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:
UNSPSC Code:
12352204
NACRES:
NA.26
MDL number:
Specific activity:
400-2,000 units/mg protein
form
lyophilized powder
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
Quality Level
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
Degradative enzyme for glutamic acid
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.
Physical form
Contains potassium phosphate, sodium citrate and magnesium acetate buffer salts
Other Notes
One unit will convert 1.0 μmole of L-glutamate to L-glutamine in 15 min at pH 7.1 at 37 °C.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
常规特殊物品
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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)
Reversible Adenylylation of Glutamine Synthetase Is Dynamically Counterbalanced during Steady-State
Okano H, et al.
Journal of molecular biology, 404(1), 522-536 (2010)
Structure-function relationships of glutamine synthetases
Eisenberg D, et al.
Biochimica et Biophysica Acta, Protein Structure and Molecular Enzymology, 1477(1-2), 122-145 (2000)
Peng Jiang et al.
Biochemistry, 51(45), 9032-9044 (2012-10-24)
Uridylyltransferase/uridylyl-removing enzyme (UTase/UR) catalyzes uridylylation of PII and deuridylylation of PII-UMP, with both activities regulated by glutamine. In a reconstituted UTase/UR-PII cycle containing wild-type UTase/UR, the steady-state modification of PII varied from nearly complete modification to nearly complete demodification as
Jane E Ladner et al.
Biochemistry, 51(51), 10121-10123 (2012-12-14)
The structure of PA5508 from Pseudomonas aeruginosa, a glutamine synthetase (GS) homologue, has been determined at 2.5 Å. Surprisingly, PA5508 forms single hexameric rings rather than the stacked double rings that are characteristic of GS. The C-terminal helical thong motif
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