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ATP + N-acetyl-D-hexosamine = ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
ATP + N-acetyl-D-hexosamine = ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
-
-
-
-
ATP + N-acetyl-D-hexosamine = ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
enzyme acts by a sequential bi bi (two substrates-two products) mechanism, with the reaction occurring after the binding of both ATP and N-acetylhexosamine
ATP + N-acetyl-D-hexosamine = ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
openclose conformational change at the active site, structure overview
ATP + N-acetyl-D-hexosamine = ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
regio- and stereoselectivity, catalytic mechanism, structure-function analysis, overview. Nucleophilic attack on the gamma-phosphate atom in a bond-breaking/bond formation manner of transfer (an SN2-like reaction). The carboxyl group of residue Asp208 within hydrogen-bond distance of C1 OH of GlcNAc/GalNAc is likely to serve as the active-site general base
-
ATP + N-acetyl-D-hexosamine = ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
regio- and stereoselectivity, catalytic mechanism, structure-function analysis, overview. Nucleophilic attack on the gamma-phosphate atom in a bond-breaking/bond formation manner of transfer (an SN2-like reaction). The carboxyl group of residue Asp208 within hydrogen-bond distance of C1 OH of GlcNAc/GalNAc is likely to serve as the active-site general base
ATP + N-acetyl-D-hexosamine = ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
the N-acetylhexosamine 1-kinase shows a concerted mechanism of two-magnesium-ion-assisted GlcNAc phosphorylation, flexibility behavior of lid motif upon substrate recognition, and water-assisted GlcNAc-1-P release
ATP + N-acetyl-D-hexosamine = ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
the N-acetylhexosamine 1-kinase shows a concerted mechanism of two-magnesium-ion-assisted GlcNAc phosphorylation, flexibility behavior of lid motif upon substrate recognition, and water-assisted GlcNAc-1-P release
-
-
ATP + N-acetyl-D-hexosamine = ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
the N-acetylhexosamine 1-kinase shows a concerted mechanism of two-magnesium-ion-assisted GlcNAc phosphorylation, flexibility behavior of lid motif upon substrate recognition, and water-assisted GlcNAc-1-P release
-
-
ATP + N-acetyl-D-hexosamine = ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
enzyme acts by a sequential bi bi (two substrates-two products) mechanism, with the reaction occurring after the binding of both ATP and N-acetylhexosamine
-
-
ATP + N-acetyl-D-hexosamine = ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
regio- and stereoselectivity, catalytic mechanism, structure-function analysis, overview. Nucleophilic attack on the gamma-phosphate atom in a bond-breaking/bond formation manner of transfer (an SN2-like reaction). The carboxyl group of residue Asp208 within hydrogen-bond distance of C1 OH of GlcNAc/GalNAc is likely to serve as the active-site general base
-
-
ATP + N-acetyl-D-hexosamine = ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
openclose conformational change at the active site, structure overview
-
-
ATP + N-acetyl-D-hexosamine = ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
the N-acetylhexosamine 1-kinase shows a concerted mechanism of two-magnesium-ion-assisted GlcNAc phosphorylation, flexibility behavior of lid motif upon substrate recognition, and water-assisted GlcNAc-1-P release
-
-
ATP + N-acetyl-D-hexosamine = ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
the N-acetylhexosamine 1-kinase shows a concerted mechanism of two-magnesium-ion-assisted GlcNAc phosphorylation, flexibility behavior of lid motif upon substrate recognition, and water-assisted GlcNAc-1-P release
-
-
ATP + N-acetyl-D-hexosamine = ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
regio- and stereoselectivity, catalytic mechanism, structure-function analysis, overview. Nucleophilic attack on the gamma-phosphate atom in a bond-breaking/bond formation manner of transfer (an SN2-like reaction). The carboxyl group of residue Asp208 within hydrogen-bond distance of C1 OH of GlcNAc/GalNAc is likely to serve as the active-site general base
-
-
ATP + N-acetyl-D-hexosamine = ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
the N-acetylhexosamine 1-kinase shows a concerted mechanism of two-magnesium-ion-assisted GlcNAc phosphorylation, flexibility behavior of lid motif upon substrate recognition, and water-assisted GlcNAc-1-P release
-
-
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ATP + 2-(acetylamino)-2-deoxy-D-allopyranose
ADP + 2-(acetylamino)-2-deoxy-D-allopyranose 1-phosphate
22% phosphorylation yield
-
-
?
