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Information on EC 6.3.1.2 - glutamine synthetase and Organism(s) Bacillus subtilis and UniProt Accession P12425
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6.3.1.2 glutamine synthetaseIUBMB Comments
Glutamine synthetase, which catalyses the incorporation of ammonium into glutamate, is a key enzyme of nitrogen metabolism found in all domains of life. Several types have been described, differing in their oligomeric structures and cofactor requirements.
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- 6.3.1.2
- aminotransferase
- gg
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- astrocyte
- nitrate
- bilirubin
- sulfoximine
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alt
- cerebral
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- retina
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fibrillary
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- glutaminase
- albumin
- transaminase
- creatinine
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adenylylation
- triglyceride
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astroglial
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neurotransmitter
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excitatory
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uric
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neurotoxicity
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glutamatergic
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hyperammonemia
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excitotoxicity
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- l-methionine
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periportal
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- cholestasis
- gamma-gt
-
photorespiratory
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n2-fixing
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pericentral
- gamma-glutamyltransferase
-
photorespiration
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corpuscular
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drinker
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assimilatory
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remobilization
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- pharmacology
- diagnostics
- heterocysts
- medicine
- analysis
The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
glutamine synthetase, gamma-glutamyl transferase, gs-ii, gsiii, taase, glna1, glna2, gln1;2, gln synthetase, gs(1), 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Chloroplast GS2
-
-
-
-
Clone lambda-GS28
-
-
-
-
Clone lambda-GS31
-
-
-
-
Clone lambda-GS8
-
-
-
-
Cytoplasmic GS3
-
-
-
-
Cytosolic GS1
-
-
-
-
Gln isozyme alpha
-
-
-
-
Gln isozyme beta
-
-
-
-
Gln isozyme gamma
-
-
-
-
Glutamate--ammonia ligase
-
-
-
-
glutamate-ammonia ligase
-
-
-
-
Glutamine synthetase
Glutamylhydroxamic synthetase
-
-
-
-
GS
-
-
-
-
GS(1)
-
-
-
-
GS1
-
-
-
-
GS107
-
-
-
-
GS112
-
-
-
-
GS117
-
-
-
-
GS122
-
-
-
-
GS2
-
-
-
-
GSI
-
-
-
-
GSII
-
-
-
-
GSIII
-
-
-
-
Isozyme delta
-
-
-
-
L-Glutamine synthetase
-
-
-
-
N47/N48
-
-
-
-
S2205/S2287
-
-
-
-
Synthetase, glutamine
-
-
-
-
Glutamine synthetase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
reaction mechanism
ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
structure-function relationship and catalytic mechanism, overview
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
L-glutamate:ammonia ligase (ADP-forming)
Glutamine synthetase, which catalyses the incorporation of ammonium into glutamate, is a key enzyme of nitrogen metabolism found in all domains of life. Several types have been described, differing in their oligomeric structures and cofactor requirements.
CAS REGISTRY NUMBER
COMMENTARY
9023-70-5
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
hydroxylamine + L-glutamine + ATP
L-gamma-glutamyl-hydroxamate + ammonium + ADP
gamma-glutamylhydroxamate synthetase activity
-
-
r
ATP + L-glutamate + hydroxylamine
ADP + phosphate + gamma-L-glutamyl hydroxamate
-
in presence of Mn2+
-
-
?
L-glutamine + hydroxylamine + ADP
gamma-glutamylhydroxamate + NH3 + ?
-
partial reverse reaction
-
-
?
L-glutamine + hydroxylamine + ADP
gamma-glutamylhydroxamate + NH4+ + ?
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
a two-step reaction with phosphorylation of L-glutamate by ATP to give gamma-glutamyl phosphate followed by addition of ammonia and release of phosphate resulting in L-glutamine, phosphate and ADP
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
the enzyme is involved in the regulation of the nitrogen metabolism, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
the enzyme is involved in the signal transduction for regulation of the nitrogen metabolism, overview
-
-
?
additional information
?
-
structure-activity relationship, overview
-
-
?
additional information
?
