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D-fructose 6-phosphate
D-glucose 6-phosphate
L-gamma-glutamyl-p-nitroanilide + D-fructose 6-phosphate
?
-
-
-
-
?
L-gamma-glutamyl-p-nitroanilide + H2O
L-glutamine + p-nitroaniline
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
additional information
?
-
D-fructose 6-phosphate
D-glucose 6-phosphate
-
determination of hexose phosphate-isomerizing 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
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
-
-
?
L-gamma-glutamyl-p-nitroanilide + H2O
L-glutamine + p-nitroaniline
determination of amidohydrolysing activity
-
-
?
L-gamma-glutamyl-p-nitroanilide + H2O
L-glutamine + p-nitroaniline
-
determination of amidohydrolysing activity
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
specific for: L-glutamine
-
ir
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
-
-
-
-
ir
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
Helminthosporium sativum
-
-
-
?
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
-
importance for N-acetylglucosamine synthesis in human liver
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
-
enzyme plays a key role in induction of insulin resistance in cultured cells
-
?
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
-
specific for: L-glutamine
-
ir
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
-
-
-
?
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
-
-
-
?
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
-
specific for: L-glutamine
-
ir
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
-
specific for: L-glutamine
-
?
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
-
specific for: L-glutamine
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
-
-
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
-
-
-
?
additional information
?
-
enzyme possesses an independent glutaminase activity, converting glutamine to glutamate in the absence of fructose 6-phosphate
-
-
?
additional information
?
-
-
enzyme possesses an independent glutaminase activity, converting glutamine to glutamate in the absence of fructose 6-phosphate
-
-
?
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
-
-
-
additional information
?
-
-
asparagine is not a substrate
-
-
?
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(2S)-2-amino-3-(([(2R,3R)-3-benzoyloxiran-2-yl]carbonyl)amino)propanoic acid
-
-
(2S)-2-amino-3-([(2E)-4-oxo-4-phenylbut-2-enoyl]amino)propanoic acid
-
-
(2S)-2-amino-3-([(2E)-4-oxopent-2-enoyl]amino)propanoic acid
-
-
(2S)-3-(([(2R,3R)-3-acetyloxiran-2-yl]carbonyl)amino)-2-aminopropanoic acid
-
-
(3R,4S)-4-(methylamino)-1-phenylpent-1-en-3-ol
(4S)-2-methyl-2-phenylpentane-1,4-diol
1'-N-methyl spiro[2'.2'']-acenaphthyleno-3'-cholestrylcarboxylate pyrrolidine
1'-N-methyl spiro[2'.2'']-indane-1'',3''-dione-3'-cholestrylcarboxylate pyrrolidine
1'-N-methyl spiro[2'.3'']-(4'',7''-dichloro)-oxindolo-3'-cholestrylcarboxylate pyrrolidine
1'-N-methyl spiro[2'.3'']-(5'',7''-bromo)-oxindolo-3'-cholestrylcarboxylate pyrrolidine
1'-N-methyl spiro[2'.3'']-(5''-bromo)-oxindolo-3'-cholestrylcarboxylate pyrrolidine
1'-N-methyl spiro[2'.3'']-(N-methyl)-oxindolo-3'-cholestrylcarboxylate pyrrolidine
1'-N-methyl spiro[2'.3'']-(N-phenyl)-oxindolo-3'-cholestrylcarboxylate pyrrolidine
1'-N-methyl spiro[2'.3'']oxindolo-3'-cholestrylcarboxylate pyrrolidine
1,1'-[1,3,4-thiadiazole-2,5-diylbis[sulfanediyl(1-oxoethane-2,1-diyl)]]ditetrahydropyridazine-3,6-dione
-
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
1-methyl 8-(2-oxopropyl) (2E,7S)-7-amino-4-oxooct-2-enedioate
-
ester derivative of N3-(4-metoxyfumaroyl)-(S)-2,3-diaminopropanoic acid, potent inhibitory activity against fungal glucosamine-6-phosphate synthase, good antifungal activity against Candida albicans
1-methyl 8-[(2R)-3-oxobutan-2-yl] (2E,7S)-7-amino-4-oxooct-2-enedioate
-
ester derivative of N3-(4-metoxyfumaroyl)-(S)-2,3-diaminopropanoic acid, potent inhibitory activity against fungal glucosamine-6-phosphate synthase, good antifungal activity against Candida albicans
2,2'-(1,3,4-thiadiazole-2,5-diyldisulfanediyl)bis[N-(pyrrolidin-1-yl)acetamide]
-
2-(4-hydroxyphenyl)-4-(4-nitrophenylimino)chroman-5,7-diol
2-amino-2-deoxy-D-glucitol 6-phosphate
2-amino-2-deoxy-D-glucitol-6-phosphate
2-amino-2-deoxy-D-glucitol-6-phosphate dimethyl ester
-
-
2-amino-2-deoxy-D-mannitol 6-phosphate
2-amino-2-deoxy-D-mannitol-6-phosphate
2-Amino-2-deoxyglucitol 6-phosphate
-
competitive with respect to D-fructose 6-phosphate
3-(tert-butoxycarbonyl)-6-(3-benzoylprop-2-yl)phenol
4,4'-dithiodipyridine
-
inactivation reversed by dithiothreitol. Competitive with respect to L-glutamine. Non-competitive with respect to D-fructose 6-phosphate
4-(1,3-dihydroxypropan-2-ylimino)-2-(4-hydroxyphenyl)chroman-5,7-diol
4-(2-chlorophenylimino)-2-(4-hydroxyphenyl)chroman-5,7-diol
4-(2-fluorophenylimino)-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
4-Glutamylhydroxamate
-
-
5,5'-dithionitrobenzoic acid
5-phospho-D-arabinoamide
-
-
6,6'-Dithiodinicotinic acid
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
6-diazo-5-oxo-L-norleucine
7-methoxy-2,3-dihydro-2-phenyl-4 quinolone
8-(3,3-dimethyl-2-oxobutyl) 1-methyl (2E,7S)-7-amino-4-oxooct-2-enedioate
-
ester derivative of N3-(4-metoxyfumaroyl)-(S)-2,3-diaminopropanoic acid, potent inhibitory activity against fungal glucosamine-6-phosphate synthase, good antifungal activity against Candida albicans
arabinose oxime 5-phosphate
-
inhibitor of the sugar isomerising domain
cholest-5-en-3-yl 1,3-dioxo-1,1',2',3,5',6',7',7'a-octahydrospiro[indene-2,3'-pyrrolizine]-2'-carboxylate
cholest-5-en-3-yl 1-methyl-2-oxo-1,1',2,2',5',6',7',7'a-octahydrospiro[indole-3,3'-pyrrolizine]-2'-carboxylate
cholest-5-en-3-yl 2-oxo-1',2',5',6',7',7'a-hexahydro-2H-spiro[acenaphthylene-1,3'-pyrrolizine]-2'-carboxylate