ATP + 2-deoxy-2-azido-D-mannose
ADP + 2-deoxy-2-azido-alpha-D-mannose 1-phosphate
ATP + 2-deoxy-2-fluoro-D-mannose
ADP + 2-deoxy-2-fluoro-alpha-D-mannose 1-phosphate
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-alpha-D-glucose 1-phosphate
ATP + 4- deoxy-N-acetyl-D-glucosamine
ADP + 4-deoxy-N-acetyl-alpha-D-glucosamine 1-phosphate
-
50% phosphorylation yield
-
-
?
ATP + 4-deoxy-4-azido-N-acetyl-D-galactosamine
ADP + 4-deoxy-4-azido-N-acetyl-alpha-D-galactosamine 1-phosphate
-
73% phosphorylation yield
-
-
?
ATP + 4-deoxy-D-mannose
ADP + 4-deoxy-alpha-D-mannose 1-phosphate
ATP + 6-deoxy-6-azido-N-acetyl-D-galactosamine
ADP + 6-deoxy-6-azido-N-acetyl-alpha-D-galactosamine 1-phosphate
-
42% phosphorylation yield
-
-
?
ATP + 6-deoxy-6-azido-N-acetyl-D-glucosamine
ADP + 6-deoxy-6-azido-N-acetyl-alpha-D-glucosamine 1-phosphate
ATP + 6-deoxy-6-methyl-N-acetyl-D-glucosamine
ADP + 6-deoxy-6-methyl-N-acetyl-alpha-D-glucosamine 1-phosphate
ATP + 6-deoxy-N-acetyl-D-galactosamine
ADP + 6-deoxy-N-acetyl-alpha-D-galactosamine 1-phosphate
-
37% phosphorylation yield
-
-
?
ATP + 6-deoxy-N-acetyl-D-glucosamine
ADP + 6-deoxy-N-acetyl-alpha-D-glucosamine 1-phosphate
75% phosphorylation yield
-
-
?
ATP + 6-methyl-N-acetyl-D-mannosamine
ADP + 6-methyl-N-acetyl-alpha-D-mannosamine 1-phosphate
ATP + D-galactopyranose
ADP + alpha-D-galactopyranose 1-phosphate
-
below 5% phosphorylation yield
-
-
?
ATP + D-galactosamine
ADP + D-galactosamine 1-phosphate
ATP + D-galactose
ADP + D-galactose 1-phosphate
ATP + D-glucosamine
ADP + D-glucosamine 1-phosphate
-
-
-
?
ATP + D-glucose
ADP + D-glucose 1-phosphate
low activity
-
-
?
ATP + D-mannosamine
ADP + alpha-D-mannosamine 1-phosphate
-
-
-
?
ATP + D-mannose
ADP + alpha-D-mannose 1-phosphate
ATP + D-talose
?
phosphorylation at 3% of the activity with N-acetylglucosamine
-
-
?
ATP + mannose
ADP + mannose 1-phosphate
-
-
-
?
ATP + N-acetyl-alpha-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
ATP + N-acetyl-alpha-D-glucosamine
ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
ATP + N-acetyl-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
ATP + N-acetyl-D-hexosamine
ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
ATP + N-acetyl-D-mannosamine
?
phosphorylation at 15% of the activity with N-acetylglucosamine
-
-
?
ATP + N-acetyl-D-mannosamine
ADP + ?
-
-
-
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-alpha-D-mannosamine 1-phosphate
low activity
-
-
?
ATP + N-azidoacetyl-D-galactosamine
ADP + N-azidoacetyl-alpha-D-galactosamine 1-phosphate
-
65% phosphorylation yield
-
-
?
ATP + N-azidoacetyl-D-glucosamine
ADP + N-azidoacetyl-alpha-D-glucosamine 1-phosphate
87% phosphorylation yield
-
-
?
ATP + N-benzoyl-alpha-D-galactosamine
ADP + N-benzoyl-alpha-D-galactosamine 1-phosphate
ATP + N-butanoyl-D-galactosamine
ADP + N-butanoyl-alpha-D-galactosamine 1-phosphate
ATP + N-butanoyl-D-glucosamine
ADP + N-butanoyl-alpha-D-glucosamine 1-phosphate
ATP + N-phenylacetyl-D-galactosamine
ADP + N-phenylacetyl-alpha-D-galactosamine 1-phosphate
-
77% phosphorylation yield
-
-
?
ATP + N-phenylacetyl-D-glucosamine
ADP + N-phenylacetyl-alpha-D-glucosamine 1-phosphate
88% phosphorylation yield
-
-
?
