Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

2.6.1.16: glutamine-fructose-6-phosphate transaminase (isomerizing)

This is an abbreviated version!
For detailed information about glutamine-fructose-6-phosphate transaminase (isomerizing), go to the full flat file.

Word Map on EC 2.6.1.16

Reaction

L-glutamine
+
D-fructose 6-phosphate
=
L-glutamate
+
D-glucosamine 6-phosphate

Synonyms

2-amino-2-deoxy-D-glucose-6-phosphate ketol-isomerase, BsglmS, EC 5.3.1.19, G-6-P synthase, Gfa1, Gfa1p, GFAT, GFAT1, GFAT2, GFPT1, GlcN-6-P synthase, GlmS, glmS ribozyme, glucosamine 6-phosphate synthase, glucosamine 6-phosphate synthetase, glucosamine phosphate isomerase (glutamine-forming), glucosamine synthase, glucosamine-6-P synthase, glucosamine-6-phosphate isomerase (glutamine-forming), glucosamine-6-phosphate synthase, glucosamine-6-phosphate synthetase, glucosamine-6P synthase, glucosamine:fructose-6-phosphate aminotransferase, glutamine-fructose 6-phosphate amidotransferase, glutamine-fructose 6-phosphate aminotransferase, glutamine-fructose-6-phosphate aminotransferase, glutamine-fructose-6-phosphate transaminase 1, glutamine: fructose-6-phosphate amidotransferase, glutamine: fructose-6-phosphate amidotransferase 1, glutamine: fructose-6-phosphate aminotransferase, glutamine:fructose-6-phosphate amidotransferase, glutamine:fructose-6-phosphate aminotransferase, hexosephosphate aminotransferase, isomerase, glucosamine phosphate (glutamine-forming), L-glutamine D-fructose 6-phosphate amidotransferase, L-glutamine fructose 6-phosphate transamidase, L-glutamine: D-fructose-6-phosphate amidotransferase, L-glutamine: L-fructose-6-phosphate amidotransferase, L-glutamine:D-fructose-6-phosphate amidotransferase, L-glutamine:D-fructose-6-phosphate amidotransferase (hexose isomerizing), L-glutamine:D-fructose-6-phosphate amidotransferase (hexose-isomerizing), L-glutamine:L-fructose-6-phosphate amidotransferase

ECTree

     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.16 glutamine-fructose-6-phosphate transaminase (isomerizing)

Crystallization

Crystallization on EC 2.6.1.16 - glutamine-fructose-6-phosphate transaminase (isomerizing)

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals are composed of a trans-acting form of the Thermoanaerobacter tengcongensis ribozyme with a single 2'-deoxyribose substitution at the cleavage site, which traps the RNA in the precleavage state. These crystals yield an accurate structure of the RNA to 1.7 A resolution
-
crystal structure of the isomerase domain in complex with the allosteric inhibitor UDP-GlcNAc and in the presence of glucose 6-phosphate, fructose 6-phosphate and an analogue of the reaction intermediate, 2-amino-2-deoxy-D-mannitol 6-phosphate. Deduction of a solution structure of the native protein. The tetrameric enzyme can be described as a dimer of dimers, with each half similar to the related enzyme from Escherichia coli. The core of the protein consists of the isomerase domains
hanging drop vapour diffusion and sitting drop vapour diffusion in 20% (w/v) PEG 600 and 0.15 M KSCN at pH 8.5
-
molecular docking of inhibitors methyl (2E)-4-([(2S)-2,3-diamino-3-oxopropyl]amino)-4-oxobut-2-enoate and methyl (2E)-4-([(2S)-2-amino-3-(methylamino)-3-oxopropyl]amino)-4-oxobut-2-enoate
-
crystal structure of intact protein
crystal structures of enzyme alone and in complex with the glucosamine 6-phosphate product at 2.95 A and 2.9 A resolution, respectively. No electron density for the glutaminase domain is observed. Upon sugar binding, the C-terminal loop, which forms the major part of the channel walls, becomes ordered and covers the synthase site. The ordering of the glutaminase domains likely follows fructose 6-phosphate binding by the anchoring of Trp74, which acts as the gate of the channel, on the closed C-terminal loop. This is accompanied by a major conformational change of the side chain of Lys503 of the neighboring synthase domain that strengthens the interactions of the synthase domain with the C-terminal loop and completely shields the synthase site. The concomitant conformational change of theLys503-Gly505 tripeptide places catalytic His504 in the proper position to open the sugar and buries the linear sugar, which is now in the vicinity of the catalytic groups involved in the sugar isomerization reaction
docking study using inhibitors 1,1'-[1,3,4-thiadiazole-2,5-diylbis[sulfanediyl(1-oxoethane-2,1-diyl)]]ditetrahydropyridazine-3,6-dione, 2,2'-(1,3,4-thiadiazole-2,5-diyldisulfanediyl)bis[N-(pyrrolidin-1-yl)acetamide]. The binding pocket of the enzyme includes the residues, Cys300, Gly301, Thr302, Ser303, Ser347, Gln348, Ser349, Thr352, Val399, Ser401, Ala602 and Lys603. The high docking energies of all generated conformers of 1,1'-[1,3,4-thiadiazole-2,5-diylbis[sulfanediyl(1-oxoethane-2,1-diyl)]]ditetrahydropyridazine-3,6-dione are strongly proportional to the antibacterial activities
hanging drop vapour diffusion method, 12% polyethylene glycol 8000, 0.1 M KCl, 5% glycerol
molecular dynamics simulations. Key role for Trp74, in the sealing of the hydrophobic channel connecting the two binding sites, as well as for the two Ala602 and Val605 residues, which form a narrow passage whose opening/closing constitutes an essential event in ammonia transfer
the crystal structure of the C1A mutant of Escherichia coli GlmS, solved at 2.5 A resolution, is organized as a hexamer, where the glutaminase domains adopt an inactive conformation
two crystal complexes of the isomerase domain with D-glucose 6-phosphate and 2-amino-2-deoxyglucitol 6-phosphate
-
isomerase domain of the human GFAT in the presence of cyclic glucose-6-phosphate and linear D-glucosamine 6-phosphate, hanging drop vapor diffusion method, at 20°C using 12% (v/v) isopropanol, 0.8 M ammonium acetate and 40 mM Tris-HCl at pH 8.5
molecular model of the 3-D on the basis of the crystal structures of Escherichia coli GlcN-6-P synthase, PDB entry 4AMV and Candida albicans GlcN-6-P synthase, PDB entry 2POC. The protein has a terminal glutamine amidotransferase type 2 domain (residues 2-318). The phosphosugar-binding SIS domain (residues 390-529; 562-707) plays a key role in catalysis and communication of fructose 6-phosphate and D-glucosamine 6-phosphate between the two active sites