cholest-5-en-3-yl 2-oxo-1,1',2,2',5',6',7',7'a-octahydrospiro[indole-3,3'-pyrrolizine]-2'-carboxylate
cholest-5-en-3-yl 2-oxo-1-phenyl-1,1',2,2',5',6',7',7'a-octahydrospiro[indole-3,3'-pyrrolizine]-2'-carboxylate
cholest-5-en-3-yl 4,7-dichloro-2-oxo-1,1',2,2',5',6',7',7'a-octahydrospiro[indole-3,3'-pyrrolizine]-2'-carboxylate
cholest-5-en-3-yl 5,7-dibromo-2-oxo-1,1',2,2',5',6',7',7'a-octahydrospiro[indole-3,3'-pyrrolizine]-2'-carboxylate
cholest-5-en-3-yl 5-bromo-2-oxo-1,1',2,2',5',6',7',7'a-octahydrospiro[indole-3,3'-pyrrolizine]-2'-carboxylate
Congo red
CR, affects the growth, morphology, and activity of glucosamine-6-phosphate synthase in human pathogenic fungus Sporothrix schenckii. Under conditions of yeast development, 0.015 mM CR abolishes conidia germination, but when yeast cells are first obtained in the absence of the dye and then post-incubated in its presence, yeasts rapidly differentiate into mycelial cells. On the other hand, under conditions of mycelium development, 0.150 mM CR do not affect conidia germination, but filamentous cells undergo structural changes characterized by a distorted cell wall contour, the loss of polarity and the formation of red-pigmented, hyphal globose structures. Under these conditions, CR also induces a significant and transient increase in the activity of GlcN-6-P synthase, an essential enzyme in cell wall biogenesis
D-glucitol 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
D-glucosamine-6-phosphate
-
1 mM, about 50% loss of activity
dihydroxyacetone phosphate
-
weak
DL-delta-1-pyrroline-5-carboxylate
-
competitive with respect to L-glutamine
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
fructose 1,6-diphosphate
-
weak
glyceraldehyde 3-phosphate
-
50% inhibition at 0.2 mM
Glyoxal
-
50% inhibition at 0.03 mM
L-2,3-diaminopropanoic acid
L-alpha-glycerophosphate
-
weak
Mercuric chloride
-
84% inhibition at 1 mM
methyl (2E)-4-([(2S)-2,3-diamino-3-oxopropyl]amino)-4-oxobut-2-enoate
-
-
methyl (2E)-4-([(2S)-2-amino-3-(methylamino)-3-oxopropyl]amino)-4-oxobut-2-enoate
-
-
N-acetyl-2-amino-2-deoxy-D-glucitol-6-phosphate
-
-
N-iodoacetylglucosamine 6-phosphate
-
D-fructose 6-phosphate protects
N3-(4-Methoxyfumaroyl)-L-2,3-diaminopropanoic acid
N3-bromoacetyl-L-2,3-diaminopropanoic acid
N3-chloroacetyl-L-2,3-diaminopropanoic acid
N3-fumaramoyl-L-2,3-diaminopropanoic acid
N3-fumaroyl-L-2,3-diaminopropanoic acid
N3-fumarylcarboxyamido-L-2,3-diaminopropionic acid
N3-iodoacetyl-L-2,3-diaminopropanoic acid
N3-L-trans-epoxysuccinamoyl-L-2,3-diaminopropanoic acid
-
inhibitor of the glutamine binding site
N4-(4-Methoxyfumaroyl)-L-2,4-diaminobutanoic acid
-
-
p-hydroxymercuribenzoate
-
-
pyridoxamine-5'-phosphate
-
-
Tolbutamide
-
80% inhibition at 2 mg/ml
UDP-N-acetyl-alpha-D-glucosamine
-
-
uridine 5'-diphospho-N-acetyl-D-glucosamine
-
-
uridine 5'-diphospho-N-acetylglucosamine
-
(3R,4S)-4-(methylamino)-1-phenylpent-1-en-3-ol
-
(3R,4S)-4-(methylamino)-1-phenylpent-1-en-3-ol
-
(3R,4S)-4-(methylamino)-1-phenylpent-1-en-3-ol
-
(3R,4S)-4-(methylamino)-1-phenylpent-1-en-3-ol
-
(3R,4S)-4-(methylamino)-1-phenylpent-1-en-3-ol
-
(3R,4S)-4-(methylamino)-1-phenylpent-1-en-3-ol
-
(4S)-2-methyl-2-phenylpentane-1,4-diol
-
(4S)-2-methyl-2-phenylpentane-1,4-diol
-
(4S)-2-methyl-2-phenylpentane-1,4-diol
-
(4S)-2-methyl-2-phenylpentane-1,4-diol
-
(4S)-2-methyl-2-phenylpentane-1,4-diol
-
(4S)-2-methyl-2-phenylpentane-1,4-diol
-
1'-N-methyl spiro[2'.2'']-acenaphthyleno-3'-cholestrylcarboxylate pyrrolidine
-
1'-N-methyl spiro[2'.2'']-acenaphthyleno-3'-cholestrylcarboxylate pyrrolidine
-
-
1'-N-methyl spiro[2'.2'']-acenaphthyleno-3'-cholestrylcarboxylate pyrrolidine
-
1'-N-methyl spiro[2'.2'']-acenaphthyleno-3'-cholestrylcarboxylate pyrrolidine
-
-
1'-N-methyl spiro[2'.2'']-indane-1'',3''-dione-3'-cholestrylcarboxylate pyrrolidine
-
1'-N-methyl spiro[2'.2'']-indane-1'',3''-dione-3'-cholestrylcarboxylate pyrrolidine
-
-
1'-N-methyl spiro[2'.2'']-indane-1'',3''-dione-3'-cholestrylcarboxylate pyrrolidine
-
1'-N-methyl spiro[2'.2'']-indane-1'',3''-dione-3'-cholestrylcarboxylate pyrrolidine
-
-
1'-N-methyl spiro[2'.3'']-(4'',7''-dichloro)-oxindolo-3'-cholestrylcarboxylate pyrrolidine
-
1'-N-methyl spiro[2'.3'']-(4'',7''-dichloro)-oxindolo-3'-cholestrylcarboxylate pyrrolidine
-
-
1'-N-methyl spiro[2'.3'']-(4'',7''-dichloro)-oxindolo-3'-cholestrylcarboxylate pyrrolidine
-
1'-N-methyl spiro[2'.3'']-(4'',7''-dichloro)-oxindolo-3'-cholestrylcarboxylate pyrrolidine
-
-
1'-N-methyl spiro[2'.3'']-(5'',7''-bromo)-oxindolo-3'-cholestrylcarboxylate pyrrolidine
-
1'-N-methyl spiro[2'.3'']-(5'',7''-bromo)-oxindolo-3'-cholestrylcarboxylate pyrrolidine
-
-
1'-N-methyl spiro[2'.3'']-(5'',7''-bromo)-oxindolo-3'-cholestrylcarboxylate pyrrolidine
-
1'-N-methyl spiro[2'.3'']-(5'',7''-bromo)-oxindolo-3'-cholestrylcarboxylate pyrrolidine
-
-
1'-N-methyl spiro[2'.3'']-(5''-bromo)-oxindolo-3'-cholestrylcarboxylate pyrrolidine
-
1'-N-methyl spiro[2'.3'']-(5''-bromo)-oxindolo-3'-cholestrylcarboxylate pyrrolidine
-
-
1'-N-methyl spiro[2'.3'']-(5''-bromo)-oxindolo-3'-cholestrylcarboxylate pyrrolidine
-
1'-N-methyl spiro[2'.3'']-(5''-bromo)-oxindolo-3'-cholestrylcarboxylate pyrrolidine
-
-
1'-N-methyl spiro[2'.3'']-(N-methyl)-oxindolo-3'-cholestrylcarboxylate pyrrolidine
-
1'-N-methyl spiro[2'.3'']-(N-methyl)-oxindolo-3'-cholestrylcarboxylate pyrrolidine
-
-
1'-N-methyl spiro[2'.3'']-(N-methyl)-oxindolo-3'-cholestrylcarboxylate pyrrolidine
-
1'-N-methyl spiro[2'.3'']-(N-methyl)-oxindolo-3'-cholestrylcarboxylate pyrrolidine
-
-
1'-N-methyl spiro[2'.3'']-(N-phenyl)-oxindolo-3'-cholestrylcarboxylate pyrrolidine
-
1'-N-methyl spiro[2'.3'']-(N-phenyl)-oxindolo-3'-cholestrylcarboxylate pyrrolidine
-
-
1'-N-methyl spiro[2'.3'']-(N-phenyl)-oxindolo-3'-cholestrylcarboxylate pyrrolidine
-
1'-N-methyl spiro[2'.3'']-(N-phenyl)-oxindolo-3'-cholestrylcarboxylate pyrrolidine
-
-
