to be accurately screened as either positive or negative for the presence of toxigenic Clostridium difficile in less than 30 min and with minimal hands-on time. Use of a random-access PCR for the analysis of specimens with discrepant allows the easy, rapid, and highly sensitive and specific diagnosis of Clostridium difficile disease
analysis
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gluD gene encoding glutamate dehydrogenase is highly conserved and glutamate dehydrogenase, which is used as marker for the presence of Clostridium difficile in fecal specimens, is readily expressed in vitro by all 77 Clostridium difficile ribotypes assayed. All ribotypes, including ARL 002, ARL 027, and ARL 106, are reactive in assays that detect Clostridium difficile glutamate dehydrogenase
analysis
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the latex test-reactive protein is a glutamate dehydrogenase present in all isolates of Peptoclostridium difficile analyzed, suggesting that it is not related to pathogenicity
analysis
the protein that reacts in commercial latex tests for Clostridium difficile is a glutamate dehydrogenase
biotechnology
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a strategy to control flocculation is investigated using dimorphic yeast, Benjaminiella poitrasii as a model. Parent form of this yeast (Y) exhibit faster flocculation (11.1 min) than the monomorphic yeast form mutant Y-5 (12.6 min). Flocculation of both Y and Y-5 can be altered by supplementing either substrates or inhibitor of NAD-glutamate dehydrogenase (NAD-GDH) in the growth media. The rate of flocculation is promoted by alpha-ketoglutarate or isophthalic acid and decelerated by glutamate with a statistically significant inverse correlation to corresponding NAD-GDH levels. This opens up new possibilities of using NAD-GDH modulating agents to control flocculation in fermentations for easier downstream processing
biotechnology
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method describes immobilization of enzymes by the maximum amount of subunits and rigidification of the enzyme subunits involved in the immobilization
biotechnology
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the rate of flocculation is promoted by a-ketoglutarate or isophthalic acid and decelerated by glutamate with a statistically significant inverse correlation to corresponding NAD-GDH levels. These interesting findings open up new possibilities of using NAD-GDH modulating agents to control flocculation in fermentations for easier downstream processing
degradation
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at high salinity glutamate seems to be preferentially produced through the process catalyzed by NADH-GDH, whereas GS-catalysis might be the main glutamate synthesis pathway under low salinity
degradation
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clarification of the in vivo direction of the reaction catalyzed by GDH isoenzyme 1, the enzyme catabolizes L-glutamate in roots, and does not assimilate NH4+ in source leaves
diagnostics
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GDH electrophoretic type (ETs) and sequence types may serve as useful markers in predicting the pathogenic behavior of strains of this serotype and that the molecular basis for the observed differences in the ETs is amino acid substitutions and not deletion, insertion, or processing uniqueness
diagnostics
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GLDH, gama-glutamyltransferase, aspartate-aminotransferase, alanine-aminotransferase and erythrocyte mean cell volume are assessed in 238 alcoholics admitted to hospital: on admission, after 24 h and after 7 days. All the values are significantly higher than those in healthy persons. The fastest activity decrease is seen in GLDH. The kinetics of GLDH and aspartate-aminotranferase are more applicable than gama-glutamyltransferase kinetics after a week, but GLDH kinetics are most reliable. GLDH is the most specific laboratory marker with almost 90% specificity. The sensitivity of combination erythrocyte mean cell volume and GLDH kinetics after 1 week of abstinence is pathognomonic by 97.2%. GLDH is an equally accurate marker of alcoholism in comparison to others
food industry
plays an essential role during postharvest senescence, its expression most likely is controlled by multigenes and regulated either transcriptionally or posttranscriptionally
food industry
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Lactococcus lactis IFPL 953 shows the highest NAD-GDH activity among wild isolates from raw milk cheeses. L. lactis IFPL 953 also demonstrates a remarkable 2-oxoisovalerate decarboxylase activity, which along with its high GDH activity makes the strain particularly useful in enhancing cheese flavour formation
food industry
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Lactococcus lactis IFPL 953 shows the highest NAD-GDH activity among wild isolates from raw milk cheeses. L. lactis IFPL 953 also demonstrates a remarkable 2-oxoisovalerate decarboxylase activity, which along with its high GDH activity makes the strain particularly useful in enhancing cheese flavour formation
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medicine
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prolonged exposure to Corydalis ternata may be one of the ways to regulate glutamate concentration in brain through the activation of GDH
medicine
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the findings emphasize the integration of glucose metabolism, glutamine metabolism, and oncogenic signaling in glioblastoma cells and suggest that exploiting compensatory pathways of glutamine metabolism can improve the efficacy of cancer treatments that impair glucose utilization
medicine
