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
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2.6.1.16
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hexosamine
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udp-glcnac
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albicans
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n-acetylglucosamine
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glcn6p
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o-glcnac
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riboswitches
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myasthenic
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udp-n-acetylglucosamine
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o-linked
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o-glcnacylation
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chitin
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self-cleavage
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azaserine
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self-cleaving
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limb-girdle
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glutaminase
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o-glcnacase
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pyridostigmine
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fatigable
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glucosamine-induced
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d-glucosamine
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hammerhead
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dpagt1
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6-diazo-5-oxo-l-norleucine
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analysis
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synthesis
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medicine
- 2.6.1.16
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hexosamine
- udp-glcnac
- albicans
- n-acetylglucosamine
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glcn6p
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o-glcnac
- riboswitches
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myasthenic
- udp-n-acetylglucosamine
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o-linked
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o-glcnacylation
- chitin
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self-cleavage
- azaserine
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self-cleaving
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limb-girdle
- glutaminase
- o-glcnacase
- pyridostigmine
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fatigable
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glucosamine-induced
- d-glucosamine
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hammerhead
- dpagt1
- 6-diazo-5-oxo-l-norleucine
- analysis
- synthesis
- medicine
Reaction
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
2.6.1.16 glutamine-fructose-6-phosphate transaminase (isomerizing)Advanced search results
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General Information on EC 2.6.1.16 - glutamine-fructose-6-phosphate transaminase (isomerizing)
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
metabolism
glutamine: fructose-6-phosphate amidotransferase (GFAT) enzymes catalyse the first committed step of the hexosamine biosynthesis pathway (HBP) using glutamine and fructose-6-phosphate to form glucosamine-6-phosphate (GlcN6P)
physiological function
additional information
physiological function
glutamine:fructose-6-phosphate amidotransferase is a rate-limiting enzyme in the hexoamine biosynthetic pathway and plays an important role in type 2 diabetes
physiological function
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a GlmS deletion mutant is defective in growth unless media are supplemented with D-glucosamine. The mutant is highly sensitive to detergents, hydrophobic antibiotics, and bile salts compared to the wild-type. Mutant secretes higher amounts of beta-lactamase than the wild-type in culture supernatant fractions and is attenuated in cell culture models of Salmonella infection
physiological function
the recombinant enzyme restores glucosamine prototrophy of the Saccharomyces cerevisiae gfa1 null mutant
physiological function
glucosamine-6-phosphate N-acetyltransferase (GNA1), catalyzing acetyl transfer from acetyl-coenzyme A to glucosamine-6-phosphate (GlcN-6P) and glutamine-fructose-6-phosphate aminotransferase (GlmS) catalyzing the formation of GlcN-6P from fructose-6-phosphate (Fru-6P), are two key enzymes in Bacillus subtilis for the bioproduction of N-acetylglucosamine (GlcNAc)
physiological function
glucosamine-6-phosphate synthase (GlmS) is a key enzyme in the biosynthesis of hexosamine
physiological function
glucosamine-6-phosphate synthase is an important enzyme for bacterial and fungal cell wall synthesis
physiological function
glucosamine-6-phosphate synthase is an important enzyme for bacterial and fungal cell wall synthesis
physiological function
glucosamine-6-phosphate synthase is an important enzyme for bacterial and fungal cell wall synthesis
physiological function
glucosamine-6-phosphate synthase is an important enzyme for bacterial and fungal cell wall synthesis
physiological function
glucosamine-6-phosphate synthase is an important enzyme for bacterial and fungal cell wall synthesis
physiological function
glucosamine-6-phosphate synthase is an important enzyme for bacterial and fungal cell wall synthesis
physiological function
