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Information on EC 2.6.1.16 - glutamine-fructose-6-phosphate transaminase (isomerizing) and Organism(s) Escherichia coli and UniProt Accession P17169
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2.6.1.16 glutamine-fructose-6-phosphate transaminase (isomerizing)IUBMB Comments
Although the overall reaction is that of a transferase, the mechanism involves the formation of ketimine between fructose 6-phosphate and a 6-amino group from a lysine residue at the active site, which is subsequently displaced by ammonia (transamidination).
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Word Map
- 2.6.1.16
-
hexosamine
- udp-glcnac
- albicans
- n-acetylglucosamine
-
glcn6p
-
o-glcnac
- riboswitches
-
myasthenic
- udp-n-acetylglucosamine
-
o-linked
-
o-glcnacylation
- chitin
-
self-cleavage
- azaserine
-
self-cleaving
-
limb-girdle
- glutaminase
- o-glcnacase
- pyridostigmine
-
fatigable
-
glucosamine-induced
- d-glucosamine
-
hammerhead
- dpagt1
- 6-diazo-5-oxo-l-norleucine
- analysis
- synthesis
- medicine
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
gfpt1, gfat1, glms ribozyme, glucosamine-6-phosphate synthase, glutamine:fructose-6-phosphate amidotransferase, glcn-6-p synthase, gfat2, glutamine fructose-6-phosphate amidotransferase, g-6-p synthase, glucosamine 6-phosphate synthase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-amino-2-deoxy-D-glucose-6-phosphate ketol-isomerase
-
-
-
-
GFAT
-
-
-
-
GlmS
glucosamine 6-phosphate synthase
-
-
-
-
glucosamine 6-phosphate synthetase
-
-
-
-
glucosamine phosphate isomerase (glutamine-forming)
-
-
-
-
glucosamine synthase
glucosamine-6-phosphate isomerase (glutamine-forming)
-
-
-
-
glucosamine-6-phosphate synthetase
-
-
-
-
glucosamine:fructose-6-phosphate aminotransferase
-
-
-
-
glutamine-fructose 6-phosphate amidotransferase
-
-
-
-
glutamine-fructose 6-phosphate aminotransferase
-
-
-
-
glutamine:fructose-6-phosphate aminotransferase
-
-
-
-
hexosephosphate aminotransferase
-
-
-
-
isomerase, glucosamine phosphate (glutamine-forming)
-
-
-
-
L-glutamine fructose 6-phosphate transamidase
-
-
-
-
GlmS
-
in the absence of D-fructose 6-phosphate, the enzyme exhibits a weak hydrolyzing activity of Gln into Glu and ammonia (glutaminase activity), whereas the presence of D-fructose 6-phosphate strongly stimulates its hemisynthase activity
glucosamine synthase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate
analysis of two catalytic mechanism variants (with neutral Cys1NH2 as the activating base or with His71 as the activating base) by molecular dynamics (MD) and quantum mechanics/molecular mechanics (QM/MM) computational methods, detailed overview. Results shows that the most likely catalytic mechanism is determined to involve a neutral Cys1NH2 group acting as the base that activates the Cys1 thiol
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amino group transfer
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-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
L-glutamine:D-fructose-6-phosphate isomerase (deaminating)
Although the overall reaction is that of a transferase, the mechanism involves the formation of ketimine between fructose 6-phosphate and a 6-amino group from a lysine residue at the active site, which is subsequently displaced by ammonia (transamidination).
CAS REGISTRY NUMBER
COMMENTARY
9030-45-9
-
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
D-fructose 6-phosphate
D-glucose 6-phosphate
determination of hexose phosphate-isomerizing activity
-
-
?
L-gamma-glutamyl-p-nitroanilide + H2O
L-glutamine + p-nitroaniline
determination of amidohydrolysing activity
-
-
?