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evaluation of comercially available rapid membrane enzyme immunoassays that use either glutamate dehydrogenase antigen or toxin A and B detection or a combination of both. Sensitivity, specificity, positive predictive values, and negative predictive values are 63.6%, 98.0%, 76.1%, and 96.4%, respectively, for the CD COMPLETE-toxin assay and 75.5%, 97.4%, 72.5%, and 97.8%, respectively, for the VIDAS CDAB assay. In comparison to the enriched Clostridium difficile cultures, the sensitivity, specificity, positive predictive values, and negative predictive values for the CD COMPLETE-GDH assay are 91.0%, 92.4%, 70.5%, and 98.1%, respectively. The CD COMPLETE assay is a reliable method for the diagnosis of Costridium difficile infection and provides greater sensitivity than toxin enzyme immunoassay alone
medicine
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gluD gene encoding glutamate dehydrogenase is highly conserved and glutamate dehydrogenase, which is used as marker for the presence of Clostridium difficile in fecal specimens, is readily expressed in vitro by all 77 Clostridium difficile ribotypes assayed. All ribotypes, including ARL 002, ARL 027, and ARL 106, are reactive in assays that detect Clostridium difficile glutamate dehydrogenase
medicine
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the latex test-reactive protein is a glutamate dehydrogenase present in all isolates of Peptoclostridium difficile analyzed, suggesting that it is not related to pathogenicity
molecular biology
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GDH is essential for the full development of the secretory response in beta-cells
molecular biology
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GDH, in conjunction with NADH-glutamte synthase, contributes to the control of leaf glutamate homeostasis, an amino acid that plays a central signaling and metabolic role at the interface of the carbon and nitrogen assimilatory pathways
synthesis
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produktion of L-ornithine in Corynebacterium glutamicum SNK118, by deletion of genes argF, argR, and ncgl2228 to block the degradation of L-ornithine, and overexpression of NADP-dependent glyceraldehyde 3-phosphate dehydrogenases gene from Clostridium saccharobutylicum and glutamate dehydrogenase RocG. In fed-batch fermentation, L-ornithine of 88.26 g/l with productivity of 1.23 g/l/h (over 72 h) and yield of 0.414 g/g glucose are achieved by the final strain in a 10-l bioreactor
synthesis
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produktion of L-ornithine in Corynebacterium glutamicum SNK118, by deletion of genes argF, argR, and ncgl2228 to block the degradation of L-ornithine, and overexpression of NADP-dependent glyceraldehyde 3-phosphate dehydrogenases gene from Clostridium saccharobutylicum and glutamate dehydrogenase RocG. In fed-batch fermentation, L-ornithine of 88.26 g/l with productivity of 1.23 g/l/h (over 72 h) and yield of 0.414 g/g glucose are achieved by the final strain in a 10-l bioreactor
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additional information
GDH gene expression and translation are apparently subject to complex regulation
additional information
GDH gene expression and translation are apparently subject to complex regulation
additional information
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GDH gene expression and translation are apparently subject to complex regulation
additional information
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glutamine synthetase-GOGAT pathway and GDH play distinct roles in the source-sink nitrogen cycle of tobacco leaves, regardless of leaf age, [15N]ammonium does not depend on GDH
additional information
high sequence similarity to GDH genes from the Bacteroides, GDH is an anabolic enzyme catalysing the assimilation of ammonia by Entodinium caudatum in the rumen, the gene is probably acquired by lateral gene transfer from a ruminal bacterium
additional information
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high sequence similarity to GDH genes from the Bacteroides, GDH is an anabolic enzyme catalysing the assimilation of ammonia by Entodinium caudatum in the rumen, the gene is probably acquired by lateral gene transfer from a ruminal bacterium
additional information
induction of GDH1 and GDH2 transcripts along the root do not coincide with that of NADH-GOGAT expression
additional information
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induction of GDH1 and GDH2 transcripts along the root do not coincide with that of NADH-GOGAT expression
additional information
large modulation of GDH beta-subunit titre does not affect plant viability under ideal growing conditions, GDH gene expression and translation are apparently subject to complex regulation
additional information
large modulation of GDH beta-subunit titre does not affect plant viability under ideal growing conditions, GDH gene expression and translation are apparently subject to complex regulation
additional information
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large modulation of GDH beta-subunit titre does not affect plant viability under ideal growing conditions, GDH gene expression and translation are apparently subject to complex regulation
additional information
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possible role of enzyme under Hg-stress
additional information
Q144R can be used as a template gene to modify the substrate specificity of Bacillus subtilis GluDH for industrial use
additional information
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Q144R can be used as a template gene to modify the substrate specificity of Bacillus subtilis GluDH for industrial use
additional information
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reactivation of D165N is a consequence of the catalytic chemistry of the enzymes active site
additional information
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shift in GDH cellular compartmentation is important during leaf nitrogen remobilization
additional information
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subunit rearrangement, i.e., a change in the quaternary structure of the hexameric recombinant GDH, is essential for activation of the enzyme
additional information
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Q144R can be used as a template gene to modify the substrate specificity of Bacillus subtilis GluDH for industrial use
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