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Information on EC 2.7.1.162 - N-acetylhexosamine 1-kinase
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2.7.1.162 N-acetylhexosamine 1-kinaseIUBMB Comments
This enzyme is involved in the lacto-N-biose I/galacto-N-biose degradation pathway in the probiotic bacterium Bifidobacterium longum. Differs from EC 2.7.1.157, N-acetylgalactosamine kinase, as it can phosphorylate both N-acetylgalactosamine and N-acetylglucosamine at similar rates. Also has some activity with N-acetyl-D-mannosamine, D-talose and D-mannose as substrate. ATP can be replaced by GTP or ITP but with decreased enzyme activity. Requires a divalent cation, with Mg2+ resulting in by far the greatest stimulation of enzyme activity.
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Word Map
- 2.7.1.162
- n-acetylglucosamine
- galnac
- longum
- udp-glcnac
- uridyltransferase
-
chemoenzymatic
-
bifidobacteria
- pyrophosphatase
-
one-pot
- 5'-diphosphate
-
three-enzyme
- galacto-n-biose
- oligosaccharide
- milk
- infantis
- uridine
- synthesis
- glycosyltransferases
- utp
- n-acetylgalactosamine
-
anomeric
- udp-n-acetylglucosamine
-
4-epimerase
- n-acetylglucosamine-1-phosphate
-
glcnac-1-p
The enzyme appears in viruses and cellular organisms
Synonyms
BLLJ_1622, hexosamine kinase, lnpB, N-acetylhexosamine 1-kinase, N-acetylhexosamine 1-phosphate kinase, N-acetylhexosamine kinase, NahK, NahKATCC15697, NahK_15697, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BLLJ_1622
hexosamine kinase
lnpB
N-acetylhexosamine 1-kinase
N-acetylhexosamine 1-phosphate kinase
NahK
NahKATCC15697
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
openâclose 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
openâclose 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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Phosphorylation
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SYSTEMATIC NAME
IUBMB Comments
ATP:N-acetyl-D-hexosamine 1-phosphotransferase
This enzyme is involved in the lacto-N-biose I/galacto-N-biose degradation pathway in the probiotic bacterium Bifidobacterium longum. Differs from EC 2.7.1.157, N-acetylgalactosamine kinase, as it can phosphorylate both N-acetylgalactosamine and N-acetylglucosamine at similar rates. Also has some activity with N-acetyl-D-mannosamine, D-talose and D-mannose as substrate. ATP can be replaced by GTP or ITP but with decreased enzyme activity. Requires a divalent cation, with Mg2+ resulting in by far the greatest stimulation of enzyme activity.
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CAS REGISTRY NUMBER
COMMENTARY
959459-09-7
protein sequence
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 2-(acetylamino)-2-deoxy-D-allopyranose
ADP + 2-(acetylamino)-2-deoxy-D-allopyranose 1-phosphate
22% phosphorylation yield
-
-
?
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 + 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-mannosamine
ADP + alpha-D-mannosamine 1-phosphate
-
-
-
?
ATP + D-talose
?
phosphorylation at 3% of the activity with N-acetylglucosamine
-
-
?
ATP + N-acetyl-D-mannosamine
?
phosphorylation at 15% of the activity with N-acetylglucosamine
-
-
?
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-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
-
-
?
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
?
-
-
substrate binding structures, overview
-
-
?
additional information
?
-
-
substrate binding structures, overview
-
-
?
additional information
?
-
GlcNAc/GalNAc is phosphorylated to GlcNAc1P/GalNAc1P by N-acetylhexosamine 1-kinase (NahK), which acts on either
-
-
-
additional information
?
-
GlcNAc/GalNAc is phosphorylated to GlcNAc1P/GalNAc1P by N-acetylhexosamine 1-kinase (NahK), which acts on either
-
-
-
additional information
?
-
GlcNAc/GalNAc is phosphorylated to GlcNAc1P/GalNAc1P by N-acetylhexosamine 1-kinase (NahK), which acts on either
-
-
-
additional information
?