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glucosamine-6-phosphate synthase is an important enzyme for bacterial and fungal cell wall synthesis
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physiological function
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glucosamine-6-phosphate synthase is an important enzyme for bacterial and fungal cell wall synthesis
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physiological function
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glucosamine-6-phosphate N-acetyltransferase (GNA1), catalyzing acetyl transfer from acetyl-coenzyme A to glucosamine-6-phosphate (GlcN-6P) and glutamine-fructose-6-phosphate aminotransferase (GlmS) catalyzing the formation of GlcN-6P from fructose-6-phosphate (Fru-6P), are two key enzymes in Bacillus subtilis for the bioproduction of N-acetylglucosamine (GlcNAc)
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physiological function
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glucosamine-6-phosphate synthase is an important enzyme for bacterial and fungal cell wall synthesis
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physiological function
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glucosamine-6-phosphate synthase is an important enzyme for bacterial and fungal cell wall synthesis
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physiological function
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a GlmS deletion mutant is defective in growth unless media are supplemented with D-glucosamine. The mutant is highly sensitive to detergents, hydrophobic antibiotics, and bile salts compared to the wild-type. Mutant secretes higher amounts of beta-lactamase than the wild-type in culture supernatant fractions and is attenuated in cell culture models of Salmonella infection
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physiological function
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glucosamine-6-phosphate synthase is an important enzyme for bacterial and fungal cell wall synthesis
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physiological function
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glucosamine-6-phosphate synthase is an important enzyme for bacterial and fungal cell wall synthesis
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physiological function
Aspergillus niger FGSC A1513
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glucosamine-6-phosphate synthase is an important enzyme for bacterial and fungal cell wall synthesis
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physiological function
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glucosamine-6-phosphate synthase is an important enzyme for bacterial and fungal cell wall synthesis
-
physiological function
-
glucosamine-6-phosphate synthase is an important enzyme for bacterial and fungal cell wall synthesis
-
physiological function
-
glucosamine-6-phosphate synthase is an important enzyme for bacterial and fungal cell wall synthesis
-
physiological function
-
glucosamine-6-phosphate synthase is an important enzyme for bacterial and fungal cell wall synthesis
-
physiological function
-
glucosamine-6-phosphate synthase is an important enzyme for bacterial and fungal cell wall synthesis
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additional information
mutation of residue Ser593 enhances the flexibility of the protein, which ultimately leads to increased enzyme activity, molecular dynamics simulation, homology modeling, and protein-ligand docking, overview
additional information
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mutation of residue Ser593 enhances the flexibility of the protein, which ultimately leads to increased enzyme activity, molecular dynamics simulation, homology modeling, and protein-ligand docking, overview
additional information
the glutaminase domain catalyzes the conversion of glutamine to glutamic acid with the release of ammonia. A catalytically important cysteinyl (Cys1) has been suggested to act as the mechanistic nucleophile after being activated by the N-terminal amine of the glutaminase domain (i.e. its own alpha-amine). Using molecular dynamics (MD) and quantum mechanics/molecular mechanics (QM/MM) computational methods, the active site of the glutaminase domain, the protonation state of its N-terminal amine, substrate binding, and catalytic mechanism are analysed, potential for an active site histidyl (His71) to alternatively act as the required base. A tetrahedral oxyanion intermediate is formed during the mechanism, stabilized by a water and two enzyme residues: Asn98 and Gly99. The overall rate-limiting step of the mechanism is the nucleophilic attack of a water on the thioester cross-linked intermediate with a barrier of 74.4 kJ/mol. An alternate mechanism in which His71 acts as the nucleophile-activating base, and which requires the Cys1 alpha-amine to be protonated, is calculated to be enzymatically feasible but to have a much higher overall rate-limiting barrier of 93.7 kJ/mol. Structure-function analysis and enzyme-substrate binding, overview
additional information
the residues involved in substrate binding are conserved in both Drosophila melanogaster GFAT1 and GFAT2 isozymes
additional information
the residues involved in substrate binding are conserved in both Drosophila melanogaster GFAT1 and GFAT2 isozymes
additional information
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mutation of residue Ser593 enhances the flexibility of the protein, which ultimately leads to increased enzyme activity, molecular dynamics simulation, homology modeling, and protein-ligand docking, overview
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