D-fructose 6-phosphate
D-glucose 6-phosphate
-
isomerase activity studied over C-terminal D-fructose 6-phosphate binding domain constituted by residues 241 to 608
-
r
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
-
-
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
-
-
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
-
-
-
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
-
-
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
-
-
-
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
-
-
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
mechanism proposed
-
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
-
-
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
-
-
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
-
-
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
-
-
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
-
-
-
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
-
-
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
-
-
-
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
-
-
-
ir
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
-
specific for: L-glutamine
-
ir
additional information
?
-
enzyme follows an ordered process to bind sequentially Fru-6P and L-Gln and successively releases L-glutamate (hemisynthase activity) and D-glucosamine 6-phosphate (synthase activity)
-
-
?
additional information
?
-
the glutaminase domain catalyzes the conversion of glutamine to glutamic acid with the release of ammonia
-
-
-
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
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
-
-
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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]
-
4-(1,3-dihydroxypropan-2-ylimino)-2-(4-hydroxyphenyl)chroman-5,7-diol
-
4-(furan-2-ylcarbonyl)-3-hydroxy-5-(4-phenoxyphenyl)-1-(pyridin-3-ylmethyl)-1,5-dihydro-2H-pyrrol-2-one
20% inhibition at 0.1 mM
6,7-bis(2-methoxyphenyl)-10-methyl-1,4,7,12-tetrahydro-6H-chromeno[4,3-d][1,2,4]triazolo[1,5-a]pyrimidine
70% inhibition at 0.1 mM
ethyl 2-[2-(3-bromophenyl)-3-[(4-fluorophenyl)carbonyl]-4-hydroxy-5-oxo-2,5-dihydro-1H-pyrrol 1-yl]-4-methyl-1,3-thiazole-5-carboxylate
70% inhibition at 0.1 mM
ethyl 2-[3-[(4-fluorophenyl)carbonyl]-4-hydroxy-2-(4-methoxyphenyl)-5-oxo-2,5-dihydro-1H pyrrol-1-yl]-4-methyl-1,3-thiazole-5-carboxylate
70% inhibition at 0.1 mM
1,2-anhydrohexitol 6-phosphate
-
mixture of the four diastereoisomers. Irreversible inactivation. D-fructose 6-phosphate and 2-amino-2-deoxyglucitol protect, L-glutamine does not
2-Amino-2-deoxyglucitol 6-phosphate
-
competitive with respect to D-fructose 6-phosphate
D-glucosamine 6-phosphate
-
negative feedback-regulation at post-transcriptional level. The biological function of small RNA GlmZ is to positively control the enzyme's mRNA in response to D-glucosamine 6-phosphate concentrations. YhbJ, a gene of the rpoN operon, negatively regulates GlmZ
DL-delta-1-pyrroline-5-carboxylate
-
competitive with respect to L-glutamine
N3-bromoacetyl-L-2,3-diaminopropanoic acid
-
competitive with respect to L-glutamine
N3-chloroacetyl-L-2,3-diaminopropanoic acid
-
competitive with respect to L-glutamine
N3-iodoacetyl-L-2,3-diaminopropanoic acid
-
competitive with respect to L-glutamine
additional information
synthesis of naringenin derivatives with potent glucosamine-6-phosphate synthase inhibitory capacities and antioxidant, antimicrobial, and preservative efficacy. Molecular docking and in silico ADMET analysis, structure-activity relationship studies, overview. MIC values for growth inhibition of the cells
-
additional information
-
synthesis of naringenin derivatives with potent glucosamine-6-phosphate synthase inhibitory capacities and antioxidant, antimicrobial, and preservative efficacy. Molecular docking and in silico ADMET analysis, structure-activity relationship studies, overview. MIC values for growth inhibition of the cells
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
16
D-glucose 6-phosphate
-
pH 7.2, 37°C, isomerization catalyzed by C-terminal domain
0.36
D-fructose 6-phosphate
wild type enzyme, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C
0.67
D-fructose 6-phosphate
mutant enzyme V605L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C
0.93
D-fructose 6-phosphate
