G1270
L-Glutamine Synthetase from Escherichia coli
lyophilized powder, 400-2,000 units/mg protein
Sinónimos:
L-Glutamate:ammonia ligase (ADP-forming)
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About This Item
Número de CAS:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.26
Productos recomendados
Formulario
lyophilized powder
Nivel de calidad
actividad específica
400-2,000 units/mg protein
purificado por
affinity chromatography
contiene
dithioerythritol as preservative
composición
Protein, ~5% Lowry
solubilidad
H2O: soluble 0.95-1.05 mg/mL, clear to hazy
Nº de acceso UniProt
actividad extraña
ATPase <0.2%
temp. de almacenamiento
−20°C
Información sobre el gen
Escherichia coli K12 ... glnA(948370)
Descripción general
L-Glutamine Synthetase from bacteria shows dodecameric structure comprising of 12 active sites. Each active site termed bifunnel, has an ATP and glutamate binding sites. The dodecamer is stabilized by two hexameric rings.
Aplicación
L-Glutamine Synthetase from Escherichia coli has been used in the synthesis of methylglutamine from methylammonium in E coli and in the glutamine synthetase protection activity of human thioredoxin peroxidase enzyme, AOE372.
L-Glutamine synthetase may be used for the purification of proteases from Escherichia coli.
Acciones bioquímicas o fisiológicas
L-glutamine synthetase catalyzes the condensation of L-glutamate and ammonia to L-glutamine. It is a degradative enzyme for glutamic acid.
Nitrogen starvation dictates the expression of the glutamine synthetase (GS) gene in E. coli. GS plays a key role in ammonia assimilation in bacteria. Adenylylation of GS is catalyzed by adenylyltransferase. Adenylylation of GS modulates its catalytic functionality resulting in glutamine limitation in E coli.
Degradative enzyme for glutamic acid
Definición de unidad
One unit will convert 1.0 μmole of L-glutamate to L-glutamine in 15 min at pH 7.1 at 37 °C.
Forma física
Contains potassium phosphate, sodium citrate and magnesium acetate buffer salts
Palabra de señalización
Danger
Frases de peligro
Consejos de prudencia
Clasificaciones de peligro
Resp. Sens. 1
Código de clase de almacenamiento
11 - Combustible Solids
Clase de riesgo para el agua (WGK)
WGK 1
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Equipo de protección personal
Eyeshields, Gloves, type N95 (US)
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Los clientes también vieron
Reversible Adenylylation of Glutamine Synthetase Is Dynamically Counterbalanced during Steady-State
Okano H, et al.
Journal of molecular biology, 404(1), 522-536 (2010)
Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation
Jin DY, et al.
The Journal of Biological Chemistry, 272(49), 30952-30961 (1997)
S H Liaw et al.
Protein science : a publication of the Protein Society, 4(11), 2358-2365 (1995-11-01)
Glutamine synthetase (GS) catalyzes the ATP-dependent condensation of ammonia and glutamate to yield glutamine, ADP, and inorganic phosphate in the presence of divalent cations. Bacterial GS is an enzyme of 12 identical subunits, arranged in two rings of 6, with
Kamal Krishna Singh et al.
Plant cell reports, 32(2), 183-193 (2012-10-17)
KEY MESSAGE : The regulation of GS isoforms by WD was organ specific. Two GS isoforms i.e. OsGS1;1 and OsGS2 were differentially regulated in IR-64 (drought-sensitive) and Khitish (drought-tolerant) cultivars of rice. Water deficit (WD) has adverse effect on rice
Purification of a protease from Escherichia coli with specificity for oxidized glutamine synthetase.
J E Roseman et al.
The Journal of biological chemistry, 262(5), 2101-2110 (1987-02-15)
A soluble Escherichia coli protease has been identified and purified to homogeneity. The protease cleaves glutamine synthetase which has been modified by mixed function oxidation; native glutamine synthetase is not a substrate. Using [14C]glutamine synthetase as a substrate (prepared by
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