The Experts below are selected from a list of 111 Experts worldwide ranked by ideXlab platform

G R Stewart - One of the best experts on this subject based on the ideXlab platform.

  • the role of Glutamate Dehydrogenase in plant nitrogen metabolism
    Plant Physiology, 1991
    Co-Authors: Sharon A Robinson, A P Slade, Richard Phillips, R G Ratcliffe, G R Stewart
    Abstract:

    In vivo nuclear magnetic resonance spectroscopy, in vitro gas chromatography-mass spectrometry, and automated 15N/13C mass spectrometry have been used to demonstrate that Glutamate Dehydrogenase is active in the oxidation of Glutamate, but not in the reductive amination of 2-oxogiutarate. In cell suspension cultures of carrot (Daucus carota L. cv Chantenay), primary assimilation of ammonium occurs via the Glutamate synthase pathway. Glutamate Dehydrogenase is derepressed in carbonlimited cells and in such cells the function of Glutamate Dehydrogenase appears to be the oxidation of Glutamate, thus ensuring sufficient carbon skeletons for effective functioning of the tricarboxylic acid cycle. This catabolic role for Glutamate Dehydrogenase implies an important regulatory function in carbon and nitrogen metabolism.

Sharon A Robinson - One of the best experts on this subject based on the ideXlab platform.

  • the role of Glutamate Dehydrogenase in plant nitrogen metabolism
    Plant Physiology, 1991
    Co-Authors: Sharon A Robinson, A P Slade, Richard Phillips, R G Ratcliffe, G R Stewart
    Abstract:

    In vivo nuclear magnetic resonance spectroscopy, in vitro gas chromatography-mass spectrometry, and automated 15N/13C mass spectrometry have been used to demonstrate that Glutamate Dehydrogenase is active in the oxidation of Glutamate, but not in the reductive amination of 2-oxogiutarate. In cell suspension cultures of carrot (Daucus carota L. cv Chantenay), primary assimilation of ammonium occurs via the Glutamate synthase pathway. Glutamate Dehydrogenase is derepressed in carbonlimited cells and in such cells the function of Glutamate Dehydrogenase appears to be the oxidation of Glutamate, thus ensuring sufficient carbon skeletons for effective functioning of the tricarboxylic acid cycle. This catabolic role for Glutamate Dehydrogenase implies an important regulatory function in carbon and nitrogen metabolism.

John D Helmann - One of the best experts on this subject based on the ideXlab platform.

  • Glutamate Dehydrogenase affects resistance to cell wall antibiotics in Bacillus subtilis
    Journal of Bacteriology, 2012
    Co-Authors: Yong Heon Lee, Anthony W. Kingston, John D Helmann
    Abstract:

    The Glutamate Dehydrogenase RocG of Bacillus subtilis is a bifunctional protein with both enzymatic and regulatory functions. Here we show that the rocG null mutant is sensitive to β-lactams, including cefuroxime (CEF), and to fosfomycin but that resistant mutants arise due to gain-of-function mutations in gudB, which encodes an otherwise inactive Glutamate Dehydrogenase. In the presence of CEF, ΔrocG ΔgudB mutant cells exhibit growth arrest when they reach mid-exponential phase. Using microarray-based transcriptional profiling, we found that the σ(W) regulon was downregulated in the ΔrocG ΔgudB null mutant. A survey of σ(W)-controlled genes for effects on CEF resistance identified both the NfeD protein YuaF and the flotillin homologue YuaG (FloT). Notably, overexpression of yuaFG in the rocG null mutant prevents the growth arrest induced by CEF. The YuaG flotillin has been shown previously to localize to defined lipid microdomains, and we show here that the yuaFGI operon contributes to a σ(W)-dependent decrease in membrane fluidity. We conclude that Glutamate Dehydrogenase activity affects the expression of the σ(W) regulon, by pathways that are yet unclear, and thereby influences resistance to CEF and other antibiotics.

Henry C. Reeves - One of the best experts on this subject based on the ideXlab platform.

  • Phosphorylation ofEscherichia coli NADP+-specific Glutamate Dehydrogenase
    Current Microbiology, 1991
    Co-Authors: Henry C. Reeves
    Abstract:

    Glutamate Dehydrogenase fromEscherichia coli is phosphorylated in vitro in an ATP-dependent enzymatic reaction. The phosphorylated protein, when exposed to acid conditions, releases the phosphate; this implies that the phosphorylation site is not on a serine, tyrosine, or threonine residue(s). Treatment of Glutamate Dehydrogenase with diethyl pyrocarbonate, a highly specific histidine-modifying reagent, blocks incorporation of32P-phosphate from [γ-32P]ATP into the enzyme, suggestive that the phosphorylation site is a histidine residue(s). The phosphorylated Glutamate Dehydrogenase was identified on the basis of its comigration with highly purified Glutamate Dehydrogenase, isolated fromE. coli, on denaturing, nondenaturing, and isoelectric focusing polyacrylamide gels and by sequence analysis.

Franz M Matschinsky - One of the best experts on this subject based on the ideXlab platform.