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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:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.26

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

Pictograms

Health hazard

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)

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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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)
Huijuan Jia et al.
Molecular nutrition & food research, 57(2), 291-306 (2012-11-21)
This study addresses the effects of branched-chain amino acids (BCAA) on global gene expression in liver and skeletal muscle and the molecular mechanisms underlying the improvement in liver cirrhosis using DNA microarray analysis combined with RNase protection assay. Male Wistar
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

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