1'-N-methyl spiro[2'.3'']oxindolo-3'-cholestrylcarboxylate pyrrolidine
-
1'-N-methyl spiro[2'.3'']oxindolo-3'-cholestrylcarboxylate pyrrolidine
-
-
1'-N-methyl spiro[2'.3'']oxindolo-3'-cholestrylcarboxylate pyrrolidine
-
1'-N-methyl spiro[2'.3'']oxindolo-3'-cholestrylcarboxylate pyrrolidine
-
-
1,1'-dithiodiformamidine
-
irreversible inhibition
1,1'-dithiodiformamidine
-
irreversible inhibition
1,1'-dithiodiformamidine
-
irreversible inhibition
1,1'-dithiodiformamidine
-
irreversible inhibition
1,1'-dithiodiformamidine
-
irreversible inhibition
2-(4-hydroxyphenyl)-4-(4-nitrophenylimino)chroman-5,7-diol
-
2-(4-hydroxyphenyl)-4-(4-nitrophenylimino)chroman-5,7-diol
-
2-(4-hydroxyphenyl)-4-(4-nitrophenylimino)chroman-5,7-diol
-
2-(4-hydroxyphenyl)-4-(4-nitrophenylimino)chroman-5,7-diol
-
2-(4-hydroxyphenyl)-4-(4-nitrophenylimino)chroman-5,7-diol
-
2-(4-hydroxyphenyl)-4-(4-nitrophenylimino)chroman-5,7-diol
-
2-amino-2-deoxy-D-glucitol 6-phosphate
-
-
2-amino-2-deoxy-D-glucitol 6-phosphate
-
-
2-amino-2-deoxy-D-glucitol-6-phosphate
-
-
2-amino-2-deoxy-D-glucitol-6-phosphate
IC50: 0.056 mM
2-amino-2-deoxy-D-glucitol-6-phosphate
-
inhibitor of the sugar isomerising domain
2-amino-2-deoxy-D-glucitol-6-phosphate
-
2-amino-2-deoxy-D-mannitol 6-phosphate
-
-
2-amino-2-deoxy-D-mannitol 6-phosphate
-
2-amino-2-deoxy-D-mannitol-6-phosphate
-
-
2-amino-2-deoxy-D-mannitol-6-phosphate
-
exhibits stronger affinity for the sugar-binding site of GlcN-6-P synthase than 2-amino-2-deoxy-D-glucitol-6-phosphate
3-(tert-butoxycarbonyl)-6-(3-benzoylprop-2-yl)phenol
-
3-(tert-butoxycarbonyl)-6-(3-benzoylprop-2-yl)phenol
-
3-(tert-butoxycarbonyl)-6-(3-benzoylprop-2-yl)phenol
-
3-(tert-butoxycarbonyl)-6-(3-benzoylprop-2-yl)phenol
-
3-(tert-butoxycarbonyl)-6-(3-benzoylprop-2-yl)phenol
-
3-(tert-butoxycarbonyl)-6-(3-benzoylprop-2-yl)phenol
-
4-(1,3-dihydroxypropan-2-ylimino)-2-(4-hydroxyphenyl)chroman-5,7-diol
-
4-(1,3-dihydroxypropan-2-ylimino)-2-(4-hydroxyphenyl)chroman-5,7-diol
-
4-(1,3-dihydroxypropan-2-ylimino)-2-(4-hydroxyphenyl)chroman-5,7-diol
-
4-(1,3-dihydroxypropan-2-ylimino)-2-(4-hydroxyphenyl)chroman-5,7-diol
-
4-(1,3-dihydroxypropan-2-ylimino)-2-(4-hydroxyphenyl)chroman-5,7-diol
-
4-(1,3-dihydroxypropan-2-ylimino)-2-(4-hydroxyphenyl)chroman-5,7-diol
-
4-(2-chlorophenylimino)-2-(4-hydroxyphenyl)chroman-5,7-diol
-
4-(2-chlorophenylimino)-2-(4-hydroxyphenyl)chroman-5,7-diol
-
4-(2-chlorophenylimino)-2-(4-hydroxyphenyl)chroman-5,7-diol
-
4-(2-chlorophenylimino)-2-(4-hydroxyphenyl)chroman-5,7-diol
-
4-(2-chlorophenylimino)-2-(4-hydroxyphenyl)chroman-5,7-diol
-
4-(2-chlorophenylimino)-2-(4-hydroxyphenyl)chroman-5,7-diol
-
4-(2-fluorophenylimino)-2-(4-hydroxyphenyl)chroman-5,7-diol
-
4-(2-fluorophenylimino)-2-(4-hydroxyphenyl)chroman-5,7-diol
-
4-(2-fluorophenylimino)-2-(4-hydroxyphenyl)chroman-5,7-diol
-
4-(2-fluorophenylimino)-2-(4-hydroxyphenyl)chroman-5,7-diol
-
4-(2-fluorophenylimino)-2-(4-hydroxyphenyl)chroman-5,7-diol
-
4-(2-fluorophenylimino)-2-(4-hydroxyphenyl)chroman-5,7-diol
-
5,5'-dithionitrobenzoic acid
-
irreversible inhibition
5,5'-dithionitrobenzoic acid
-
irreversible inhibition
5,5'-dithionitrobenzoic acid
-
irreversible inhibition
5,5'-dithionitrobenzoic acid
-
irreversible inhibition
5,5'-dithionitrobenzoic acid
-
inactivation reversed by dithiothreitol
5,5'-dithionitrobenzoic acid
-
irreversible inhibition
6,6'-Dithiodinicotinic acid
-
irreversible inhibition
6,6'-Dithiodinicotinic acid
-
irreversible inhibition
6,6'-Dithiodinicotinic acid
-
irreversible inhibition
6,6'-Dithiodinicotinic acid
-
irreversible inhibition
6,6'-Dithiodinicotinic acid
-
irreversible inhibition
6-diazo-5-oxo-L-norleucine
-
competitive with respect to L-glutamine
6-diazo-5-oxo-L-norleucine
-
-
6-diazo-5-oxo-L-norleucine
-
-
6-diazo-5-oxo-L-norleucine
2 mM
6-diazo-5-oxo-L-norleucine
-
-
6-diazo-5-oxo-L-norleucine
-
inhibitor of the glutamine binding site
6-diazo-5-oxo-L-norleucine
-
-
6-diazo-5-oxo-L-norleucine
-
-
6-diazo-5-oxo-L-norleucine
-
-
7-methoxy-2,3-dihydro-2-phenyl-4 quinolone
-
7-methoxy-2,3-dihydro-2-phenyl-4 quinolone
-
7-methoxy-2,3-dihydro-2-phenyl-4 quinolone
-
7-methoxy-2,3-dihydro-2-phenyl-4 quinolone
-
7-methoxy-2,3-dihydro-2-phenyl-4 quinolone
-
7-methoxy-2,3-dihydro-2-phenyl-4 quinolone
-
anticapsin
-
L-glutamine protects, irreversible inhibition
anticapsin
-
L-glutamine protects, irreversible inhibition
anticapsin
-
inhibitor of the glutamine binding site
anticapsin
-
L-glutamine protects, irreversible inhibition
anticapsin
-
L-glutamine protects, irreversible inhibition
azaserine
-
weak
catechin
-
cholest-5-en-3-yl 1,3-dioxo-1,1',2',3,5',6',7',7'a-octahydrospiro[indene-2,3'-pyrrolizine]-2'-carboxylate
-
cholest-5-en-3-yl 1,3-dioxo-1,1',2',3,5',6',7',7'a-octahydrospiro[indene-2,3'-pyrrolizine]-2'-carboxylate
-
-
cholest-5-en-3-yl 1,3-dioxo-1,1',2',3,5',6',7',7'a-octahydrospiro[indene-2,3'-pyrrolizine]-2'-carboxylate
-
cholest-5-en-3-yl 1,3-dioxo-1,1',2',3,5',6',7',7'a-octahydrospiro[indene-2,3'-pyrrolizine]-2'-carboxylate
-
-
cholest-5-en-3-yl 1-methyl-2-oxo-1,1',2,2',5',6',7',7'a-octahydrospiro[indole-3,3'-pyrrolizine]-2'-carboxylate
-
cholest-5-en-3-yl 1-methyl-2-oxo-1,1',2,2',5',6',7',7'a-octahydrospiro[indole-3,3'-pyrrolizine]-2'-carboxylate
-
-
cholest-5-en-3-yl 1-methyl-2-oxo-1,1',2,2',5',6',7',7'a-octahydrospiro[indole-3,3'-pyrrolizine]-2'-carboxylate
-
cholest-5-en-3-yl 1-methyl-2-oxo-1,1',2,2',5',6',7',7'a-octahydrospiro[indole-3,3'-pyrrolizine]-2'-carboxylate
-
-
cholest-5-en-3-yl 2-oxo-1',2',5',6',7',7'a-hexahydro-2H-spiro[acenaphthylene-1,3'-pyrrolizine]-2'-carboxylate
-
cholest-5-en-3-yl 2-oxo-1',2',5',6',7',7'a-hexahydro-2H-spiro[acenaphthylene-1,3'-pyrrolizine]-2'-carboxylate
-
-
cholest-5-en-3-yl 2-oxo-1',2',5',6',7',7'a-hexahydro-2H-spiro[acenaphthylene-1,3'-pyrrolizine]-2'-carboxylate
-
cholest-5-en-3-yl 2-oxo-1',2',5',6',7',7'a-hexahydro-2H-spiro[acenaphthylene-1,3'-pyrrolizine]-2'-carboxylate
