G1270
L-Glutamine Synthetase from Escherichia coli
lyophilized powder, 400-2,000 units/mg protein
Synonym(s):
L-Glutamate:ammonia ligase (ADP-forming)
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.26
Recommended Products
form
lyophilized powder
Quality Level
specific activity
400-2,000 units/mg protein
purified by
affinity chromatography
contains
dithioerythritol as preservative
composition
Protein, ~5% Lowry
solubility
H2O: soluble 0.95-1.05 mg/mL, clear to hazy
UniProt accession no.
foreign activity
ATPase <0.2%
storage temp.
−20°C
Gene Information
Escherichia coli K12 ... glnA(948370)
General description
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.
Application
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.
Biochem/physiol Actions
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
Unit Definition
One unit will convert 1.0 μmole of L-glutamate to L-glutamine in 15 min at pH 7.1 at 37 °C.
Physical form
Contains potassium phosphate, sodium citrate and magnesium acetate buffer salts
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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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
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
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