mutant enzyme W74A, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C
1.11
D-fructose 6-phosphate
mutant enzyme W74L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C
1.15
D-fructose 6-phosphate
mutant enzyme A602L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C
1.45
D-fructose 6-phosphate
mutant enzyme W74F, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C
3.8
D-fructose 6-phosphate
-
pH 7.2, 37°C, isomerization catalyzed by C-terminal domain
0.04
L-glutamine
mutant enzyme W74L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C
0.048
L-glutamine
mutant enzyme W74F, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C
0.072
L-glutamine
mutant enzyme V605L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C
0.1
L-glutamine
mutant enzyme A602L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C
0.27
L-glutamine
wild type enzyme, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C
0.38
L-glutamine
mutant enzyme W74A, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.083
D-fructose 6-phosphate
mutant enzyme W74L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C
0.12
D-fructose 6-phosphate
mutant enzyme W74A, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C
0.15
D-fructose 6-phosphate
mutant enzyme V605L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C
0.22
D-fructose 6-phosphate
mutant enzyme A602L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C
0.52
D-fructose 6-phosphate
wild type enzyme, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C
0.92
D-fructose 6-phosphate
mutant enzyme W74F, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C
14.42
D-fructose 6-phosphate
wild type enzyme, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C
0.28
L-glutamine
mutant enzyme V605L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C
0.38
L-glutamine
mutant enzyme A602L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C
0.97
L-glutamine
wild type enzyme, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C
1.55
L-glutamine
mutant enzyme W74L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C
3.02
L-glutamine
mutant enzyme W74A, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C
7.17
L-glutamine
mutant enzyme W74F, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C
17.17
L-glutamine
wild type enzyme, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.088
2-Amino-2-deoxyglucitol 6-phosphate
-
takes into account 2.2% of the open form present in a solution of D-fructose 6-phosphate
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.38
0.42
additional information
-
development of an assay for glucosamine 6-phosphate synthase that measures the production of glucosamine 6-phosphate by either following the consumption of acetyl-CoA spectrophotometrically at 230 nm or quantifying the free thiol with 5,5'-dithio-bis(2-nitrobenzoic acid), i.e. Ellmans reagent in a discontinuous manner. Simple assay method, which can be adapted to 96-well microtiter plate format
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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
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
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70000
2 * 70000, calculated by means of crystalline structure determined by X ray diffraction
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
hexamer
the enzyme is regulated by a morpheein-type allosteric mechanism, in which functional dimeric GlmS is in equilibrium with the inactive hexamer
dimer
oligomer
-
sedimentation velocity experiments show that at low concentration the enzyme is mainly present as a dimer. At a higher protein concentration the equilibrium between the two forms of GlmS is significantly displaced toward the oligomeric form
dimer
2 * 70000, calculated by means of crystalline structure determined by X ray diffraction
dimer
the enzyme is regulated by a morpheein-type allosteric mechanism, in which functional dimeric GlmS is in equilibrium with the inactive hexamer
dimer
-
sedimentation velocity experiments show that at low concentration the enzyme is mainly present as a dimer. At a higher protein concentration the equilibrium between the two forms of GlmS is significantly displaced toward the oligomeric form
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C1A