-
GlcNAc/GalNAc is phosphorylated to GlcNAc1P/GalNAc1P by N-acetylhexosamine 1-kinase (NahK), which acts on either
-
-
-
additional information
?
-
GlcNAc/GalNAc is phosphorylated to GlcNAc1P/GalNAc1P by N-acetylhexosamine 1-kinase (NahK), which acts on either
-
-
-
additional information
?
-
GlcNAc/GalNAc is phosphorylated to GlcNAc1P/GalNAc1P by N-acetylhexosamine 1-kinase (NahK), which acts on either
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
lacto-N-biose I/galacto-N-biose metabolic pathway
-
-
?
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
lacto-N-biose I/galacto-N-biose metabolic pathway
-
-
?
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-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
-
-
-
?
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-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
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
additional information
Mg2+
requires a divalent cation, with Mg2+ resulting in the greatest stimulation of enzyme activity
Mg2+
requirement of the second magnesium ion, the enzyme has two magnesium binding sites, Mg1 and Mg2, structure overview
Mg2+
required for catalysis, optimum for wild-type enzyme is 5 mM, for mutants H31A and F247A 10 mM
Mg2+
required, bindin gstructure and analysis, one Mg2+ per subunit
additional information
-
divalent cation required for activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
isopropyl-1-thio-beta-D-galactoside
induction of protein expression at a final concentration of 0.5 mM
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.005
ATP
pH 8.0, 37°C, recombinant mutant K210A, at 5.0 mM MgCl2
0.038
ATP
pH 8.0, 37°C, recombinant mutant N213A at 50 mM MgCl2
0.08
ATP
-
cosubstrate N-acetyl-alpha-D-galactosamine, pH 8.0, 37°C
0.1
ATP
-
cosubstrate N-acetyl-alpha-D-glucosamine, pH 8.0, 37°C
0.1
ATP
pH 8.0, 37°C, recombinant wild-type enzyme, at 5.0 mM MgCl2
0.172
ATP
cosubstrate: N-acetyl-alpha-D-glucosamine, pH 8.5, 30°C
0.9
ATP
pH 8.0, 37°C, recombinant mutant N213A at 5.0 mM MgCl2
0.35
N-acetyl-D-glucosamine
pH 8.0, 37°C, recombinant mutant K210A, at 5.0 mM MgCl2
1.8
N-acetyl-D-glucosamine
pH 8.0, 37°C, recombinant wild-type enzyme, at 5.0 mM MgCl2
2.5
N-acetyl-D-glucosamine
pH 8.0, 37°C, recombinant mutant N213A at 5.0 mM MgCl2
3.14
N-acetyl-D-glucosamine
pH 8.0, 37°C, recombinant mutant N213A at 50 mM MgCl2
additional information
additional information
summary of ITC analysis of wild-type NahK and mutants
-
additional information
additional information
-
summary of ITC analysis of wild-type NahK and mutants
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.12
ATP
pH 8.0, 37°C, recombinant mutant K210A, at 5.0 mM MgCl2
0.38
ATP
-
cosubstrate N-acetyl-alpha-D-galactosamine, pH 8.0, 37°C
1.1
ATP
-
cosubstrate N-acetyl-alpha-D-glucosamine, pH 8.0, 37°C
6.4
ATP
pH 8.0, 37°C, recombinant mutant N213A at 5.0 mM MgCl2
16.3
ATP
pH 8.0, 37°C, recombinant wild-type enzyme, at 5.0 mM MgCl2
0.11
N-acetyl-D-glucosamine
pH 8.0, 37°C, recombinant mutant K210A, at 5.0 mM MgCl2
5.9
N-acetyl-D-glucosamine
pH 8.0, 37°C, recombinant mutant N213A at 5.0 mM MgCl2
9.9
N-acetyl-D-glucosamine
pH 8.0, 37°C, recombinant wild-type enzyme, at 5.0 mM MgCl2
13.6
N-acetyl-D-glucosamine
pH 8.0, 37°C, recombinant mutant N213A at 50 mM MgCl2
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.8
ATP
-
cosubstrate N-acetyl-alpha-D-galactosamine, pH 8.0, 37°C
11
ATP
-
cosubstrate N-acetyl-alpha-D-glucosamine, pH 8.0, 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
Incubation of 4 microM LnpB protein with 10 mM N-acetyl-alpha-D-glucosamine 6-sulfate in 0.1 M MOPS buffer (pH 7.5) at 30°C for 30 min shows that the protein have no hydrolytic activity
additional information
-
Incubation of 4 microM LnpB protein with 10 mM N-acetyl-alpha-D-glucosamine 6-sulfate in 0.1 M MOPS buffer (pH 7.5) at 30°C for 30 min shows that the protein have no hydrolytic activity
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 8