ATP + N-propionyl-D-galactosamine
ADP + N-propionyl-alpha-D-galactosamine 1-phosphate
-
85% phosphorylation yield
-
-
?
ATP + N-propionyl-D-glucosamine
ADP + N-propionyl-alpha-D-glucosamine 1-phosphate
86% phosphorylation yield
-
-
?
ATP + N-trifluoroacetyl-alpha-D-galactosamine
ADP + N-trifluoroacetyl-alpha-D-galactosamine 1-phosphate
-
0.75 microM, 21.8% conversion
-
-
?
ATP + N-trifluoroacetyl-D-glucosamine
ADP + N-trifluoroacetyl-alpha-D-glucosamine 1-phosphate
-
recombinant enzyme
-
-
?
GTP + N-acetyl-alpha-D-glucosamine
GDP + N-acetyl-alpha-D-glucosamine 1-phosphate
GTP shows about 45% of the activity with ATP
-
-
?
ITP + N-acetyl-alpha-D-glucosamine
IDP + N-acetyl-alpha-D-glucosamine 1-phosphate
ITP shows about 30% of the activity with ATP
-
-
?
additional information
?
-
ATP + 2-deoxy-2-azido-D-mannose
ADP + 2-deoxy-2-azido-alpha-D-mannose 1-phosphate
-
0.75 microM, 40.2% conversion
-
-
?
ATP + 2-deoxy-2-azido-D-mannose
ADP + 2-deoxy-2-azido-alpha-D-mannose 1-phosphate
-
0.75 microM, 53.3% conversion
-
-
?
ATP + 2-deoxy-2-azido-D-mannose
ADP + 2-deoxy-2-azido-alpha-D-mannose 1-phosphate
-
0.75 microM, 53.3% conversion
-
-
?
ATP + 2-deoxy-2-fluoro-D-mannose
ADP + 2-deoxy-2-fluoro-alpha-D-mannose 1-phosphate
-
0.75 microM, 47.0% conversion
-
-
?
ATP + 2-deoxy-2-fluoro-D-mannose
ADP + 2-deoxy-2-fluoro-alpha-D-mannose 1-phosphate
-
0.75 microM, 44.4% conversion
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-alpha-D-glucose 1-phosphate
-
0.75 microM, 28.4% conversion
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-alpha-D-glucose 1-phosphate
-
0.75 microM, 44.8% conversion
-
-
?
ATP + 4-deoxy-D-mannose
ADP + 4-deoxy-alpha-D-mannose 1-phosphate
-
0.75 microM, 23.9% conversion
-
-
?
ATP + 4-deoxy-D-mannose
ADP + 4-deoxy-alpha-D-mannose 1-phosphate
-
0.75 microM, 37.1% conversion
-
-
?
ATP + 6-deoxy-6-azido-N-acetyl-D-glucosamine
ADP + 6-deoxy-6-azido-N-acetyl-alpha-D-glucosamine 1-phosphate
34% phosphorylation yield
-
-
?
ATP + 6-deoxy-6-azido-N-acetyl-D-glucosamine
ADP + 6-deoxy-6-azido-N-acetyl-alpha-D-glucosamine 1-phosphate
-
0.75 microM, 23.4% conversion
-
-
?
ATP + 6-deoxy-6-azido-N-acetyl-D-glucosamine
ADP + 6-deoxy-6-azido-N-acetyl-alpha-D-glucosamine 1-phosphate
-
0.75 microM, 23.4% conversion
-
-
?
ATP + 6-deoxy-6-azido-N-acetyl-D-glucosamine
ADP + 6-deoxy-6-azido-N-acetyl-alpha-D-glucosamine 1-phosphate
-
0.75 microM, 37.2% conversion
-
-
?
ATP + 6-deoxy-6-azido-N-acetyl-D-glucosamine
ADP + 6-deoxy-6-azido-N-acetyl-alpha-D-glucosamine 1-phosphate
-
0.75 microM, 37.2% conversion
-
-
?
ATP + 6-deoxy-6-methyl-N-acetyl-D-glucosamine
ADP + 6-deoxy-6-methyl-N-acetyl-alpha-D-glucosamine 1-phosphate
-
0.75 microM, 36.3% conversion
-
-
?
ATP + 6-deoxy-6-methyl-N-acetyl-D-glucosamine
ADP + 6-deoxy-6-methyl-N-acetyl-alpha-D-glucosamine 1-phosphate
-
0.75 microM, 41.8% conversion
-
-
?