the structure of the inactive C1A mutant, crystallized in the presence of D-fructose 6-phosphate and Gln is deterimined. The C1A-GlmS structure is organized as a hexamer. The enzyme is regulated by a morpheein-type allosteric mechanism, in which functional dimeric GlmS is in equilibrium with the inactive hexamer
W74A
efficiency of ammonia transfer is close to zero. No use of ammonia as a substrate
W74L
decrease in ammonia transfer, 5-7fold increase in the affinity for glutamine in the presence of fructose 6-phosphate
A602L
enhanced activity compared to the wild type enzyme, the behaviour of the mutant is similar to that of the wild type counterpart during purification demonstrating no significant modification in the overall protein structure
C1A
-
C1A-GlmS does not reveal glutaminase activity at 37°C when tested in the presence of Gln only
V605L
enhanced activity compared to the wild type enzyme, the behaviour of the mutant is similar to that of the wild type counterpart during purification demonstrating no significant modification in the overall protein structure
W74A
enhanced activity compared to the wild type enzyme, the behaviour of the mutant is similar to that of the wild type counterpart during purification demonstrating no significant modification in the overall protein structure
W74F
enhanced activity compared to the wild type enzyme, the behaviour of the mutant is similar to that of the wild type counterpart during purification demonstrating no significant modification in the overall protein structure
W74L
enhanced activity compared to the wild type enzyme, the behaviour of the mutant is similar to that of the wild type counterpart during purification demonstrating no significant modification in the overall protein structure
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
-
activity of the wild type enzyme is not affected by incubation at 50°C for 60 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0-2°C, potassium phosphate buffer, pH 7.0, 0.06 M L-glutamine, 0.01 M EDTA, stable for up to 3 or 4 weeks
-
5°C, potassium phosphate buffer, pH 7.5, 1 mM EDTA, 1 mM dithiothreitol, 0.5 mM L-glutamine, 0.05 mM D-glucose 6-phosphate, 600 mM sucrose, stable for few weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Q-Sepharose fast flow column chromatography and Superdex 200 Hiload gel filtration
Q-Sepharose fast flow column chromatography and Superdex 200 HR 26/60 Hiload gel filtration
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
assay of synthase and hemisynthase activities of glucosamine-6-phosphate synthase by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry, allowing determination of both hemisynthase and synthase parameters from a single assay kinetic experiment
analysis
-
development of an assay for glucosamine 6-phosphate synthase that measures the production of glucosamine 6-phosphate by either following the consumption of acetyl-CoA spectrophotometrically at 230 nm or quantifying the free thiol with 5,5'-dithio-bis(2-nitrobenzoic acid), i.e. Ellmans reagent in a discontinuous manner. Simple assay method, which can be adapted to 96-well microtiter plate format
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ghosh, S.; Blumenthal, H.J.; Davidson, E.; Roseman, S.
Glucosamine metabolism.V. Enzymatic synthesis of glucosamine 6-phosphate
J. Biol. Chem.
235
1265-1273
1960
Aspergillus flavus, Aspergillus parasiticus, Colletotrichum gloeosporioides, Hypomyces rosellus, Escherichia coli, Penicillium sp., Helminthosporium sativum, Neurospora crassa, Neurospora tetrasperma, Penicillium chrysogenum, Rattus norvegicus
Chmara, H.; Zhner, H.
The inactivation of glucosamine synthetase from bacteria by anticapsin, the C-terminal epoxyamino acid of the antibiotic tetaine
Biochim. Biophys. Acta
787
45-52
1984
Bacillus thuringiensis, Escherichia coli, Paenarthrobacter aurescens, Pseudomonas aeruginosa
Milewski, S.; Chmara, H.; Andruszkiewicz, R.; Borowski, E.
N3-haloacetyl derivatives of L-2,3-diaminopropanoic acid: novel inactivators of glucosamine-6-phosphate synthase
Biochim. Biophys. Acta
1115
225-229
1992
Bacillus pumilus, Candida albicans, Escherichia coli
Badet, B.; Vermoote, P.; Le Goffic, F.
Glucosamine synthetase from Escherichia coli: kinetic mechanism and inhibition by N3-fumaroyl-L-2,3-diaminopropionic derivatives
Biochemistry
27
2282-2287
1988
Escherichia coli
Badet, B.; Vermoote, P.; Haumont, P.Y.; Lederer, F.; Le Goffic, F.
