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
Synonym(s):
L-Glutamate:ammonia ligase (ADP-forming)
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100 UNITS
$612.75
About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.26
$612.75
List price$645.00Save 5%Web-Only Promotion
Available to ship onApril 07, 2025Details
Request a Bulk Order
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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.[1]
Application
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]
Biochem/physiol Actions
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
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
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Reversible Adenylylation of Glutamine Synthetase Is Dynamically Counterbalanced during Steady-State
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Journal of molecular biology, 404(1), 522-536 (2010)
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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
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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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