Results 111 to 120 of about 83,270 (165)

Glutamate synthase and nitrogen assimilation

Trends in Plant Science, 1998
The assimilation of ammonia by a wide variety of organisms is the primary route for the introduction of nitrogen into the biosphere. The assimilatory enzymes glutamine synthetase and glutamate synthase catalyze reactions that convert α-ketoglutarate and ammonia to glutamate, which is then used in a wide variety of biosynthetic reactions.
Stephen J. Temple, Carroll P. Vance, J. Stephen Gantt   +2 more
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Human cytosolic folylpoly-γ-glutamate synthase

1997
Publisher Summary This chapter describes the expression of human folylpolyglutamate synthase (FPGS) in Escherichia coli and the purification and properties of the enzyme. Folylpolyglutamate synthase activity is normally measured by the incorporation of [ 14 C]glutamate into folylpolyglutamate products using (6ambo)-H 4 PteGlu as the substrate ...
I, Atkinson, T, Garrow, A, Brenner, B, Shane   +3 more
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Glutamate synthase and the synthesis of glutamate in plants

Plant Physiology and Biochemistry, 2003
The discovery of glutamate synthases (E.C. 1.4.1.13 and E.C. 1.4.7.1) caused a major re-assessment of the way in which ammonium is assimilated in bacteria and higher plants. The history of that discovery is reviewed and considered in the light of recent developments in the biochemistry and genetics of the higher plant ferredoxin- and NADH-dependent ...
Lea, Peter John, Miflin, Ben J.
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Glutamate synthase: a fascinating pathway from L-glutamine to L-glutamate

Cellular and Molecular Life Sciences (CMLS), 2004
Glutamate synthase is a multicomponent iron-sulfur flavoprotein belonging to the class of N-terminal nucleophile amidotransferases. It catalyzes the conversion of L-glutamine and 2-oxoglutarate into two molecules of L-glutamate. In recent years the X-ray structures of the ferredoxin-dependent glutamate synthase and of the a subunit of the NADPH ...
R. H. H. van den Heuvel, B. Curti, M.A. Vanoni, A. Mattevi   +3 more
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Mechanistic studies on Azospirillum brasilense glutamate synthase

Biochemistry, 1991
The reaction mechanism of Azospirillum brasilense glutamate synthase has been investigated by several approaches. 15N nuclear magnetic resonance studies demonstrate that the amide nitrogen of glutamine is reductively transferred to 2-oxoglutarate in an irreversible manner with no release of the transferred ammonia group into the medium.
M A, Vanoni, D E, Edmondson, M, Rescigno, G, Zanetti, B, Curti   +4 more
openaire   +2 more sources

Glutamate synthase: a complex iron-sulfur flavoprotein

Cellular and Molecular Life Sciences (CMLS), 1999
Glutamate synthase is a complex iron-sulfur flavoprotein that forms L-glutamate from L-glutamine and 2-oxoglutarate. It participates with glutamine synthetase in ammonia assimilation processes. The known structural and biochemical properties of glutamate synthase from Azospirillum brasilense, a nitrogen-fixing bacterium, will be discussed in comparison
M A, Vanoni, B, Curti
openaire   +2 more sources

Glutamate synthase is plastid-encoded in a red alga: implications for the evolution of glutamate synthases

Plant Molecular Biology, 1993
An actively transcribed gene (glsF) encoding for ferredoxin-dependent glutamate synthase (Fd-GOGAT) was found on the plastid genome of the multicellular red alga Antithamnion sp. Fd-GOGAT is not plastid-encoded in chlorophytic plants, demonstrating that red algal plastid genomes encode for additional functions when compared to those known from green ...
K, Valentin, M, Kostrzewa, K, Zetsche
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Ligh-dependent activity of glutamate synthase in vitro

Biochemical and Biophysical Research Communications, 1982
Abstract Glutamate synthase from rice (Oryza sativa) green leaves was assayed in a chloroplast reconstituted system. The enzyme activity was totally dependent on externally supplied thylakoid membranes and ferredoxin in the light. Glutamate synthase activity was also detected from etiolated leaves with photoreduced ferredoxin as an electron donor.
A, Suzuki, J P, Jacquot, F, Martin, P, Gadal   +3 more
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Affinity purification of glutamate synthase from Escherichia coli

Analytical Biochemistry, 1980
Abstract A method is described for the affinity purification of the NADPH-dependent glutamate synthase from Escherichia coli . Enzyme partially purified by ammonium sulfate precipitation and gel filtration was chromatographed on 2′,5′-ADP-Sepharose. Glutamate synthase was eluted specifically from this adsorbent by a low concentration of NADPH.
C N, Schmidt, L, Jervis
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Regulation of glutamate synthase from Bacillussubtilis by Glutamine

Biochemical and Biophysical Research Communications, 1980
Abstract Glutamate synthase, an important enzyme in the assimilation of ammonia, was measured in cultures of Bacillus subtilis grown with different nitrogen sources. An attempt was made to correlate the specific activity to the intracellular levels of five metabolites of glutamate metabolism: aspartate, glutamate, glutamine, alanine and NH
K L, Desphande, J R, Katze, J F, Kane
openaire   +2 more sources