-
-
cholest-5-en-3-yl 2-oxo-1,1',2,2',5',6',7',7'a-octahydrospiro[indole-3,3'-pyrrolizine]-2'-carboxylate
-
cholest-5-en-3-yl 2-oxo-1,1',2,2',5',6',7',7'a-octahydrospiro[indole-3,3'-pyrrolizine]-2'-carboxylate
-
-
cholest-5-en-3-yl 2-oxo-1,1',2,2',5',6',7',7'a-octahydrospiro[indole-3,3'-pyrrolizine]-2'-carboxylate
-
cholest-5-en-3-yl 2-oxo-1,1',2,2',5',6',7',7'a-octahydrospiro[indole-3,3'-pyrrolizine]-2'-carboxylate
-
-
cholest-5-en-3-yl 2-oxo-1-phenyl-1,1',2,2',5',6',7',7'a-octahydrospiro[indole-3,3'-pyrrolizine]-2'-carboxylate
-
cholest-5-en-3-yl 2-oxo-1-phenyl-1,1',2,2',5',6',7',7'a-octahydrospiro[indole-3,3'-pyrrolizine]-2'-carboxylate
-
-
cholest-5-en-3-yl 2-oxo-1-phenyl-1,1',2,2',5',6',7',7'a-octahydrospiro[indole-3,3'-pyrrolizine]-2'-carboxylate
-
cholest-5-en-3-yl 2-oxo-1-phenyl-1,1',2,2',5',6',7',7'a-octahydrospiro[indole-3,3'-pyrrolizine]-2'-carboxylate
-
-
cholest-5-en-3-yl 4,7-dichloro-2-oxo-1,1',2,2',5',6',7',7'a-octahydrospiro[indole-3,3'-pyrrolizine]-2'-carboxylate
-
cholest-5-en-3-yl 4,7-dichloro-2-oxo-1,1',2,2',5',6',7',7'a-octahydrospiro[indole-3,3'-pyrrolizine]-2'-carboxylate
-
-
cholest-5-en-3-yl 4,7-dichloro-2-oxo-1,1',2,2',5',6',7',7'a-octahydrospiro[indole-3,3'-pyrrolizine]-2'-carboxylate
-
cholest-5-en-3-yl 4,7-dichloro-2-oxo-1,1',2,2',5',6',7',7'a-octahydrospiro[indole-3,3'-pyrrolizine]-2'-carboxylate
-
-
cholest-5-en-3-yl 5,7-dibromo-2-oxo-1,1',2,2',5',6',7',7'a-octahydrospiro[indole-3,3'-pyrrolizine]-2'-carboxylate
-
cholest-5-en-3-yl 5,7-dibromo-2-oxo-1,1',2,2',5',6',7',7'a-octahydrospiro[indole-3,3'-pyrrolizine]-2'-carboxylate
-
-
cholest-5-en-3-yl 5,7-dibromo-2-oxo-1,1',2,2',5',6',7',7'a-octahydrospiro[indole-3,3'-pyrrolizine]-2'-carboxylate
-
cholest-5-en-3-yl 5,7-dibromo-2-oxo-1,1',2,2',5',6',7',7'a-octahydrospiro[indole-3,3'-pyrrolizine]-2'-carboxylate
-
-
cholest-5-en-3-yl 5-bromo-2-oxo-1,1',2,2',5',6',7',7'a-octahydrospiro[indole-3,3'-pyrrolizine]-2'-carboxylate
-
cholest-5-en-3-yl 5-bromo-2-oxo-1,1',2,2',5',6',7',7'a-octahydrospiro[indole-3,3'-pyrrolizine]-2'-carboxylate
-
-
cholest-5-en-3-yl 5-bromo-2-oxo-1,1',2,2',5',6',7',7'a-octahydrospiro[indole-3,3'-pyrrolizine]-2'-carboxylate
-
cholest-5-en-3-yl 5-bromo-2-oxo-1,1',2,2',5',6',7',7'a-octahydrospiro[indole-3,3'-pyrrolizine]-2'-carboxylate
-
-
iodoacetamide
-
irreversible inhibition
iodoacetamide
-
irreversible inhibition
iodoacetamide
-
irreversible inhibition
iodoacetamide
-
irreversible inhibition
iodoacetamide
-
irreversible inhibition
L-2,3-diaminopropanoic acid
-
-
L-2,3-diaminopropanoic acid
-
-
L-2,3-diaminopropanoic acid
-
-
L-ascorbic acid
-
luteolin
-
methylglyoxal
-
50% inhibition at 0.01 mM, non competitive
methylglyoxal
-
inhibits preincubated enzyme less profoundly than the untreated enzyme
N-ethylmaleimide
-
irreversible inhibition
N-ethylmaleimide
-
irreversible inhibition
N-ethylmaleimide
-
irreversible inhibition
N-ethylmaleimide
-
irreversible inhibition
N-ethylmaleimide
-
78% inhibition at1 mM
N-ethylmaleimide
-
irreversible inhibition
N3-(4-Methoxyfumaroyl)-L-2,3-diaminopropanoic acid
-
-
N3-(4-Methoxyfumaroyl)-L-2,3-diaminopropanoic acid
-
acts as active-site-directed inactivator blocking the N-terminal, glutamine-binding domain of the enzyme; inhibitor of the glutamine binding site
N3-(4-Methoxyfumaroyl)-L-2,3-diaminopropanoic acid
-
L-glutamine and some analogs protect
N3-(4-Methoxyfumaroyl)-L-2,3-diaminopropanoic acid
selective
N3-(4-Methoxyfumaroyl)-L-2,3-diaminopropanoic acid
-
N3-bromoacetyl-L-2,3-diaminopropanoic acid
-
competitive with respect to L-glutamine
N3-bromoacetyl-L-2,3-diaminopropanoic acid
-
competitive with respect to L-glutamine
N3-bromoacetyl-L-2,3-diaminopropanoic acid
-
competitive with respect to L-glutamine
N3-bromoacetyl-L-2,3-diaminopropanoic acid
-
inhibitor of the glutamine binding site
N3-chloroacetyl-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-chloroacetyl-L-2,3-diaminopropanoic acid
-
competitive with respect to L-glutamine
N3-fumaramoyl-L-2,3-diaminopropanoic acid
-
-
N3-fumaramoyl-L-2,3-diaminopropanoic acid
-
-
N3-fumaroyl-L-2,3-diaminopropanoic acid
-
-
N3-fumaroyl-L-2,3-diaminopropanoic acid
-
-
N3-fumarylcarboxyamido-L-2,3-diaminopropionic acid
-
competitive with L-glutamine
N3-fumarylcarboxyamido-L-2,3-diaminopropionic acid
-
-
N3-iodoacetyl-L-2,3-diaminopropanoic acid
-
competitive with respect to L-glutamine
N3-iodoacetyl-L-2,3-diaminopropanoic acid
-
competitive with respect to L-glutamine
N3-iodoacetyl-L-2,3-diaminopropanoic acid
-
competitive with respect to L-glutamine
naringenin
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
84% inhibition at 0.1 mM
UDP-N-acetylglucosamine
-
competitive with respect to D-fructose 6-phosphate, non-competitive with respect to L-glutamine
UDP-N-acetylglucosamine
-
partial
UDP-N-acetylglucosamine
-
feed-back inhibition
UDP-N-acetylglucosamine
-
weak
UDP-N-acetylglucosamine
-
-
UDP-N-acetylglucosamine
-
40% inhibition at 1 mM
UDP-N-acetylglucosamine
maximum inhibition at 1 mM
UDP-N-acetylglucosamine
-
competitive inhibitor with respect to D-fructose 6-phosphate
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
-
additional information
a series of covalent cholesterol-spiro pyrrolidine/pyrrolizidine heterocyclic hybrids possessing biologically active oxindole, indanedione, and acenaphthylene-1-one are synthesized as enzyme inhibitors by the reaction of C3-beta-cholesteroalacrylate with heterocyclic di- and tri-ketones, the compounds are obtained as a single isomer in good yield through a stereo- and regioselective 1,3-dipolar cycloaddition methodology, method overview. Analysis of in vitro antibacterial activity, and inhibitory activity against highly pathogenic Gram-positive and Gram-negative bacteria. Automated in silico molecular docking analysis of cadidates in order to validate their effective orientation as inhibitors bound in the active site of glucosamine-6-phosphate synthase (1XFF) enzyme