-
-
feedback-inhibited glutamine synthetase acts as a molecular chaperone to stabilize the association of dimers of transcripion factor GlnR, the repressor of the glutamine synthetase operon in Bacillus subtilis, with their DNA binding sites, molecular mechanism, overview. The cell shuts off synthesis of GS, and hence of glutamine, when both the enzyme and its product are in excess. The feedback-inhibited enzyme also regulates the activity of TnrA, the global regulator of nitrogen metabolism genes, but by a very different mechanism, overview
-
-
?
additional information
?
-
-
the glutamine synthetase transmits the nitrogen regulatory signal to GlnR, a transcription factor involved in nitrogen metabolism regulation, the enzyme interacts with GlnR via the factor's C-terminal autoinhibitory domain, the protein-protein interaction of GlnR and glutamine synthetase stabilizes the GlnR-DNA complexes, interaction analysis of enzyme with wild-type and truncated GlnR proteins, overview
-
-
?
additional information
?
-
-
the feedback-inhibited enzyme, acting as a chaperone, is required for the binding of transcription factor GlnR to DNA, the feedback inhibition of GS by L-glutamine induces the sequence-specific binding of transcription factor GlnR to DNA in nitrogen metabolism regulation by 32fold and reduces the dissociation rate by 18fold stabilizing the complexes, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
the enzyme is involved in the regulation of the nitrogen metabolism, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
the enzyme is involved in the signal transduction for regulation of the nitrogen metabolism, overview
-
-
?
additional information
?
-
-
feedback-inhibited glutamine synthetase acts as a molecular chaperone to stabilize the association of dimers of transcripion factor GlnR, the repressor of the glutamine synthetase operon in Bacillus subtilis, with their DNA binding sites, molecular mechanism, overview. The cell shuts off synthesis of GS, and hence of glutamine, when both the enzyme and its product are in excess. The feedback-inhibited enzyme also regulates the activity of TnrA, the global regulator of nitrogen metabolism genes, but by a very different mechanism, overview
-
-
?
additional information
?
-
-
the glutamine synthetase transmits the nitrogen regulatory signal to GlnR, a transcription factor involved in nitrogen metabolism regulation, the enzyme interacts with GlnR via the factor's C-terminal autoinhibitory domain, the protein-protein interaction of GlnR and glutamine synthetase stabilizes the GlnR-DNA complexes, interaction analysis of enzyme with wild-type and truncated GlnR proteins, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
Mn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
L-glutamine
feedback inhibition of isozymes GSI-alpha and GSI-beta. Feedback inhibition arises from a hydrogen bond network between Gln, the catalytic glutamate, and the GSI-alpha-specific residue, Arg62, from an adjacent subunit. Arg62 must be ejected for proper active site reorganization. An R62A mutation abrogates Gln feedback inhibition but does not affect catalysis
ATP
-
mutant S186F enzyme is resistant to feedback inhibition by glutamine and AMP
glutamine
-
feed-back inhibition of wild-type enzyme, mutant S186F enzyme is resistant to feedback inhibition
additional information
structure-activity relationships and inhibitor design, overview
-
L-glutamine
-
the enzyme is feedback inhibited, the feedback inhibition of GS induces the sequence-specific binding of transcription factor GlnR to DNA in nitrogen metabolism regulation by 32fold and reduces the dissociation rate by 18fold stabilizing the complexes, overview
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.2
ATP
pH 7.0, temperature not specified in the publication, mutant E304A
2.3
ATP
pH 7.0, temperature not specified in the publication, mutant R62A
2.4
ATP
pH 7.0, temperature not specified in the publication, wild-type enzyme
0.68
hydroxylamine
pH 7.0, temperature not specified in the publication, mutant E304A
0.83
hydroxylamine
pH 7.0, temperature not specified in the publication, wild-type enzyme
1.4
hydroxylamine
pH 7.0, temperature not specified in the publication, mutant R62A
1 - 4
L-glutamate