Glucosamine synthetase from Escherichia coli: purification, properties, and glutamine-utilizing site location
Biochemistry
26
1940-1948
1987
Escherichia coli
Badet-Denisot, M.A.; Leriche, C.; Massiere, F.; Badet, B.
Nitrogen transfer in E. coli glucosamine-6P synthase. Investigations using substrate and bisubstrate analogs
Bioorg. Med. Chem. Lett.
5
815-820
1995
Escherichia coli
-
Bearne, S.L.
Active site-directed inactivation of Escherichia coli glucosamine-6-phosphate synthase. Determination of the fructose 6-phosphate binding constant using a carbohydrate-based inactivator
J. Biol. Chem.
271
3052-3057
1996
Escherichia coli
Leriche, C.; Badet-Denisot, M.A.; Badet, B.
Affinity labeling of Escherichia coli glucosamine-6-phosphate synthase with a fructose 6-phosphate analog. Evidence for proximity between the N-terminal cysteine and the fructose-6-phosphate-binding site
Eur. J. Biochem.
245
418-422
1997
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Deng, M.D.; Grund, A.D.; Wassink, S.L.; Peng, S.S.; Nielsen, K.L.; Huckins, B.D.; Burlingame, R.P.
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Floquet, N.; Richez, C.; Durand, P.; Maigret, B.; Badet, B.; Badet-Denisot, M.A.
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Kalamorz, F.; Reichenbach, B.; Maerz, W.; Rak, B.; Goerke, B.
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Valerio-Lepiniec, M.; Aumont-Nicaise, M.; Roux, C.; Raynal, B.; England, P.; Badet, B.; Badet-Denisot, M.A.; Desmadril, M.
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Structural basis for morpheein-type allosteric regulation of Escherichia coli glucosamine-6-phosphate synthase: equilibrium between inactive hexamer and active dimer
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Gaucher-Wieczorek, F.; Guerineau, V.; Touboul, D.; Thetiot-Laurent, S.; Pelissier, F.; Badet-Denisot, M.A.; Badet, B.; Durand, P.
Evaluation of synthase and hemisynthase activities of glucosamine-6-phosphate synthase by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
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Hussein, S.; Kubba, A.; Abdula, A.
Docking study of some new 2, 5-disubstituted-1, 3, 4-thiadiazole derivatives against glucosamine-6-phosphate synthase
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Lather, A.; Sharma, S.; Khatkar, A.
Naringenin derivatives as glucosamine-6-phosphate synthase inhibitors synthesis, antioxidants, antimicrobial, preservative efficacy, molecular docking and in silico ADMET analysis
BMC Chem.
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Aspergillus niger (A2QH83), Aspergillus niger, Proteus mirabilis (B4F0F0), Proteus mirabilis, Escherichia coli (P17169), Escherichia coli, Candida albicans (P53704), Candida albicans, Staphylococcus aureus (Q6GES3), Staphylococcus aureus, Pseudomonas aeruginosa (Q9HT25), Pseudomonas aeruginosa ATCC 15692 (Q9HT25), Staphylococcus aureus MRSA252 (Q6GES3), Proteus mirabilis HI4320 (B4F0F0), Pseudomonas aeruginosa 1C (Q9HT25), Candida albicans ATCC MYA-2876 (P53704), Pseudomonas aeruginosa PRS 101 (Q9HT25), Aspergillus niger FGSC A1513 (A2QH83), Pseudomonas aeruginosa DSM 22644 (Q9HT25), Pseudomonas aeruginosa CIP 104116 (Q9HT25), Pseudomonas aeruginosa LMG 12228 (Q9HT25), Aspergillus niger CBS 513.88 (A2QH83), Pseudomonas aeruginosa JCM 14847 (Q9HT25)
Wei, W.; Monard, G.; Gauld, J.
Computational insights into substrate binding and catalytic mechanism of the glutaminase domain of glucosamine-6-phosphate synthase (GlmS)
RSC Adv.
7
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