-
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
-
additional information
no inhibition by 0.1 mM c3, 4, 6, 9, 12, 13
-
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
-
additional information
-
a series of covalent cholesterol-spiro pyrrolidine/pyrrolizidine heterocyclic hybrids possessing biologically active oxindole, indanedione, and acenaphthylene-1-one are synthesized as enzyme inhibitors by the reaction of C3-beta-cholesteroalacrylate with heterocyclic di- and tri-ketones, the compounds are obtained as a single isomer in good yield through a stereo- and regioselective 1,3-dipolar cycloaddition methodology, method overview. Analysis of in vitro antibacterial activity, and inhibitory activity against highly pathogenic Gram-positive and Gram-negative bacteria. Automated in silico molecular docking analysis of cadidates in order to validate their effective orientation as inhibitors bound in the active site of glucosamine-6-phosphate synthase (1XFF) enzyme
-
additional information
a series of covalent cholesterol-spiro pyrrolidine/pyrrolizidine heterocyclic hybrids possessing biologically active oxindole, indanedione, and acenaphthylene-1-one are synthesized as enzyme inhibitors by the reaction of C3-beta-cholesteroalacrylate with heterocyclic di- and tri-ketones, the compounds are obtained as a single isomer in good yield through a stereo- and regioselective 1,3-dipolar cycloaddition methodology, method overview. Analysis of in vitro antibacterial activity, and inhibitory activity against highly pathogenic Gram-positive and Gram-negative bacteria. Automated in silico molecular docking analysis of cadidates in order to validate their effective orientation as inhibitors bound in the active site of glucosamine-6-phosphate synthase (1XFF) enzyme
-
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
-
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
-
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
-
a series of covalent cholesterol-spiro pyrrolidine/pyrrolizidine heterocyclic hybrids possessing biologically active oxindole, indanedione, and acenaphthylene-1-one are synthesized as enzyme inhibitors by the reaction of C3-beta-cholesteroalacrylate with heterocyclic di- and tri-ketones, the compounds are obtained as a single isomer in good yield through a stereo- and regioselective 1,3-dipolar cycloaddition methodology, method overview. Analysis of in vitro antibacterial activity, and inhibitory activity against highly pathogenic Gram-positive and Gram-negative bacteria. Automated in silico molecular docking analysis of cadidates in order to validate their effective orientation as inhibitors bound in the active site of glucosamine-6-phosphate synthase (1XFF) enzyme
-
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0.2 - 6.5
D-fructose 6-phosphate
16
D-glucose 6-phosphate
-
pH 7.2, 37°C, isomerization catalyzed by C-terminal domain
0.67
L-gamma -glutamyl-p-nitroanilide
-
reaction mixture contains 1 mM L-gamma-glutamyl-p-nitroanilide, 1 mM EDTA, 1 mM DTT and the appropriately diluted enzyme preparation in 20 mM HEPES buffer (pH 7.5) at 25°C
0.0064 - 12.2
L-gamma-glutamyl-p-nitroanilide
additional information
additional information
-
0.2
D-fructose 6-phosphate
-
wild type enzyme
0.23
D-fructose 6-phosphate
-
calorimetric determination, pH 7.2, 37°C
0.25
D-fructose 6-phosphate
-
pH 7.5, 37°C
0.3
D-fructose 6-phosphate
-
calorimetric determination, pH 7.2, 25°C
0.36
D-fructose 6-phosphate
wild-type, 37°C
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
0.38
D-fructose 6-phosphate
-
pH 7.7, 37°C
0.39
D-fructose 6-phosphate
-
pH 7.0, 37°C
0.4
D-fructose 6-phosphate
-
-
0.5
D-fructose 6-phosphate
-
pH 6.3, 38°C
0.5
D-fructose 6-phosphate
synthase activity, pH 7.2, 37°C
0.52
D-fructose 6-phosphate
-
mutant S243E, 37°C, pH 7.5
0.55
D-fructose 6-phosphate
recombinant enzyme, in 10 mM KCl, 1 mg/ml bovine serum albumin, 20 mM imidazole buffer (pH 6.8), 1 mM EDTA, 1 mM dithiothreitol, and 10% (v/v) glycerol
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
0.67
D-fructose 6-phosphate
mutant V605L, 37°C
0.75
D-fructose 6-phosphate
-
pH 7.0, 37°C
0.8
D-fructose 6-phosphate
hemisynthase activity, pH 7.2, 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
0.93
D-fructose 6-phosphate
mutant W74A, 37°C
1.04
D-fructose 6-phosphate
-
wild-type, 37°C, pH 7.5
1.08
D-fructose 6-phosphate
-
hexose phosphate-isomerizing activity, wild-type with N-terminal His-tag, pH 7.5, 25°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
1.11
D-fructose 6-phosphate
mutant W74L, 37°C
1.12
D-fructose 6-phosphate
-
mutant mutant Gfa1-His6DELTA655-660, pH 6.8, 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
1.15
D-fructose 6-phosphate
mutant A602L, 37°C
1.2
D-fructose 6-phosphate
-
reaction mixture contains 2 mM D-fructose 6-phosphate, 0.5 mM NADP+, 1 mM EDTA, and appropriately diluted GlcN-6-P synthase preparation in 50 mM Tris/HCl buffer (pH 7.5) at 25°C
1.2
D-fructose 6-phosphate
-
wild type enzyme, in in 25 mM potassium phosphate buffer at pH 7.0 and 37°C
1.2
D-fructose 6-phosphate
-
hexose phosphate-isomerizing activity, wild-type, pH 7.5, 25°C
1.4
D-fructose 6-phosphate
-
hexose phosphate-isomerizing activity, residues 346-712, His-tagged hexose phosphate-isomerizing domain, pH 7.5, 25°C
1.41
D-fructose 6-phosphate
-
glutamine 6-phosphate-synthetic activity, wild-type, pH 7.5, 25°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
1.45
D-fructose 6-phosphate
mutant W74F, 37°C
1.56
D-fructose 6-phosphate
-
wild-type, pH 6.8, 37°C
1.9
D-fructose 6-phosphate
-
mutant mutant Gfa1-K568H/S569H, pH 6.8, 37°C
2
D-fructose 6-phosphate
-
pH 7.5, 37°C
2
D-fructose 6-phosphate
-
pH 7.0, 37°C
2.6
D-fructose 6-phosphate
-
mutant Gfa1-His6DELTA343-348, pH 6.8, 37°C