8.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
-
the enzyme belongs to the sugar kinase-Hsp70-actin superfamily
evolution
the enzyme belongs to the sugar kinase-Hsp70-actin superfamily
evolution
-
the enzyme belongs to the sugar kinase-Hsp70-actin superfamily
-
evolution
-
the enzyme belongs to the sugar kinase-Hsp70-actin superfamily
-
metabolism
-
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
-
the enzyme is involved in the lacto-N-biose I (LNB) metabolic pathway catalyzing the phosphorylation of GlcNAc/GalNAc to GlcNAc1P/GalNAc1P , 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
-
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
-
the enzyme is involved in the lacto-N-biose I (LNB) metabolic pathway catalyzing the phosphorylation of GlcNAc/GalNAc to GlcNAc1P/GalNAc1P , 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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
Show AA Sequence and Transmembrane Helices (192 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
42500
42500
-
gel-filtration and analytical ultracentrifugation
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
additional information
monomer
-
1 * 42500, SDS-PAGE, enzyme NahK is a monomer in solution, and its polypeptide folds in a crescent-like architecture subdivided into two domains by a deep cleft. The N- and C-terminal domains of NahK comprise residues 1-103 and 117-359, respectively. The N-terminal domain contains a characteristic five-stranded antiparallel beta-sheet flanked by two alpha-helices
monomer
-
1 * 42500, SDS-PAGE, enzyme NahK is a monomer in solution, and its polypeptide folds in a crescent-like architecture subdivided into two domains by a deep cleft. The N- and C-terminal domains of NahK comprise residues 1-103 and 117-359, respectively. The N-terminal domain contains a characteristic five-stranded antiparallel beta-sheet flanked by two alpha-helices
-
additional information
enzyme NahK is a monomer in solution, and its polypeptide folds in a crescent-like architecture subdivided into two domains by a deep cleft. The N- and C-terminal domains of NahK comprise residues 1-103 and 117-359, respectively. The N-terminal domain contains a characteristic five-stranded antiparallel beta-sheet flanked by two alpha-helices
additional information
-
enzyme NahK is a monomer in solution, and its polypeptide folds in a crescent-like architecture subdivided into two domains by a deep cleft. The N- and C-terminal domains of NahK comprise residues 1-103 and 117-359, respectively. The N-terminal domain contains a characteristic five-stranded antiparallel beta-sheet flanked by two alpha-helices
additional information
-
enzyme NahK is a monomer in solution, and its polypeptide folds in a crescent-like architecture subdivided into two domains by a deep cleft. The N- and C-terminal domains of NahK comprise residues 1-103 and 117-359, respectively. The N-terminal domain contains a characteristic five-stranded antiparallel beta-sheet flanked by two alpha-helices
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged enzyme in complex with substrates GalNAc, GlcNAc-1P, GlcNAc/AMPPNP (a nonhydrolyzable ATP analogue) and GlcNAc-1P/ADP, hanging drop vapour diffusion method, pre-incubation of SeMet-substituted/wild-type NahK with GlcNAc (20fold excess), GalNAc (20fold excess) or GlcNAc-1P (10fold excess), and mixing of 20 mg/ml protein in 50 mM HEPES, pH 7.5, with a crystallization solution containing 20% w/v PEG 3350, 0.1 M Bis-Tris, pH 5.5, crystals of NahK-GlcNAc-AMPPNP are obtained by soaking NahK-GlcNAc crystals with 10 mM AMPPNP and 20 mM MgCl2 for 15 min, or the crystals of NahK-GlcNAc-1P-ADP by soaking NahK-GlcNAc-1P crystals with 5 mM ADP and 10 mM MgCl2 for 30 min, crystallization time is 10-14 days, 20°C, X-ray diffraction structure determination and analysis at 1.72-2.15 A resolution, molecular replacement method, modelling