ATP + 6-methyl-N-acetyl-D-mannosamine
ADP + 6-methyl-N-acetyl-alpha-D-mannosamine 1-phosphate
-
0.75 microM, 28.6% conversion
-
-
?
ATP + 6-methyl-N-acetyl-D-mannosamine
ADP + 6-methyl-N-acetyl-alpha-D-mannosamine 1-phosphate
-
0.75 microM, 32.6% conversion
-
-
?
ATP + D-galactosamine
ADP + D-galactosamine 1-phosphate
low activity
-
-
?
ATP + D-galactosamine
ADP + D-galactosamine 1-phosphate
low activity
-
-
?
ATP + D-galactose
ADP + D-galactose 1-phosphate
low activity
-
-
?
ATP + D-galactose
ADP + D-galactose 1-phosphate
low activity
-
-
?
ATP + D-mannose
?
phosphorylation at 1.6% of the activity with N-acetylglucosamine
-
-
?
ATP + D-mannose
?
phosphorylation at 1.6% of the activity with N-acetylglucosamine
-
-
?
ATP + D-mannose
ADP + alpha-D-mannose 1-phosphate
-
0.75 microM, 37.1% conversion
-
-
?
ATP + D-mannose
ADP + alpha-D-mannose 1-phosphate
-
0.75 microM, 68.0% conversion
-
-
?
ATP + N-acetyl-alpha-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
-
?
ATP + N-acetyl-alpha-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
the enzyme is involved in the lacto-N-biose I/galacto-N-biose degradation pathway
-
-
?
ATP + N-acetyl-alpha-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
phosphorylation at 60% of the activity with N-acetylglucosamine
-
-
?
ATP + N-acetyl-alpha-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
lacto-N-biose I/galacto-N-biose metabolic pathway
-
-
?
ATP + N-acetyl-alpha-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
-
?
ATP + N-acetyl-alpha-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
the enzyme is involved in the lacto-N-biose I/galacto-N-biose degradation pathway
-
-
?
ATP + N-acetyl-alpha-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
phosphorylation at 60% of the activity with N-acetylglucosamine
-
-
?
ATP + N-acetyl-alpha-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
lacto-N-biose I/galacto-N-biose metabolic pathway
-
-
?
ATP + N-acetyl-alpha-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
-
?
ATP + N-acetyl-alpha-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
-
?
ATP + N-acetyl-alpha-D-glucosamine
ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
ATP + N-acetyl-alpha-D-glucosamine
ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-alpha-D-glucosamine
ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
the enzyme is involved in the lacto-N-biose I/galacto-N-biose degradation pathway
-
-
?
ATP + N-acetyl-alpha-D-glucosamine
ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
0.75 microM, 42.3% conversion
-
-
?
ATP + N-acetyl-alpha-D-glucosamine
ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
0.75 microM, 42.3% conversion
-
-
?
ATP + N-acetyl-alpha-D-glucosamine
ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
0.75 microM, 35.4% conversion
-
-
?
ATP + N-acetyl-alpha-D-glucosamine
ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
0.75 microM, 35.4% conversion
-
-
?
ATP + N-acetyl-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
best substrate
-
-
?
ATP + N-acetyl-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
78% phosphorylation yield
-
-
?
ATP + N-acetyl-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
78% phosphorylation yield
-
-
?
ATP + N-acetyl-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
best substrate
-
-
?
ATP + N-acetyl-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
-
?
ATP + N-acetyl-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
-
?
ATP + N-acetyl-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
high activity
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
90% phosphorylation yield
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
high activity
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
recombinant enzyme
-
-
?
ATP + N-acetyl-D-hexosamine
ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-hexosamine
ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
-
-
-
?
ATP + N-acetyl-D-hexosamine
ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
-
-
-
-
?
ATP + N-acetyl-D-hexosamine
ADP + N-acetyl-alpha-D-hexosamine 1-phosphate
-
-
-
-
?
ATP + N-benzoyl-alpha-D-galactosamine
ADP + N-benzoyl-alpha-D-galactosamine 1-phosphate
-
0.75 microM, 51.9% conversion
-
-
?
ATP + N-benzoyl-alpha-D-galactosamine
ADP + N-benzoyl-alpha-D-galactosamine 1-phosphate
-
0.75 microM, 62.2% conversion
-
-
?
ATP + N-butanoyl-D-galactosamine
ADP + N-butanoyl-alpha-D-galactosamine 1-phosphate
-
86% phosphorylation yield
-
-
?