2.8
D-fructose 6-phosphate
pH 7.0, 37°C
3.8
D-fructose 6-phosphate
-
pH 6.5, 30°C
3.8
D-fructose 6-phosphate
-
pH 7.2, 37°C, isomerization catalyzed by C-terminal domain
6.5
D-fructose 6-phosphate
-
hexose phosphate-isomerizing activity, wild-type with C-terminal His-tag, pH 7.5, 25°C
0.0064
L-gamma-glutamyl-p-nitroanilide
mutant W74F, 37°C
0.05
L-gamma-glutamyl-p-nitroanilide
wild-type, 37°C
0.1
L-gamma-glutamyl-p-nitroanilide
mutant W74L, 37°C
0.2
L-gamma-glutamyl-p-nitroanilide
mutant W74A, 37°C
0.29
L-gamma-glutamyl-p-nitroanilide
mutant V605L, 37°C
0.31
L-gamma-glutamyl-p-nitroanilide
-
residues 1-345, His-tagged glutamine amide-hydrolysing domain, pH 7.5, 25°C
0.36
L-gamma-glutamyl-p-nitroanilide
mutant A602L, 37°C
0.64
L-gamma-glutamyl-p-nitroanilide
-
wild-type with C-terminal His-tag, pH 7.5, 25°C
0.67
L-gamma-glutamyl-p-nitroanilide
-
wild-type, pH 7.5, 25°C
1.8
L-gamma-glutamyl-p-nitroanilide
-
both wild-type and mutant S243E, 37°C, pH 7.5
12.2
L-gamma-glutamyl-p-nitroanilide
-
wild-type with N-terminal His-tag, pH 7.5, 25°C
0.2
L-glutamate
-
calorimetric determination, pH 7.2, 25°C
0.34
L-glutamate
-
reaction mixture contains 10 mM L-glutamate, 1 mM EDTA, 1 mM DTT and an appropriately diluted enzyme preparation in 20 mM HEPES buffer (pH 7.5) at 25°C
1.33
L-glutamate
-
mutant Gfa1-K568H/S569H, pH 6.8, 37°C
1.36
L-glutamate
-
mutant Gfa1-His6DELTA343-348, pH 6.8, 37°C
1.41
L-glutamate
-
wild-type, pH 6.8, 37°C
2.36
L-glutamate
-
mutant Gfa1-His6DELTA655-660, pH 6.8, 37°C
0.04
L-glutamine
mutant enzyme W74L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C
0.04
L-glutamine
mutant W74L, 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
0.048
L-glutamine
mutant W74F, 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
0.072
L-glutamine
mutant V605L, 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
0.1
L-glutamine
mutant A602L, 37°C
0.11
L-glutamine
synthase activity, pH 7.2, 37°C
0.14
L-glutamine
hemisynthase activity, pH 7.2, 37°C
0.17
L-glutamine
-
wild type enzyme
0.2
L-glutamine
-
pH 7.5, 37°C
0.2
L-glutamine
-
pH 7.4, 37°C
0.225
L-glutamine
-
pH 7.5, 37°C
0.27
L-glutamine
wild-type, 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
0.3
L-glutamine
-
pH 7.5, 37°C
0.3
L-glutamine
-
pH 6.3, 38°C
0.34
L-glutamine
-
glutamine 6-phosphate-synthetic activity, wild-type, pH 7.5, 25°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
0.38
L-glutamine
mutant W74A, 37°C
0.4
L-glutamine
-
pH 7.5, 37°C
0.5
L-glutamine
-
pH 6.5, 30°C
0.6
L-glutamine
-
pH 7.5, 37°C
0.65
L-glutamine
-
pH 7.0, 37°C
0.74
L-glutamine
-
pH 7.0, 37°C
0.75
L-glutamine
recombinant enzyme, in 10 mM KCl, 1 mg/ml bovine serum albumin, 20 mM imidazole buffer (pH 6.8), 1 mM EDTA, 1 mM dithiothreitol, and 10% (v/v) glycerol
0.85
L-glutamine
-
pH 7.5, 37°C
1.6
L-glutamine
-
pH 7.7, 37°C
5.1
L-glutamine
pH 7.0, 55°C
additional information
additional information
thermodynamics
-
additional information
additional information
binding energy calculations of wild-type and mutant enzymes
-
additional information
additional information
-
binding energy calculations of wild-type and mutant enzymes
-
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0.004 - 35.5
D-fructose 6-phosphate
0.00092 - 0.68
L-gamma-glutamyl-p-nitroanilide
0.004
D-fructose 6-phosphate
-
hexose phosphate-isomerizing activity, wild-type with C-terminal His-tag, pH 7.5, 25°C
0.0092
D-fructose 6-phosphate
-
hexose phosphate-isomerizing activity, residues 346-712, His-tagged hexose phosphate-isomerizing domain, pH 7.5, 25°C
0.021
D-fructose 6-phosphate
-
hexose phosphate-isomerizing activity, wild-type with N-terminal His-tag, pH 7.5, 25°C
0.021
D-fructose 6-phosphate
-
hexose phosphate-isomerizing activity, wild-type, pH 7.5, 25°C
0.0213
D-fructose 6-phosphate
-
reaction mixture contains 2 mM D-fructose 6-phosphate, 0.5 mM NADP+, 1 mM EDTA, and appropriately diluted GlcN-6-P synthase preparation in 50 mM Tris/HCl buffer (pH 7.5) at 25°C
0.08
D-fructose 6-phosphate
mutant W74L, 37°C
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
0.12
D-fructose 6-phosphate
mutant W74A, 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
0.15
D-fructose 6-phosphate
mutant V605L, 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
0.22
D-fructose 6-phosphate
mutant A602L, 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
0.92
D-fructose 6-phosphate
mutant W74F, 37°C
9.9
D-fructose 6-phosphate
-
calorimetric determination, pH 7.2, 25°C
12
D-fructose 6-phosphate
-
calorimetric determination, pH 7.2, 37°C
14.4
D-fructose 6-phosphate
wild-type, 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
16.4
D-fructose 6-phosphate
hemisynthase activity, pH 7.2, 37°C
16.9
D-fructose 6-phosphate
synthase activity, pH 7.2, 37°C
35.5
D-fructose 6-phosphate
-
co-substrate: L-glutamine, pH 7.0, 37°C
0.00092
L-gamma-glutamyl-p-nitroanilide
-
wild-type with N-terminal His-tag, pH 7.5, 25°C
0.0075
L-gamma-glutamyl-p-nitroanilide
-
residues 1-345, His-tagged glutamine amide-hydrolysing domain, pH 7.5, 25°C
0.012
L-gamma-glutamyl-p-nitroanilide
-
wild-type, pH 7.5, 25°C
0.0123
L-gamma-glutamyl-p-nitroanilide
-
reaction mixture contains 1 mM L-gamma-glutamyl-p-nitroanilide, 1 mM EDTA, 1 mM DTT and the appropriately diluted enzyme preparation in 20 mM HEPES buffer (pH 7.5) at 25°C
0.013
L-gamma-glutamyl-p-nitroanilide
-
wild-type with C-terminal His-tag, pH 7.5, 25°C
0.13
L-gamma-glutamyl-p-nitroanilide
mutant V605L, 37°C
0.15
L-gamma-glutamyl-p-nitroanilide
mutant A602L, 37°C
0.17
L-gamma-glutamyl-p-nitroanilide
wild-type, 37°C
0.5
L-gamma-glutamyl-p-nitroanilide
mutant W74L, 37°C
0.67
L-gamma-glutamyl-p-nitroanilide
mutant W74F, 37°C
0.68
L-gamma-glutamyl-p-nitroanilide
mutant W74A, 37°C
9.81
L-glutamate
-
calorimetric determination, pH 7.2, 25°C
12
L-glutamate
-