purified recombinant wild-type enzyme in apoform, or SeMet-labeled NahK complexed with ATP, sitting drop vapor diffusion method, mixing of 500 nl protein solution containing 25 mg/mL NahK and with or without 10 mM ATP with an equal volume of reservoir solution containing 0.2 M magnesium acetate, 0.1 M sodium cacodylate, pH 6.5, and 20% PEG 8000, for ADP complex crystals, 10 mM ADP is used instead of ATP, 20°C, X-ray diffraction structure determination and analysis at 1.80-2.05 A resolution
purified recombinant His-tagged enzyme in complex with substrates GlcNAc, and GlcNAc/AMPPNP (a nonhydrolyzable ATP analogue), hanging drop vapour diffusion method, mixing of 20 mg/ml protein in 50 mM HEPES, pH 7.5, with crystallization solution containing 1.5 M Li2SO4, 0.1 M sodium acetate, pH 5.5, 2 days, crystals of the NahKATCC15697-GlcNAc-AMPPNP complex are obtained by soaking NahK-GlcNAc complex crystals with 5 mM AMPPNP and 10 mM MgCl2 for 1.5 h, 20°C, X-ray diffraction structure determination and analysis at 1.47-1.90 A resolution, molecular replacement method, modelling
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
K210A
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
-
D228A
-
site-directed mutagenesis, the mutant shows altered activity and kinetics compared to the wild-type enzyme
-
K210A
-
site-directed mutagenesis, the mutant shows altered activity and kinetics compared to the wild-type enzyme
-
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
-
R306E
-
site-directed mutagenesis, the mutant shows highly reduced activity but unaltered 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 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
-
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
-
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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9.5
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
loses half of enzyme activity during incubation for 30 min at 50°C in 0.1 M Tris buffer (pH 8.5)
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His6-tagged wild-type and SeMet-labeled NahK residues 1-359 enzymes from Escherichia coli by nickel affinity chromatography and gel filtration
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
The transformant is cultivated and protein expression is induced by the addition of isopropyl-1-thio-beta-D-galactoside. The cells are harvested by centrifugation and sonicated. Cell debris is removed by centrifugation and enzyme is purified on an Ni-nitrilotriacetic acid agarose gel.
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
-
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Escherichia coli strains select96 and BL21(DE3) are used as hosts for cloning and expression.
expression in Escherichia coli
gene lnpB, recombinant expression of C-terminally His6-tagged NahK residues 1-359 in Escherichia coli strain BL21 CodonPlus (DE3)-RIL, expression of the (SeMet)-labeled protein in Escherichia coli strain B834 (DE3)
gene lnpB, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene lnpB, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
-
gene lnpB, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
an N-acetylhexosamine 1-kinase from Bifidobacterium infantis (NahK_15697), a guanosine 5'-diphosphate (GDP)-mannose pyrophosphorylase from Pyrococcus furiosus (PFManC), and an Escherichia coli inorganic pyrophosphatase (EcPpA) are used efficiently for a one-pot three enzyme synthesis of GDP-mannose, GDP-glucose, their derivatives, and GDP-talose from simple monosaccharides and derivatives in preparative scale
synthesis
-
the enzyme is used in the chemoenzymatic synthesis of UDP-GlcNAc and UDP-GlcNTFA attempted by three recombinant enzymes in a fed batch system, overview. The process can be used for the development of an efficient scalable process for the supply of UDP-monosaccharide donors for oligosaccharide synthesis
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
-
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