ATP + N-butanoyl-D-galactosamine
ADP + N-butanoyl-alpha-D-galactosamine 1-phosphate
-
0.75 microM, 24.0% conversion
-
-
?
ATP + N-butanoyl-D-galactosamine
ADP + N-butanoyl-alpha-D-galactosamine 1-phosphate
-
0.75 microM, 24.0% conversion
-
-
?
ATP + N-butanoyl-D-glucosamine
ADP + N-butanoyl-alpha-D-glucosamine 1-phosphate
87% phosphorylation yield
-
-
?
ATP + N-butanoyl-D-glucosamine
ADP + N-butanoyl-alpha-D-glucosamine 1-phosphate
-
0.75 microM, 35.0% conversion
-
-
?
ATP + N-butanoyl-D-glucosamine
ADP + N-butanoyl-alpha-D-glucosamine 1-phosphate
-
0.75 microM, 35.0% conversion
-
-
?
ATP + N-butanoyl-D-glucosamine
ADP + N-butanoyl-alpha-D-glucosamine 1-phosphate
-
0.75 microM, 20.9% conversion
-
-
?
ATP + N-butanoyl-D-glucosamine
ADP + N-butanoyl-alpha-D-glucosamine 1-phosphate
-
0.75 microM, 20.9% conversion
-
-
?
additional information
?
-
slightly active with D-talose, D-mannose, GTP, ITP
-
-
?
additional information
?
-
-
slightly active with D-talose, D-mannose, GTP, ITP
-
-
?
additional information
?
-
enzyme demonstrates a relaxed specificity when modifications are of the N-acyl type but also shows a much more limited tolerance for 6-modifications, N-acetylglucosamine 3- and 4-epimers can also be recognized by this enzyme
-
-
?
additional information
?
-
substrate binding structures, overview. No activity with glucuronic acid, galacturonic acid, 6-azidoglucose, 6-GlcNAc, 3-glucosamine, 4-glucosamine, and 6-glucosamine
-
-
?
additional information
?
-
-
substrate binding structures, overview. No activity with glucuronic acid, galacturonic acid, 6-azidoglucose, 6-GlcNAc, 3-glucosamine, 4-glucosamine, and 6-glucosamine
-
-
?
additional information
?
-
slightly active with D-talose, D-mannose, GTP, ITP
-
-
?
additional information
?
-
substrate binding structures, overview. No activity with glucuronic acid, galacturonic acid, 6-azidoglucose, 6-GlcNAc, 3-glucosamine, 4-glucosamine, and 6-glucosamine
-
-
?
additional information
?
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substrate binding structures, overview
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additional information
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substrate binding structures, overview
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additional information
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GlcNAc/GalNAc is phosphorylated to GlcNAc1P/GalNAc1P by N-acetylhexosamine 1-kinase (NahK), which acts on either
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additional information
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GlcNAc/GalNAc is phosphorylated to GlcNAc1P/GalNAc1P by N-acetylhexosamine 1-kinase (NahK), which acts on either
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additional information
?
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GlcNAc/GalNAc is phosphorylated to GlcNAc1P/GalNAc1P by N-acetylhexosamine 1-kinase (NahK), which acts on either
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additional information
?
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GlcNAc/GalNAc is phosphorylated to GlcNAc1P/GalNAc1P by N-acetylhexosamine 1-kinase (NahK), which acts on either
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additional information
?
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GlcNAc/GalNAc is phosphorylated to GlcNAc1P/GalNAc1P by N-acetylhexosamine 1-kinase (NahK), which acts on either
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additional information
?