reaction mixture contains 10 mM L-glutamate, 1 mM EDTA, 1 mM DTT and an appropriately diluted enzyme preparation in 20 mM HEPES buffer (pH 7.5) at 25°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
0.28
L-glutamine
mutant V605L, 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
0.38
L-glutamine
mutant A602L, 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
1.5
L-glutamine
mutant W74L, 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
L-glutamine
mutant W74A, 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
7.2
L-glutamine
mutant W74F, 37°C
12
L-glutamine
-
glutamine 6-phosphate-synthetic activity, wild-type, pH 7.5, 25°C
16.8
L-glutamine
hemisynthase activity, pH 7.2, 37°C
16.95
L-glutamine
synthase activity, pH 7.2, 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
17.2
L-glutamine
wild-type, 37°C
35.5
L-glutamine
-
co-substrate: D-fructose 6-phosphate, pH 7.0, 37°C
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A594G
site-directed mutagenesis, the mutant shows unaltered activity (5 U/l) compared to wild-type (5 U/l)
K595H
site-directed mutagenesis, the mutant shows unaltered activity (5 U/l) compared to wild-type (5 U/l)
L593S
site-directed mutagenesis, the mutant shows highly increased activity (48 U/l) compared to wild-type (5 U/l)
S596F
site-directed mutagenesis, the mutant shows slightly increased activity (7 U/l) compared to wild-type (5 U/l)
V597R
site-directed mutagenesis, the mutant shows slightly increased activity (8 U/l) compared to wild-type (5 U/l)
A594G
-
site-directed mutagenesis, the mutant shows unaltered activity (5 U/l) compared to wild-type (5 U/l)
-
K595H
-
site-directed mutagenesis, the mutant shows unaltered activity (5 U/l) compared to wild-type (5 U/l)
-
L593S
-
site-directed mutagenesis, the mutant shows highly increased activity (48 U/l) compared to wild-type (5 U/l)
-
S596F
-
site-directed mutagenesis, the mutant shows slightly increased activity (7 U/l) compared to wild-type (5 U/l)
-
G40A
-
mutant with exchanged guanine is inactive. The 2.7 A resolution crystal structure of the mutant shows that the RNA is in a conformation nearly identical to that of the wild-type glmS ribozyme. The experimental electron density maps indicate that GlcN6P binds to the G40A mutant in the same location as in the wild-type ribozyme. Raman pH titrations of GlcN6P using crystals of the G40A mutant glmS ribozyme show that the pKa of the amine of the ribozyme-bound GlcN6P differs substantially for the wild-type and G40A mutant ribozymes
A38T
-
mutant shows increased resistance against glucosamine-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
G471S
-
mutant shows increased resistance against glucosamine-6-phosphate
I271T
-
mutant shows increased resistance against glucosamine-6-phosphate
I3T
-
mutant shows increased resistance against glucosamine-6-phosphate
L468P
-
mutant shows increased resistance against glucosamine-6-phosphate
S449P
-
mutant shows increased resistance against glucosamine-6-phosphate
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
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
S243E
-
increase in activity, 2fold lower Km value for D-fructose 6-phosphate than wild-type
biotechnology
the recombinant enzyme expressed in Saccharomyces cereviaise reveals some differences from the wild type enzyme, such as improved stability and less sensitivity to UDP-GlcNAc
V711F
-
mutation results in an almost complete elimination of the GlcN-6-P-synthetic activity, with the retention of the amidohydrolase and sugar phosphate-isomerizing activities
V711F
-
reduction of the glucosamine 6-phosphate-synthetic activity, with the retention of the amidohydrolase and sugar phosphate-isomerizing activities
W97F
-
mutation results in an almost complete elimination of the GlcN-6-P synthetic activity, with the retention of the amidohydrolase and sugar phosphate-isomerizing activities
W97F
-
reduction of the glucosamine 6-phosphate-synthetic activity, with the retention of the amidohydrolase and sugar phosphate-isomerizing activities. Residue W97 functions as a molecular gate, opening and closing the intramolecular channel that connects the glutamine amide-hydrolysing and hexose phosphate-isomerizing domains
W97G
-
mutation results in an almost complete elimination of the GlcN-6-P-synthetic activity, with the retention of the amidohydrolase and sugar phosphate-isomerizing activities
W97G
-
almost complete elimination of the glucosamine 6-phosphate-synthetic activity, with the retention of the amidohydrolase and sugar phosphate-isomerizing activities. Residue W97 functions as a molecular gate, opening and closing the intramolecular channel that connects the glutamine amide-hydrolysing and hexose phosphate-isomerizing domains
C1A
-
C1A-GlmS does not reveal glutaminase activity at 37°C when tested in the presence of Gln only
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
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
efficiency of ammonia transfer is close to zero. No use of ammonia as a substrate
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
W74L
decrease in ammonia transfer, 5-7fold increase in the affinity for glutamine in the presence of fructose 6-phosphate
additional information
combinatorial fine-tuning of glucosamine-6-phosphate N-acetyltransferase (GNA1) and glutamine-fructose-6-phosphate aminotransferase (GlmS) expression by 5-terminus fusion engineering leads to overproduction of N-acetylglucosamine in Bacillus subtilis. Enhanced expression of GlmS is achieved at the transcriptional and translational levels by fusing an mRNA stabilizer to the 5'-terminus of GlmS gene. Under the control of GNA1 (fusion with cMyc tag and with the optimum RBS M-Rm) and GlmS (fusion with mRNA stabilizer DELTAermC+14/7A), the GlcNAc titer and yield in the shake flask increase to 18.5 g/l and 0.37 g GlcNAc/g glucose, which are 2.9fold and 2.3fold that of the control, respectively. Synthetic pathway fine-tuning method at the transcriptional and translational levels by combinatorial modulation of regulatory elements, including epitope tag, RBS sequence, and mRNA stabilizer, method evaluation, overview
