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G1270

Sigma-Aldrich

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:
9023-70-5
Enzyme Commission number:
6.3.1.2 (BRENDA, IUBMB)
MDL number:
MFCD00131463
UNSPSC Code:
12352204
NACRES:
NA.26

form

lyophilized powder

Quality Level

200

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.

P0A9C5

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

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H334

Precautionary Statements

P261 - P284 - P501

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)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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)
Structural Analysis of Glutamine Synthetase from Helicobacter pylori
Joo HK, et al.
Scientific Reports, 8(1), 11657-11657 (2018)
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)
Ammonia acquisition in enteric bacteria: physiological role of the ammonium/methylammonium transport B (AmtB) protein
Soupene E, et al.
Proceedings of the National Academy of Sciences of the USA, 95(12), 7030-7034 (1998)
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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