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6.3.1.2: glutamine synthetase

This is an abbreviated version!
For detailed information about glutamine synthetase, go to the full flat file.

Word Map on EC 6.3.1.2

Reaction

ATP
+
L-glutamate
 +
NH3
=
ADP
 +
phosphate
 +
L-glutamine

Synonyms

AmGLN1, ATP glutamate-ammonia ligase, Chloroplast GS2, Clone lambda-GS28, Clone lambda-GS31, Clone lambda-GS8, Cytoplasmic GS3, Cytosolic GS1, gamma-glutamyl transferase, gamma-glutamyl:ammonia ligase, gamma-glutamylhydroxamate synthetase, Gln isozyme alpha, Gln isozyme beta, Gln isozyme gamma, Gln synthetase, GLN1,1, GLN1,2, GLN1,3, GLN1,4, GLN1-1, GLN1-2, Gln1;1, Gln1;2, Gln1;3, Gln1;4, Gln1;5, GLN2, GlnA, glnA-1, GlnA1, GlnA2, GlnA3, GlnA4, GlnN, GlnR, GluA, GLUL, Glutamate--ammonia ligase, glutamate-ammonia ligase, Glutamine synthetase, glutamine synthetase cytosolic isozyme 1, glutamine synthetase cytosolic isozyme 2, glutamine synthetase I, glutamine synthetase type II, glutamine synthetase type III, Glutamylhydroxamic synthetase, GS, GS type I, GS type-1, GS(1), GS-II, GS1, GS1 kinase, GS1-1, GS1-2, GS107, GS112, GS117, GS12, GS122, GS1a, GS1beta1, GS1gamma1, GS2, GS2a, GS3, GSI, GSII, GSIII, Isozyme delta, L-glutamate:ammonia ligase, L-glutamate:ammonia ligase (ADP-forming), L-Glutamine synthetase, LDBPK_060370, LdGS, MM_0964, MtGS, N47/N48, OsGLN1,1, OsGLN1,2, protein transacetylase, S2205/S2287, SSO0366, Synthetase, glutamine, TAase, type I glutamine synthetase, type III glutamine synthetase

ECTree

     6 Ligases
         6.3 Forming carbon-nitrogen bonds
             6.3.1 Acid—ammonia (or amine) ligases (amide synthases)
                6.3.1.2 glutamine synthetase

Crystallization

Crystallization on EC 6.3.1.2 - glutamine synthetase

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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
Ta6Br12 derivative, to 3.5 A resolution, space group C2221. The divergence of the type III from the type I and II GS enzymes is mainly due to differences in quaternary structure despite all the enzymes sharing a remarkably conserved active site fold.. The two hexameric rings of the GSIII dodecamer associate on the opposite surface relative to types I and II
-
untagged, full-length recombinant protein, to 3.0 A resolution, space group P1
computational study on folding state
apo-enzyme structure determination and analysis at resolution of 3.0 A, molecular replacement using a pentamer of Zea mays GS/MnADP/MSO-P complex, overview
two different enzyme complexes with: 1. phosphate, ADP, and manganese, and 2. a phosphorylated form of the inhibitor methionine sulfoximine, ADP and manganese. X-ray diffraction structure determination and analysis at resolutions of 2.05 A and 2.6 A, respectively, molecular replacement
-
to 2.35 A resolution
-
complex of the enzyme with the purine analogue 1-[(3,4-dichlorophenyl)methyl]-3,7-dimethyl-8-morpholin-4-yl-purine-2,6-dione alone to 2.55 A resolution, and in complex with 1-[(3,4-dichlorophenyl)methyl]-3,7-dimethyl-8-morpholin-4-yl-purine-2,6-dione together with methionine sulfoximine phosphate, magnesium and phosphate, to 2.2 A resolution. The former represents a relaxed, inactive conformation of the enzyme, while the latter is a taut, active one. Compound 1-[(3,4-dichlorophenyl)methyl]-3,7-dimethyl-8-morpholin-4-yl-purine-2,6-dione binds at the same position in the nucleotide site, regardless of the conformational state
enzyme complexed with 3, X-ray diffraction structure determination and analysis
vapor diffusion hanging drop method, structure of a complex with a phosphorylated form of the inhibitor methionine sulfoximine, magnesium, and ADP, solved by molecular replacement and refined at 2.1-Å resolution
four crystal structures of glutamine synthetase, complexed with the substrate Glu and with each of the three feddback inhibitors, Gly, Ala, and Ser
-
structural model for the reaction mechanism of glutamine synthetase, based on five crystal structures of enzyme-substrate complexes
-
X-ray crystallography of a binding site on the enzyme for monovalent cations, Tl+ and Cs+, which is probably the binding site for the substrate ammonium
-
hanging drop vapour diffusion method, GS crystals in complex with ADP and methionine sulfoximine phosphate, using 9% (w/v) polyethylene glycol 8000, 100 mM Tris-HCl pH 7.8, 5% (v/v) 2-methyl-2,4-pentanediol, 10 mM MnCl2
-