additional information
-
combinatorial fine-tuning of glucosamine-6-phosphate N-acetyltransferase (GNA1) and glutamine-fructose-6-phosphate aminotransferase (GlmS) expression by 5-terminus fusion engineering leads to overproduction of N-acetylglucosamine in Bacillus subtilis. Enhanced expression of GlmS is achieved at the transcriptional and translational levels by fusing an mRNA stabilizer to the 5'-terminus of GlmS gene. Under the control of GNA1 (fusion with cMyc tag and with the optimum RBS M-Rm) and GlmS (fusion with mRNA stabilizer DELTAermC+14/7A), the GlcNAc titer and yield in the shake flask increase to 18.5 g/l and 0.37 g GlcNAc/g glucose, which are 2.9fold and 2.3fold that of the control, respectively. Synthetic pathway fine-tuning method at the transcriptional and translational levels by combinatorial modulation of regulatory elements, including epitope tag, RBS sequence, and mRNA stabilizer, method evaluation, overview
additional information
improvement of enzyme BsGlms activity through computer simulation and site saturation mutagenesis, method, overview
additional information
-
improvement of enzyme BsGlms activity through computer simulation and site saturation mutagenesis, method, overview
additional information
-
combinatorial fine-tuning of glucosamine-6-phosphate N-acetyltransferase (GNA1) and glutamine-fructose-6-phosphate aminotransferase (GlmS) expression by 5-terminus fusion engineering leads to overproduction of N-acetylglucosamine in Bacillus subtilis. Enhanced expression of GlmS is achieved at the transcriptional and translational levels by fusing an mRNA stabilizer to the 5'-terminus of GlmS gene. Under the control of GNA1 (fusion with cMyc tag and with the optimum RBS M-Rm) and GlmS (fusion with mRNA stabilizer DELTAermC+14/7A), the GlcNAc titer and yield in the shake flask increase to 18.5 g/l and 0.37 g GlcNAc/g glucose, which are 2.9fold and 2.3fold that of the control, respectively. Synthetic pathway fine-tuning method at the transcriptional and translational levels by combinatorial modulation of regulatory elements, including epitope tag, RBS sequence, and mRNA stabilizer, method evaluation, overview
-
additional information
-
improvement of enzyme BsGlms activity through computer simulation and site saturation mutagenesis, method, overview
-
additional information
-
expression of truncated enzyme variants as His-tagged proteins. Fragments encompassing residues 1-345 and 346-712 represent the functional glutamine amide-hydrolysing GAH and hexose phosphate-isomerizing domains ISOM, respectively. The native GAH domain is monomeric, whereas the native ISOM domain forms tetramers, as does the whole enzyme. The binding site for the feedback inhibitor, uridine 5'-diphospho-N-acetyl-D-glucosamine, is located in the ISOM domain. Inhibitor binding affects amidohydrolysing activity of the GAH domain and, as a consequence, the D-glucosamine-6-phosphate-synthetic activity of the whole enzyme. The fragment containing residues 218-283 is neither involved in ligand binding nor in protein oligomerization. An intramolecular channel connects the GAH and ISOM domains. The channel becomes leaky upon deletion of amino acids 709-712 and in the W97F and W97G mutants
additional information
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three recombinant versions containing internal oligoHis fragments are constructed: (a) by substituting residues 343-348 of the interdomain undecapeptide linker with hexaHis, (b) by replacing solvent-exposed residues 655-660 of the isomerase domain with hexaHis, and (c) by replacing amino acids at positions 568 and 569 with His residues to generate the three-dimensional hexaHis microdomain in the enzyme quaternary structure. The resulting constructs are purified to homogeneity. Catalytic properties are comparable with that of the wild-type enzyme. The construct containing the 655-660 hexaHis insert is found to be a homodimeric protein
additional information
Crispr-mediated elimination of Drosophila gfat genes and generation of single gene null mutations in the fly counterparts of gfat1 and gfat2 (gfat1-/- and gfat2-/-). Deletions for either enzyme are fully lethal and homozygotes lacking either GFAT1 or GFAT2 die at or prior to the first instar larval stage. When genetically eliminated, neither isoform is able to compensate for the other. Dietary supplementation with D-glucosamine-6-phosphate rescues GFAT2 deficiency and restores viability to gfat2-/- mutants. In contrast, glucosamine-6-phosphate does not rescue gfat1-/- animals
additional information
Crispr-mediated elimination of Drosophila gfat genes and generation of single gene null mutations in the fly counterparts of gfat1 and gfat2 (gfat1-/- and gfat2-/-). Deletions for either enzyme are fully lethal and homozygotes lacking either GFAT1 or GFAT2 die at or prior to the first instar larval stage. When genetically eliminated, neither isoform is able to compensate for the other. Dietary supplementation with D-glucosamine-6-phosphate rescues GFAT2 deficiency and restores viability to gfat2-/- mutants. In contrast, glucosamine-6-phosphate does not rescue gfat1-/- animals
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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)
brenda
Chen, P.; Visokay, S.; Abrams, J.M.
Drosophila GFAT1 and GFAT2 enzymes encode obligate developmental functions
Fly
14
3-9
2020
Drosophila melanogaster (Q32KF3), Drosophila melanogaster (Q9Y093)
brenda
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
29626-29638
2017
Escherichia coli (P17169)
-
brenda