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GlcNAc/GalNAc is phosphorylated to GlcNAc1P/GalNAc1P by N-acetylhexosamine 1-kinase (NahK), which acts on either
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evolution
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the enzyme belongs to the sugar kinase-Hsp70-actin superfamily
evolution
the enzyme belongs to the sugar kinase-Hsp70-actin superfamily
evolution
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the enzyme belongs to the sugar kinase-Hsp70-actin superfamily
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evolution
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the enzyme belongs to the sugar kinase-Hsp70-actin superfamily
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metabolism
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the enzyme is part of the LNB/GNB pathway in bifidobacteria, overview
metabolism
the enzyme is part of the LNB/GNB pathway in bifidobacteria, overview
metabolism
the enzyme is involved in the lacto-N-biose I (LNB) metabolic pathway catalyzing the phosphorylation of GlcNAc/GalNAc to GlcNAc1P/GalNAc1P , overview
metabolism
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the enzyme is involved in the lacto-N-biose I (LNB) metabolic pathway catalyzing the phosphorylation of GlcNAc/GalNAc to GlcNAc1P/GalNAc1P , overview
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metabolism
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the enzyme is involved in the lacto-N-biose I (LNB) metabolic pathway catalyzing the phosphorylation of GlcNAc/GalNAc to GlcNAc1P/GalNAc1P , overview
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metabolism
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the enzyme is part of the LNB/GNB pathway in bifidobacteria, overview
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metabolism
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the enzyme is involved in the lacto-N-biose I (LNB) metabolic pathway catalyzing the phosphorylation of GlcNAc/GalNAc to GlcNAc1P/GalNAc1P , overview
-
metabolism
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the enzyme is involved in the lacto-N-biose I (LNB) metabolic pathway catalyzing the phosphorylation of GlcNAc/GalNAc to GlcNAc1P/GalNAc1P , overview
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metabolism
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the enzyme is part of the LNB/GNB pathway in bifidobacteria, overview
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metabolism
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the enzyme is involved in the lacto-N-biose I (LNB) metabolic pathway catalyzing the phosphorylation of GlcNAc/GalNAc to GlcNAc1P/GalNAc1P , overview
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physiological function
the N-acetylhexosamine 1-kinase (NahK) is the typical example of anomeric kinases acting on gluco-type substrate, which catalyzes the phosphorylation of GlcNAc or GalNAc at anomeric C1 position with ATP, playing a crucial role in Bifidobacteria metabolic pathway and biosynthesis of sugar 1-phosphates and oligosaccharides
physiological function
-
the N-acetylhexosamine 1-kinase (NahK) is the typical example of anomeric kinases acting on gluco-type substrate, which catalyzes the phosphorylation of GlcNAc or GalNAc at anomeric C1 position with ATP, playing a crucial role in Bifidobacteria metabolic pathway and biosynthesis of sugar 1-phosphates and oligosaccharides
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physiological function
-
the N-acetylhexosamine 1-kinase (NahK) is the typical example of anomeric kinases acting on gluco-type substrate, which catalyzes the phosphorylation of GlcNAc or GalNAc at anomeric C1 position with ATP, playing a crucial role in Bifidobacteria metabolic pathway and biosynthesis of sugar 1-phosphates and oligosaccharides
-
physiological function
-
the N-acetylhexosamine 1-kinase (NahK) is the typical example of anomeric kinases acting on gluco-type substrate, which catalyzes the phosphorylation of GlcNAc or GalNAc at anomeric C1 position with ATP, playing a crucial role in Bifidobacteria metabolic pathway and biosynthesis of sugar 1-phosphates and oligosaccharides
-
physiological function
-
the N-acetylhexosamine 1-kinase (NahK) is the typical example of anomeric kinases acting on gluco-type substrate, which catalyzes the phosphorylation of GlcNAc or GalNAc at anomeric C1 position with ATP, playing a crucial role in Bifidobacteria metabolic pathway and biosynthesis of sugar 1-phosphates and oligosaccharides
-
physiological function
-
the N-acetylhexosamine 1-kinase (NahK) is the typical example of anomeric kinases acting on gluco-type substrate, which catalyzes the phosphorylation of GlcNAc or GalNAc at anomeric C1 position with ATP, playing a crucial role in Bifidobacteria metabolic pathway and biosynthesis of sugar 1-phosphates and oligosaccharides
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additional information
nucleotide binding site structures of NahK-ATP and Nahk-ADP, overview
additional information
ab initio QM/MM MD and MM MD simulations and one-dimensional and two-dimensional free energy profiles to descript catalytic process, substrate binding structure determination and analysis, overview
additional information
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ab initio QM/MM MD and MM MD simulations and one-dimensional and two-dimensional free energy profiles to descript catalytic process, substrate binding structure determination and analysis, overview
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additional information
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ab initio QM/MM MD and MM MD simulations and one-dimensional and two-dimensional free energy profiles to descript catalytic process, substrate binding structure determination and analysis, overview
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additional information
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nucleotide binding site structures of NahK-ATP and Nahk-ADP, overview
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additional information
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ab initio QM/MM MD and MM MD simulations and one-dimensional and two-dimensional free energy profiles to descript catalytic process, substrate binding structure determination and analysis, overview
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additional information
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ab initio QM/MM MD and MM MD simulations and one-dimensional and two-dimensional free energy profiles to descript catalytic process, substrate binding structure determination and analysis, overview
-
additional information
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ab initio QM/MM MD and MM MD simulations and one-dimensional and two-dimensional free energy profiles to descript catalytic process, substrate binding structure determination and analysis, overview
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D208 A
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
D208A
site-directed mutagenesis, the mutant shows altered activity and kinetics compared to the wild-type enzyme
