G3144
L-Glutamine Synthetase from Escherichia coli W, ATCC No. 9637
Protein ≥30 % by biuret, lyophilized powder
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
specific activity
100-400 units/mg protein
composition
Protein, ≥30% biuret
solubility
H2O: soluble 0.95-1.05 mg/mL, clear to slightly hazy
UniProt accession no.
storage temp.
−20°C
Gene Information
Escherichia coli K12 ... glnA(948370)
Application
L-Glutamine synthetase may be used for the purification of proteases from Escherichia coli.[1]
Biochem/physiol Actions
Degradative enzyme for glutamic acid
L-glutamine synthetase catalyzes the condensation of L-glutamate and ammonia to L-glutamine[2]. It is a 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
Lyophilized powder containing buffer salts and stabilizer
Preparation Note
Grown in medium containing glucose and NH4Cl
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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H S Kingdon et al.
Journal of bacteriology, 94(4), 949-957 (1967-10-01)
The kinetic properties of Escherichia coli glutamine synthetase are markedly influenced by the manner in which the organism is grown. Enzyme obtained from stationary-phase cells grown on glycerol and glutamate is strongely inhibited by each of the eight feedback effectors
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
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
Lin Xu et al.
Antonie van Leeuwenhoek, 103(3), 559-565 (2012-11-13)
During a study of the diversity and phylogeny of rhizobia isolated from root nodules of Oxytropis ochrocephala grown in the northwest of China, four strains were classified in the genus Rhizobium on the basis of their 16S rRNA gene sequences.
Manuel A Matamoros et al.
The New phytologist, 197(3), 873-885 (2012-12-05)
Legume nodule senescence is a poorly understood process involving a decrease in N(2) fixation and an increase in proteolytic activity. Some physiological changes during nodule aging have been reported, but scarce information is available at the subcellular level. Biochemical, immunological
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