The K12 strain information can be found on the UniProt website under the following entry: P0A9C5.
G1270
L-Glutamine Synthetase from Escherichia coli
lyophilized powder, 400-2,000 units/mg protein
Sinônimo(s):
L-Glutamate:ammonia ligase (ADP-forming)
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100 UNITS
R$ 5.312,00
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100 UNITS
R$ 5.312,00
About This Item
Número CAS:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.26
Produtos recomendados
Formulário
lyophilized powder
Nível de qualidade
atividade específica
400-2,000 units/mg protein
purificado por
affinity chromatography
contém
dithioerythritol as preservative
composição
Protein, ~5% Lowry
solubilidade
H2O: soluble 0.95-1.05 mg/mL, clear to hazy
nº de adesão UniProt
atividade externa
ATPase <0.2%
temperatura de armazenamento
−20°C
Informações sobre genes
Escherichia coli K12 ... glnA(948370)
Descrição geral
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.[1]
Aplicação
L-Glutamine Synthetase from Escherichia coli has been used in the synthesis of methylglutamine from methylammonium in E coli[2] and in the glutamine synthetase protection activity of human thioredoxin peroxidase enzyme, AOE372.[3]
L-Glutamine synthetase may be used for the purification of proteases from Escherichia coli.[4]
Ações bioquímicas/fisiológicas
L-glutamine synthetase catalyzes the condensation of L-glutamate and ammonia to L-glutamine[5]. It is a degradative enzyme for glutamic acid.
Nitrogen starvation dictates the expression of the glutamine synthetase (GS) gene in E. coli.[1] GS plays a key role in ammonia assimilation in bacteria.[6] Adenylylation of GS is catalyzed by adenylyltransferase. Adenylylation of GS modulates its catalytic functionality resulting in glutamine limitation in E coli.[7]
Degradative enzyme for glutamic acid
Definição da unidade
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
Palavra indicadora
Danger
Frases de perigo
Declarações de precaução
Classificações de perigo
Resp. Sens. 1
Código de classe de armazenamento
11 - Combustible Solids
Classe de risco de água (WGK)
WGK 1
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Equipamento de proteção individual
Eyeshields, Gloves, type N95 (US)
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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)
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
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
E Rodriguez et al.
Plant physiology and biochemistry : PPB, 62, 19-22 (2012-11-24)
Lead (Pb) is a toxic element, but its putative mutagenic effects in plant cells, using molecular markers, remain to unveil. To evaluate if Pb induces mutagenicity, Pisum sativum L. seedlings were exposed to Pb(2+) (up to 2000 mg L(-1)) for 28 days
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From which E. coli strain is your product G1270 L-Glutamine Synthetase from Escherichia coli isolated?
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