D208A/K210A
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
D208A/K210L
site-directed mutagenesis, the mutant shows highly reduced activity and altered substrate specificity compared to the wild-type
D208L
site-directed mutagenesis, the mutant shows highly reduced activity and altered substrate specificity compared to the wild-type
D228A
site-directed mutagenesis, the mutant shows altered activity and kinetics compared to the wild-type enzyme
I146E
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
I146E/T231E
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
K210E
site-directed mutagenesis, the mutant shows reduced highly activity and altered substrate specificity compared to the wild-type
K210L
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
N213A
site-directed mutagenesis, the mutant shows altered activity and kinetics compared to the wild-type enzyme
Q48A
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
R306A
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
R306A/Y317A
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
R306E
site-directed mutagenesis, the mutant shows highly reduced activity but unaltered substrate specificity compared to the wild-type
R306E/Y317F
site-directed mutagenesis, the mutant shows highly reduced activity but unaltered substrate specificity compared to the wild-type
T231 E
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
Y317A
site-directed mutagenesis, the mutant shows similar activity but slightly altered substrate specificity compared to the wild-type
Y317F
site-directed mutagenesis, the mutant shows similar activity but slightly altered substrate specificity compared to the wild-type
D208A
-
site-directed mutagenesis, the mutant shows altered activity and kinetics compared to the wild-type enzyme
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D228A
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site-directed mutagenesis, the mutant shows altered activity and kinetics compared to the wild-type enzyme
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K210A
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site-directed mutagenesis, the mutant shows altered activity and kinetics compared to the wild-type enzyme
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N213A
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site-directed mutagenesis, the mutant shows altered activity and kinetics compared to the wild-type enzyme
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Q48A
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site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
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R306A
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site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
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R306E
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site-directed mutagenesis, the mutant shows highly reduced activity but unaltered substrate specificity compared to the wild-type
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Y317A
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site-directed mutagenesis, the mutant shows similar activity but slightly altered substrate specificity compared to the wild-type
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Y317F
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site-directed mutagenesis, the mutant shows similar activity but slightly altered substrate specificity compared to the wild-type
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D208A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
D208E
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
D208N
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
F247A
site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
H31A
site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
H31V
site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
I24A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
I24V
site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
D208A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
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D208N
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site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
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F247A
-
site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
-
H31A
-
site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
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H31V
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site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
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D208A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
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D208N
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site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
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F247A
-
site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
-
H31A
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site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
-
H31V
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site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
-
D208A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
-
D208N
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
-
F247A
-
site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
-
H31A
-
site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
-
H31V
-
site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
-
D208A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
-
D208N
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
-
F247A
-
site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
-
H31A
-
site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
-
H31V
-
site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
-
D208A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
-
D208N
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
-
F247A
-
site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
-
H31A
-
site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
-
H31V
-
site-directed mutagenesis, the mutant shows altered pH optimum of pH 7.0 as compared to wild-type optimum of pH 7.5
-
K210A
site-directed mutagenesis, the mutant shows altered activity and kinetics compared to the wild-type enzyme
K210A
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to the wild-type
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Nishimoto, M.; Kitaoka, M.
Identification of N-acetylhexosamine 1-kinase in the complete lacto-N-biose I/galacto-N-biose metabolic pathway in Bifidobacterium longum
Appl. Environ. Microbiol.
73
6444-6449
2007
Bifidobacterium longum (E8MF12), Bifidobacterium longum, Bifidobacterium longum JCM 1217 (E8MF12)
brenda
Cai, L.; Guan, W.; Wang, W.; Zhao, W.; Kitaoka, M.; Shen, J.; ONeil, C.; Wang, P.G.
Substrate specificity of N-acetylhexosamine kinase towards N-acetylgalactosamine derivatives
Bioorg. Med. Chem. Lett.
19
5433-5435
2009
Bifidobacterium longum
brenda
Cai, L.; Guan, W.; Kitaoka, M.; Shen, J.; Xia, C.; Chen, W.; Wang, P.G.