pH 7.0, temperature not specified in the publication, mutant R62A
3.4
L-glutamate
pH 7.0, temperature not specified in the publication, mutant E304A
27
L-glutamate
pH 7.0, temperature not specified in the publication, wild-type enzyme
0.18
NH3
pH 7.0, temperature not specified in the publication, wild-type enzyme
0.34
NH3
pH 7.0, temperature not specified in the publication, mutant R62A
32
NH3
pH 7.0, temperature not specified in the publication, mutant E304A
0.68
hydroxylamine
-
mutant E304H, 25°C, pH not specified in the publication
0.74
hydroxylamine
-
mutant E304D, 25°C, pH not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
L-methionine-S-sulfoximine
Bacillus subtilis
-
mutant Y303H, 25°C, pH not specified in the publication
0.1
L-methionine-S-sulfoximine
Bacillus subtilis
-
mutant Y303L, 25°C, pH not specified in the publication
0.12
L-methionine-S-sulfoximine
Bacillus subtilis
-
mutant V300A, 25°C, pH not specified in the publication
0.13
L-methionine-S-sulfoximine
Bacillus subtilis
-
wild-type, 25°C, pH not specified in the publication
0.25
L-methionine-S-sulfoximine
Bacillus subtilis
-
mutant P306A, 25°C, pH not specified in the publication
0.28
L-methionine-S-sulfoximine
Bacillus subtilis
-
mutant G302A, 25°C, pH not specified in the publication
0.61
L-methionine-S-sulfoximine
Bacillus subtilis
-
mutant Y303A, 25°C, pH not specified in the publication
2.7
L-methionine-S-sulfoximine
Bacillus subtilis
-
mutant A305G, 25°C, pH not specified in the publication
20
L-methionine-S-sulfoximine
Bacillus subtilis
-
mutant E304D, 25°C, pH not specified in the publication
26
L-methionine-S-sulfoximine
Bacillus subtilis
-
mutant E304A, 25°C, pH not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
glutamine synthetase plays essential roles in nitrogen metabolism
physiological function
-
glutathione synthetase binds to transcription factor TnrA in its feedback-inhibited form, and also in its non-feedback-inhibited form, although less efficiently. TnrA forms either a stable soluble complex with GlnK in the absence of transmembrane ammonium transporter AmtB, or constitutively binds to glutathione synthetase in the absence of regulatuor GlnK. In vitro, the TnrA C-terminus is responsible for interactions with either glutathione synthetase or GlnK, and this region appears also to mediate proteolysis, suggesting that binding of GlnK or glutathione synthetase protects TnrA from degradation
additional information
additional information
the Bacillus subtilis enzyme undergoes dramatic intersubunit conformational alterations during formation of the transition state. Structure-function relationship, overview
additional information
-
the Bacillus subtilis enzyme undergoes dramatic intersubunit conformational alterations during formation of the transition state. Structure-function relationship, overview
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70000
x * 70000, fusion-protein with SUMO-tag, SDS-PAGE and calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dodecamer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant detagged apo-enzyme, enzyme-glutamate-AMPPCP complex, and enzyme transition state, hanging drop vapor diffusion, for enzyme-glutamate-AMPPCP crystals: mixing of 40 mg/ml protein at a 1:1 ratio with 40% 4-methyl-2,4-pentanediol and 200 mM MgSO4, and inverting the drop over the reservoir solution containing 15% PEG 8000, 0.1 M HEPES, pH 7.5, and 10 mM MgCl2, for enzyme-L-methionine-S-sulfoximine-phosphate-ADP crystals: mixing of 40 mg/ml protein with 5 mM MgCl2, 5 mM ATP, and 5 mM L-methionine-S-sulfoximine,and combining in a 1:1 ratio with crystallization reagent containing 10% PEG 4000, 0.1 M HEPES, pH 7.5, for apo-enzyme crystals: mixing the protein 40 mg/ml at a 1:1 ratio with 40% 4-methyl-2,4-pentanediol and 200 mM MgSO4 and inverting the drop over the reservoir solution, room temperature, X-ray diffraction structure determination and analysis at 3.1 A, 2.87 A, and 2.58 A resolution, respectively
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E304A/A305G
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R62A
site-directed mutagenesis, the mutation abrogates Gln feedback inhibition but does not affect catalysis
A305G
-
