EC Number |
Application |
Reference |
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1.4.1.2 | 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 |
743232 |
1.4.1.2 | agriculture |
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 |
675147 |
1.4.1.2 | agriculture |
plays some role in triticale plants defence against effects of different types of environmental stresses |
671178 |
1.4.1.2 | analysis |
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 |
728042 |
1.4.1.2 | analysis |
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 |
728043 |
1.4.1.2 | analysis |
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 |
728040 |
1.4.1.2 | analysis |
the protein that reacts in commercial latex tests for Clostridium difficile is a glutamate dehydrogenase |
728039 |
1.4.1.2 | biotechnology |
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 |
696792 |
1.4.1.2 | biotechnology |
method describes immobilization of enzymes by the maximum amount of subunits and rigidification of the enzyme subunits involved in the immobilization |
697661 |
1.4.1.2 | biotechnology |
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 |
696792 |