A chemoenzymatic route to N-acetylglucosamine-1-phosphate analogues: substrate specificity investigations of N-acetylhexosamine 1-kinase
Chem. Commun. (Camb. )
2009
2944-2946
2009
Bifidobacterium longum (E8MF12)
brenda
Li, Y.; Yu, H.; Chen, Y.; Lau, K.; Cai, L.; Cao, H.; Tiwari, V.; Qu, J.; Thon, V.; Wang, P.; Chen, X.
Substrate promiscuity of N-acetylhexosamine 1-kinases
Molecules
16
6396-6407
2011
Bifidobacterium longum subsp. infantis, Bifidobacterium longum, Bifidobacterium longum subsp. infantis ATCC 15697, Bifidobacterium longum ATCC 55813
brenda
Li, L.; Liu, Y.; Wan, Y.; Li, Y.; Chen, X.; Zhao, W.; Wang, P.G.
Efficient enzymatic synthesis of guanosine 5'-diphosphate-sugars and derivatives
Org. Lett.
15
5528-5530
2013
Bifidobacterium longum subsp. infantis
brenda
Wang, K.C.; Lyu, S.Y.; Liu, Y.C.; Chang, C.Y.; Wu, C.J.; Li, T.L.
Insights into the binding specificity and catalytic mechanism of N-acetylhexosamine 1-phosphate kinases through multiple reaction complexes
Acta Crystallogr. Sect. D
70
1401-1410
2014
Bifidobacterium longum subsp. infantis, Bifidobacterium longum (E8MF12), Bifidobacterium longum, Bifidobacterium longum JCM 1217 (E8MF12), Bifidobacterium longum subsp. infantis ATCC 15697
brenda
Sato, M.; Arakawa, T.; Nam, Y.W.; Nishimoto, M.; Kitaoka, M.; Fushinobu, S.
Open-close structural change upon ligand binding and two magnesium ions required for the catalysis of N-acetylhexosamine 1-kinase
Biochim. Biophys. Acta
1854
333-340
2015
Bifidobacterium longum (E8MF12), Bifidobacterium longum JCM 1217 (E8MF12)
brenda
Li, X.; Qi, C.; Wei, P.; Huang, L.; Cai, J.; Xu, Z.
Efficient chemoenzymatic synthesis of uridine 5-diphosphate N-acetylglucosamine and uridine 5-diphosphate N-trifluoacetyl glucosamine with three recombinant enzymes
Prep. Biochem. Biotechnol.
47
852-859
2017
Escherichia coli
brenda
Nishimoto, M.
Large scale production of lacto-N-biose I, a building block of type I human milk oligosaccharides, using sugar phosphorylases
Biosci. Biotechnol. Biochem.
84
17-24
2020
Bifidobacterium longum subsp. Longum (E8MF12), Bifidobacterium longum subsp. Longum JCM 1217 (E8MF12), Bifidobacterium longum subsp. Longum ATCC 15707 (E8MF12), Bifidobacterium longum subsp. Longum DSM 20219 (E8MF12), Bifidobacterium longum subsp. Longum NCTC 11818 (E8MF12), Bifidobacterium longum subsp. Longum E194b (E8MF12)
brenda
Zhao, Y.; She, N.; Ma, Y.; Wang, C.; Cao, Z.
A description of enzymatic catalysis in N-acetylhexosamine 1-kinase concerted mechanism of two-magnesium-ion-assisted GlcNAc phosphorylation, flexibility behavior of lid motif upon substrate recognition, and water-assisted GlcNAc-1-P release
ACS Catal.
8
4143-4159
2018
Bifidobacterium longum subsp. Longum (E8MF12), Bifidobacterium longum subsp. Longum JCM 1217 (E8MF12), Bifidobacterium longum subsp. Longum ATCC 15707 (E8MF12), Bifidobacterium longum subsp. Longum DSM 20219 (E8MF12), Bifidobacterium longum subsp. Longum NCTC 11818 (E8MF12), Bifidobacterium longum subsp. Longum E194b (E8MF12)
-
brenda
Guan, W.; Bai, J.; Zhou, T.; Zhao, B.
Active sites of N-acetylhexosamine 1-kinase from Bifidobacterium longum
Wei Sheng Wu Xue Bao
56
68-77
2016
Bifidobacterium longum subsp. Longum (E8MF12), Bifidobacterium longum subsp. Longum JCM 1217 (E8MF12), Bifidobacterium longum subsp. Longum ATCC 15707 (E8MF12), Bifidobacterium longum subsp. Longum DSM 20219 (E8MF12), Bifidobacterium longum subsp. Longum NCTC 11818 (E8MF12), Bifidobacterium longum subsp. Longum E194b (E8MF12)
-
brenda