mutation in the E304 flap, a flexible 7-residue loop over the entrance to the active site. 16% of wild-type activity with L-glutamate, 2% of wild-type activity with L-glutamine
E304D
-
mutation in the E304 flap, a flexible 7-residue loop over the entrance to the active site. 37% of wild-type activity with L-glutamate, 8% of wild-type activity with L-glutamine
E304H
-
mutation in the E304 flap, a flexible 7-residue loop over the entrance to the active site. 43% of wild-type activity with L-glutamate, 5% of wild-type activity with L-glutamine
E424K
-
the mutant enzyme is defective in its ability to interact with GlnR
G302A
-
mutation in the E304 flap, a flexible 7-residue loop over the entrance to the active site. 80% of wild-type activity with L-glutamate, 58% of wild-type activity with L-glutamine
P306A
-
mutation in the E304 flap, a flexible 7-residue loop over the entrance to the active site. 160% of wild-type activity with L-glutamate, 130% of wild-type activity with L-glutamine
S186F
V300A
-
mutation in the E304 flap, a flexible 7-residue loop over the entrance to the active site. 76% of wild-type activity with L-glutamate, 18% of wild-type activity with L-glutamine
Y303A
-
mutation in the E304 flap, a flexible 7-residue loop over the entrance to the active site. 36% of wild-type activity with L-glutamate, 8% of wild-type activity with L-glutamine
Y303H
-
mutation in the E304 flap, a flexible 7-residue loop over the entrance to the active site. 150% of wild-type activity with L-glutamate, 100% of wild-type activity with L-glutamine
Y303L
-
mutation in the E304 flap, a flexible 7-residue loop over the entrance to the active site. 87% of wild-type activity with L-glutamate, 46% of wild-type activity with L-glutamine
S186F
-
kinetic properties are similar to the wild-type protein, mutant S186F enzyme is resistant to feedback inhibition by glutamine and AMP. S186F protein has a lower affinity for glutamine and AMP than the wild-type enzyme. S186F glutamine synthetase is defective in its ability to block DNA binding by TnrA in vitro
S186F
-
the mutant enzyme is defective in its ability to interact with GlnR
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
EDTA and EGTA stabilize. The combination of substrates, Mn2+, ATP and PMSF
-
inactivation by trypsin, chymotrypsin, or subtilisin follows pseudo-fast order kinetics. In presence of Glu, ATP, and Mn2+ the digestion of the glutamine synthetase by each of the three proteases is retarded completely
-
native and oxidized forms of enzyme are both cleaved in the same manner by chymotrypsin. Oxidized enzyme is completely cleaved during the 60 min incubation whereas the native enzyme is not completely digested
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme is protected from oxidative modification by either 5 mM Mn2+ or 5 mM Mn2+ plus 5 mM ATP, but not by Mg2+. Oxidative modification induces relatively subtle changes in the dodecameric enzyme molecules, but does not denature the protein
-
37531
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography, urea treatment, tag cleavage by thrombin, again nickel affinity chromatography to remove the tag, and dialysis
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
coupling genetically engineered Bacillus subtilis glutamine synthetase with yeast alcoholic fermentation system using small ubiquitin-related modifier fusion technology SUMO
recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli
functional overexpression in Escherichia coli BL21 (DE3), expression analysis
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
the GSI-alpha-specific regulatory network can be exploited for inhibitor design against Gram-positive pathogens
synthesis
high efficiency L-Gln production by coupling genetically engineered Bacillus subtilis glutamine synthetase with yeast alcoholic fermentation system using small ubiquitin-related modifier fusion technology SUMO and 0.1% lactose as inducer. Fusion protein is expressed in totally soluble form in Escherichia coli and can be purified to 90% purity by nickel nitrilo-triacetic acid resin chromatography with a yield of 625 mg per liter fermentation culture. About 121 mg recombinant GS is obtained from 1 l fermentation culture with 96% purity and 23 U/mg activity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kimura, K.; Sugano, S.
Inactivation of Bacillus subtilis glutamine synthetase by metal-catalyzed oxidation
J. Biochem.
112
828-833
1992
Bacillus subtilis, Bacillus subtilis KN2
Tanaka, E.V.; Kimura, K.
Identification of amino acid residues modified by two ATP analogs in Bacillus subtilis glutamine synthetase
J. Biochem.
110
780-784
1991
Bacillus subtilis
Kimura, K.; Sugano, S.; Funae, A.; Nakano, Y.
Characterization of Bacillus subtilis glutamine synthetase by limited proteolysis
J. Biochem.
110
526-531
1991
Bacillus subtilis
Wray, L.V., Jr.; Fisher, S.H.
A feedback-resistant mutant of Bacillus subtilis glutamine synthetase with pleiotropic defects in nitrogen-regulated gene expression
J. Biol. Chem.
280
33298-33304
2005
Bacillus subtilis
Hong, N.N.; Yang, G.; Li, J.; Zhang, Y.P.; Li, J.L.
Rapid determination of L-glutamine using engineered Escherichia coli overexpressing glutamine synthetase
Appl. Biochem. Biotechnol.
158
398-407
2008
Bacillus subtilis
Berlicki, L.
Inhibitors of glutamine synthetase and their potential application in medicine
Mini Rev. Med. Chem.
8
869-878
2008
Beta vulgaris, Bradyrhizobium japonicum, Chlorella sp., Columba sp., Escherichia coli, Ovis aries, Hordeum vulgare, Hordeum vulgare (P13564), Oryza sativa, Vigna radiata, Pisum sativum, Sorghum sp., Spinacia oleracea, Triticum aestivum, Zea mays, Senna obtusifolia, Rattus norvegicus (P09606), Salmonella enterica subsp. enterica serovar Typhimurium (P0A1P6), Bacillus subtilis (P12425), Homo sapiens (P15104), Mus musculus (P15105), Synechocystis sp. (P77961), Mycobacterium tuberculosis (P9WN39), Mycobacterium tuberculosis H37Rv (P9WN39)
Sonenshein, A.L.
Control of nitrogen metabolism by Bacillus subtilis glutamine synthetase
Mol. Microbiol.
68
242-245
2008
Bacillus subtilis
-
Wray, L.V.; Fisher, S.H.
Bacillus subtilis GlnR contains an autoinhibitory C-terminal domain required for the interaction with glutamine synthetase
Mol. Microbiol.
68
277-285
2008
Bacillus subtilis
Fisher, S.H.; Wray, L.V.
Bacillus subtilis glutamine synthetase regulates its own synthesis by acting as a chaperone to stabilize GlnR-DNA complexes
Proc. Natl. Acad. Sci. USA
105
1014-1019
2008
Bacillus subtilis
Kayumov, A.; Heinrich, A.; Fedorova, K.; Ilinskaya, O.; Forchhammer, K.
Interaction of the general transcription factor TnrA with the PII-like protein GlnK and glutamine synthetase in Bacillus subtilis
FEBS J.
278
1779-1789
2011
Bacillus subtilis
Wray, L.V.; Fisher, S.H.
Functional roles of the conserved Glu304 loop of Bacillus subtilis glutamine synthetase
J. Bacteriol.
192
5018-5025
2010
Bacillus subtilis
Wang, Q.; Min, C.; Yan, T.; Pu, H.; Xin, Y.; Zhang, S.; Luo, L.; Yin, Z.
Production of glutamine synthetase in Escherichia coli using SUMO fusion partner and application to L-glutamine synthesis
World J. Microbiol. Biotechnol.
27
2603-2610
2011
Bacillus subtilis (P12425)
Murray, D.S.; Chinnam, N.; Tonthat, N.K.; Whitfill, T.; Wray, L.V.; Fisher, S.H.; Schumacher, M.A.
Structures of the Bacillus subtilis glutamine synthetase dodecamer reveal large intersubunit catalytic conformational changes linked to a unique feedback inhibition mechanism
J. Biol. Chem.
288
35801-35811
2013
Bacillus subtilis (P12425), Bacillus subtilis, Bacillus subtilis 168 (P12425)
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